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ATP + H2O
ADP + phosphate
-
dynamin also has ATPase activity
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?
GTP + H2O
GDP + phosphate
additional information
?
-
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
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?
GTP + H2O
GDP + phosphate
-
-
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?
GTP + H2O
GDP + phosphate
involved in vesicle scission
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?
GTP + H2O
GDP + phosphate
-
-
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?
GTP + H2O
GDP + phosphate
-
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?
GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
-
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?
GTP + H2O
GDP + phosphate
-
dynamin self-association is not sufficient condition for the expression of maximal GTPase activity, dynamin molecules must be in proper conformation or orientation if they are to form an active oligomer
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?
GTP + H2O
GDP + phosphate
-
highly specific for GTP
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?
GTP + H2O
GDP + phosphate
-
critical step in fission of coated pits to form coated vesicles
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?
GTP + H2O
GDP + phosphate
-
enzyme is essential for budding clathrin-coated vesicles from the plasma membrane
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?
GTP + H2O
GDP + phosphate
-
plays an essential role in synaptic vesicle recycling
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?
GTP + H2O
GDP + phosphate
-
plays an essential role in synaptic vesicle recycling
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?
GTP + H2O
GDP + phosphate
-
involved in clathrin-mediated endocytosis and other vesicular trafficking processes, dynamin has a mechanochemical function in vesicle scission, the GTPase activity of dynamin and the resulting conformation change are essential for endocytosis
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?
GTP + H2O
GDP + phosphate
-
involved in membrane vesiculation
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?
GTP + H2O
GDP + phosphate
-
GTP hydrolysis results in conformational changes in dynamin bound to lipid nanotubes
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?
GTP + H2O
GDP + phosphate
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?
GTP + H2O
GDP + phosphate
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-
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?
GTP + H2O
GDP + phosphate
-
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?
GTP + H2O
GDP + phosphate
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?
GTP + H2O
GDP + phosphate
-
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?
GTP + H2O
GDP + phosphate
-
enzyme plays an important role in the recycling of synaptic vesicles. Different dynamin domains contribute to axonal transport and the sequestration of a pool of dynamin molecules in synaptic cytosol
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?
GTP + H2O
GDP + phosphate
-
the large GTPase dynamin is involved in membrane tubulation and vesiculation, it associates with the spindle midzone and is required for cytokinesis
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?
GTP + H2O
GDP + phosphate
-
DYN-1 mediates the signaling of the CED-1 pathway by organizing an intracellular vesicle pool and promoting vesicle delivery to phagocytic cups and phagosomes to support pseudopod extension and apoptotic cell degradation
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?
GTP + H2O
GDP + phosphate
involved in vesicle scission
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-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
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?
GTP + H2O
GDP + phosphate
-
-
-
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?
GTP + H2O
GDP + phosphate
-
-
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?
GTP + H2O
GDP + phosphate
involved in vesicle scission
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?
GTP + H2O
GDP + phosphate
Drosophila sp. (in: flies)
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?
GTP + H2O
GDP + phosphate
Drosophila sp. (in: flies)
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-
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?
GTP + H2O
GDP + phosphate
Drosophila sp. (in: flies)
-
dynein light chain 1 regulates dynamin-mediated F-actin assembly during sperm individualization in Drosophila
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?
GTP + H2O
GDP + phosphate
-
-
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?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
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?
GTP + H2O
GDP + phosphate
-
-
657723, 659560, 668369, 669471, 669573, 669581, 670364, 697236, 697237, 700294, 719766 -
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?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
regulates late events in clathrin-coated vescicle formation, GTP hydrolysis is required for vesicle detachment, a concerted conformational change resulting from coordinated GTP hydrolysis by the dynamin oligomer might by sufficient to generate force
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?
GTP + H2O
GDP + phosphate
-
dynamin is a regulatory GTPase in endocytosis of the glucose transporter GLUT4
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?
GTP + H2O
GDP + phosphate
-
critical step in fission of coated pits to form coated vesicles
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?
GTP + H2O
GDP + phosphate
-
plays an essential role in synaptic vesicle recycling
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?
GTP + H2O
GDP + phosphate
-
dynamin 2 can act as a signal transducing GTPase affecting transcriptional regulation
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?
GTP + H2O
GDP + phosphate
-
dynamin plays a role in clathrin-mediated endocytosis, it plays a role in vesicle budding, dynamin is specifically required for endocytic coated vesicle formation and its GTP binding and hydrolysis activities are required to form constricted coated pits and, subsequently, for coated vesicle budding
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?
GTP + H2O
GDP + phosphate
-
GTP hydrolysis is required for clathrin-mediated endocytosis in vivo
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?
GTP + H2O
GDP + phosphate
-
plays a role in clathrin-mediated endocytosis, the endocytically active GTPase dynamin plays a role in the regulation of Trypanosoma cruzi invasion of nonphagocytic cells, dynamin acts as a limiting factor in allowing trypomastigotes to invade host cells
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?
GTP + H2O
GDP + phosphate
-
conformational changes in the active site accompany self-assembly, dynamin domain structure, Thr-65 plays an important role in catalysis, Thr-141 has roles in both GTP binding and hydrolysis
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?
GTP + H2O
GDP + phosphate
-
dynamin is required for the clathrin-independent endocytosis of gamma cytokine receptor
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?
GTP + H2O
GDP + phosphate
-
dynamin-2 facilitates fas protein translocation from the Golgi apparatus via the trans-Golgi network to the cell surface
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?
GTP + H2O
GDP + phosphate
-
GTPase dynamin is required for budding of clathrin-coated vesicles from plasma membrane. Auxilin cooperates with dynamin during vesicle formation. DEscription of four assays that monitor auxilin-dynamin interactions
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?
GTP + H2O
GDP + phosphate
-
involved in vesicle scission
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?
GTP + H2O
GDP + phosphate
-
the dynein/dynactin complex plays an unexpected role in the regulation of mitochondrial morphology in living cells, by controlling the recruitment of Drp1 to these organelles
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?
GTP + H2O
GDP + phosphate
the recombinant GTPase-GTPase effector domain fusion protein of human Drp1 shows GTPase activity
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?
GTP + H2O
GDP + phosphate
-
-
-
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?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
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-
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?
GTP + H2O
GDP + phosphate
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-
-
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?
GTP + H2O
GDP + phosphate
-
NtDRP3 can bind to and bundle both microtubules and actin filaments in vitro
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?
GTP + H2O
GDP + phosphate
-
-
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?
GTP + H2O
GDP + phosphate
-
-
-
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?
GTP + H2O
GDP + phosphate
-
-
-
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ir
GTP + H2O
GDP + phosphate
-
GTPase is required for endocytosis
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?
GTP + H2O
GDP + phosphate
-
the enzyme is involved in membrane constriction and fission during receptor-mediated endocytosis and synaptic vesicle endocytosis
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?
GTP + H2O
GDP + phosphate
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
regulates late events in clathrin-coated vescicle formation, GTP hydrolysis is required for vesicle detachment, a concerted conformational change resulting from coordinated GTP hydrolysis by the dynamin oligomer might by sufficient to generate force
-
?
GTP + H2O
GDP + phosphate
-
dynamin 2 can act as a signal transducing GTPase affecting transcriptional regulation
-
?
GTP + H2O
GDP + phosphate
-
enzyme is involved in endocytosis
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?
GTP + H2O
GDP + phosphate
-
enzyme is involved in endocytosis
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?
GTP + H2O
GDP + phosphate
-
enzyme is involved in endocytosis
-
?
GTP + H2O
GDP + phosphate
-
dynamin I phosphorylation by protein kinase C and dephosphorylation by calcineurin serve as molecular switches to control nerve terminal vesicle recycling
-
?
GTP + H2O
GDP + phosphate
-
through its ability to oligomerize, dynamin appears to form a structural collar around the neck of caveolae that hydrolyzes GTP to mediate internalization via the fission of caveolae from the plasma membrane to form free transport vesicles
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?
GTP + H2O
GDP + phosphate
-
dynamin forms a Src kinase-sensitive complex with Cbl and regulates podosomes and osteoclast activity
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-
?
GTP + H2O
GDP + phosphate
-
GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
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?
GTP + H2O
GDP + phosphate
-
the role of dynamin in the assembly and function of podosomes and invadopodia
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?
GTP + H2O
GDP + phosphate
-
-
-
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?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
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?
additional information
?
-
-
DRP5 is involved in cytokinesis
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?
additional information
?
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-
dynamin is a midbody protein associated with membrane remodelling that is also required for cytokinesis. Dynamin may also function as a link between the plasma membrane and actin filaments through interactions with proteins like Abp1, profilin, or cortacin. Alternatively, dynamin assembled on plasma membranes can act as structural component that organizes and stabilizes acti filaments at the furrow membrane, therefore being a platform from which the contractile ring forms.
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-
?
additional information
?
-
dynamin is a midbody protein associated with membrane remodelling that is also required for cytokinesis. Dynamin may also function as a link between the plasma membrane and actin filaments through interactions with proteins like Abp1, profilin, or cortacin. Alternatively, dynamin assembled on plasma membranes can act as structural component that organizes and stabilizes acti filaments at the furrow membrane, therefore being a platform from which the contractile ring forms.
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?
additional information
?
-
dynamin regulates the focal exocytosis of endomembranes at the site of phagocytosis and accumulates on the nascent phagosome in a complex with inactive Vps34 and Rab5-GDP
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?
additional information
?
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-
dynamin regulates the focal exocytosis of endomembranes at the site of phagocytosis and accumulates on the nascent phagosome in a complex with inactive Vps34 and Rab5-GDP
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?
additional information
?
-
the enzyme mediates homotypic membrane fusion of the endoplasmic reticulum, wild-type scSey1p shows efficient fusion in the presence of GTP and Mg2+. No fusion is seen with GDP or in the absence of Mg2+. Addition of GMP-PNP caused moderate but reproducible fusion. Nucleotide-dependent conformational changes of Sey1p, nucleotide binding structure, detailed overview
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?
additional information
?
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-
the enzyme mediates homotypic membrane fusion of the endoplasmic reticulum, wild-type scSey1p shows efficient fusion in the presence of GTP and Mg2+. No fusion is seen with GDP or in the absence of Mg2+. Addition of GMP-PNP caused moderate but reproducible fusion. Nucleotide-dependent conformational changes of Sey1p, nucleotide binding structure, detailed overview
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-
?
additional information
?
-
-
dynamin is a midbody protein associated with membrane remodelling that is also required for cytokinesis. Dynamin may also function as a link between the plasma membrane and actin filaments through interactions with proteins like Abp1, profilin, or cortacin. Alternatively, dynamin assembled on plasma membranes can act as structural component that organizes and stabilizes acti filaments at the furrow membrane, therefore being a platform from which the contractile ring forms.
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?
additional information
?
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the dynamin isoform DlpB is involved in cytokinesis
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?
additional information
?
-
the dynamin isoform DlpB is involved in cytokinesis
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?
additional information
?
-
the dynamin isoform DlpB is involved in cytokinesis
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?
additional information
?
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the dynamin isoform DlpB is involved in cytokinesis
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?
additional information
?
-
the dynamin isoform DlpC is involved in cytokinesis
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?
additional information
?
-
the dynamin isoform DlpC is involved in cytokinesis
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?
additional information
?
-
the dynamin isoform DlpC is involved in cytokinesis
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?
additional information
?
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-
the dynamin isoform DlpC is involved in cytokinesis
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?
additional information
?
-
the dynamin isoforms DlpA is involved in cytokinesis
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?
additional information
?
-
the dynamin isoforms DlpA is involved in cytokinesis
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?
additional information
?
-
the dynamin isoforms DlpA is involved in cytokinesis
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?
additional information
?
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-
the dynamin isoforms DlpA is involved in cytokinesis
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?
additional information
?
-
-
dynamin is a midbody protein associated with membrane remodelling that is also required for cytokinesis. Dynamin may also function as a link between the plasma membrane and actin filaments through interactions with proteins like Abp1, profilin, or cortacin. Alternatively, dynamin assembled on plasma membranes can act as structural component that organizes and stabilizes acti filaments at the furrow membrane, therefore being a platform from which the contractile ring forms.
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?
additional information
?
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feline infectious peritonitis virus enters monocytes through a clathrin- and caveolae-independent pathway that strongly depends on dynamin
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?
additional information
?
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dynamin 2 regulates granule exocytosis during natural killer cell-mediated cytotoxicity
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?
additional information
?
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dynamin assembles at the necks of budded vesicles in vivo and functions in membrane fission, dynamin alone is sufficient to catalyze membrane fission and vesiculation from a fluid membrane reservoir
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-
?
additional information
?
-
-
dynamin is critically involved in membrane fission during endocytosis, dynamin acts as a catalyst of membrane remodelling bringing membrane nanotubes to the point of spontaneous fission via creation of regulated curvature constraints
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?
additional information
?
-
-
dynamin is involved in histamine H2 receptor endocytosis
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?
additional information
?
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MUC1-CT endocytosis is dynamin dependent
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?
additional information
?
-
Pichinde virus infection of host cells is dependent on cellular dynamin 2
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?
additional information
?
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-
sorting nexin 9-induced tubulation is antagonized dynamin 2, sorting nexin 9 binds dynamin 2 and N-WASP, and this interaction regulates the tubulating activity of SNX9 in conjunction with the actin cytoskeleton
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?
additional information
?
-
the complete HIV-1 particle transfer from the effector cells to target primary T CD4+ lymphocytes requires the presence of dynamin
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?
additional information
?
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-
the PH domain binds acidic phospholipids in the cytosolic leaflet of the plasma membrane, and phosphatidylinositol-4,5-bisphosphate in particular, via a positively charged surface at the foot of the dynamin hairpin. The membrane interaction is strengthened by charge-dependent association with other negatively charged phospholipids and by avidity afforded by dynamin polymerization
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?
additional information
?
-
MxA recognizes Thogoto virus nucleocapsid proteins independently of nucleotide binding, while both nucleotide binding and hydrolysis are required for the antiviral activity against Thogoto, influenza, and La Crosse viruses. GTP binding facilitates formation of stable MxA assemblies associated with endoplasmic reticulum membranes, whereas nucleotide hydrolysis promotes dynamic redistribution of MxAfrom cellular membranes to viral targets
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?
additional information
?
-
-
MxA recognizes Thogoto virus nucleocapsid proteins independently of nucleotide binding, while both nucleotide binding and hydrolysis are required for the antiviral activity against Thogoto, influenza, and La Crosse viruses. GTP binding facilitates formation of stable MxA assemblies associated with endoplasmic reticulum membranes, whereas nucleotide hydrolysis promotes dynamic redistribution of MxAfrom cellular membranes to viral targets
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?
additional information
?
-
enzyme-nucleotide binding studies, overview
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?
additional information
?
-
-
enzyme-nucleotide binding studies, overview
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?
additional information
?
-
analysis of the enzyme in GDP-bound state, the switch I region moves away from the active site after GTP hydrolysis and release of inorganic phosphate
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-
-
additional information
?
-
behaviour analysis of the enzyme in nucleotide and/or membrane binding, detailed overview. Nucleotide-dependent changes in PHD-membrane interactions and the non-hydrolyzable GTP analogue, GMPPCP (beta-gamma-methyleneguanosine 5'-triphosphate)-dependent loosening of the scaffold. Ability of wild-type Dyn1, and mutant Dyn1CC and Dyn1Closed to catalyze membrane fission and vesicle release from SUPER templates, overview
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-
-
additional information
?
-
dynamin 2 is required for actin assembly in phagocytosis in Sertoli cells, dynamin 2 is involved in PI(4,5)P2-induced actin polymerisation during phagocytosis
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?
additional information
?
-
-
dynamin is required for budding of clathrin-coated vesicles from the plasma membrane, functional dynamin is required for muramyl dipeptide-induced internalization and signaling
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-
?
additional information
?
-
-
the PH domain binds acidic phospholipids in the cytosolic leaflet of the plasma membrane, and phosphatidylinositol-4,5-bisphosphate in particular, via a positively charged surface at the foot of the dynamin hairpin. The membrane interaction is strengthened by charge-dependent association with other negatively charged phospholipids and by avidity afforded by dynamin polymerization
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-
?
additional information
?
-
-
in addition to the GTPase domain, neurolastin also has an E3 ubiquitin ligase domain, the enzyme shows E3 ligase activity in an in vitro ubiquitination assay
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-
?
additional information
?
-
neurolastin exhibits both GTPase and E3 ligase activities
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-
-
additional information
?
-
-
dynamin interacts with the Gigantea gene in vivo
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-
?
additional information
?
-
-
Arp2/3-mediated actin polymerization regulates the accessibility of cortactin to dynamin 2 and implies a novel mechanism by which cortactin and dynamin drive the fission of clathrin-coated pits in an actin polymerization dependent manner
-
-
?
additional information
?
-
dynamin 2 is specifically required for clathrin-mediated endocytosis in fibroblastoid cells, p75 export from the Golgi, and PDGF-stimulated macropinocytosis and cytokinesis, but not for other endocytic pathways, clathrin-mediated endocytosis and p75 exocytosis are efficiently rescued by reintroduction of dynamin 2, but not dynamin 1, suggesting that these two isoforms function differentially in vesicular trafficking in nonneuronal cells. Both isoforms rescue macropinocytosis and cytokinesis, suggesting that dynamin function in these processes may be mechanistically distinct from its role in clathrin-mediated endocytosis. Although all four dynamin 2 splice variants can equally restore clathrin-mediated endocytosis, dynamin 2ba and dynamin 2bb are more effective at restoring p75 exocytosis.
-
-
?
additional information
?
-
dynamin 2 is specifically required for clathrin-mediated endocytosis in fibroblastoid cells, p75 export from the Golgi, and PDGF-stimulated macropinocytosis and cytokinesis, but not for other endocytic pathways, clathrin-mediated endocytosis and p75 exocytosis are efficiently rescued by reintroduction of dynamin 2, but not dynamin 1, suggesting that these two isoforms function differentially in vesicular trafficking in nonneuronal cells. Both isoforms rescue macropinocytosis and cytokinesis, suggesting that dynamin function in these processes may be mechanistically distinct from its role in clathrin-mediated endocytosis. Although all four dynamin 2 splice variants can equally restore clathrin-mediated endocytosis, dynamin 2ba and dynamin 2bb are more effective at restoring p75 exocytosis.
-
-
?
additional information
?
-
dynamin 2 is specifically required for clathrin-mediated endocytosis in fibroblastoid cells, p75 export from the Golgi, and PDGF-stimulated macropinocytosis and cytokinesis, but not for other endocytic pathways, clathrin-mediated endocytosis and p75 exocytosis are efficiently rescued by reintroduction of dynamin 2, but not dynamin 1, suggesting that these two isoforms function differentially in vesicular trafficking in nonneuronal cells. Both isoforms rescue macropinocytosis and cytokinesis, suggesting that dynamin function in these processes may be mechanistically distinct from its role in clathrin-mediated endocytosis. Although all four dynamin 2 splice variants can equally restore clathrin-mediated endocytosis, dynamin 2ba and dynamin 2bb are more effective at restoring p75 exocytosis.
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-
?
additional information
?
-
-
dynamin is a binding partner of histamine H2 receptor, agonist-induced internalization of histamine H2 receptor and activation of extracellular signal-regulated kinases are dynamin-dependent. Dynamin is not involved in adenylate cyclase activation or desensitisation.
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?
additional information
?
-
LOX-1 internalisation is regulated by dynamin-2
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-
?
additional information
?
-
-
the PH domain binds acidic phospholipids in the cytosolic leaflet of the plasma membrane, and phosphatidylinositol-4,5-bisphosphate in particular, via a positively charged surface at the foot of the dynamin hairpin. The membrane interaction is strengthened by charge-dependent association with other negatively charged phospholipids and by avidity afforded by dynamin polymerization
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?
additional information
?
-
Drp6 does not participate in nuclear protein import
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?
additional information
?
-
-
DrpB is required during replication to generate vesicles for the regulated secretory pathway that form the unique secretory organelles, DrpB is required for the transport of secretory proteins
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GTP + H2O
GDP + phosphate
additional information
?
-
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
involved in vesicle scission
-
-
?
GTP + H2O
GDP + phosphate
-
critical step in fission of coated pits to form coated vesicles
-
?
GTP + H2O
GDP + phosphate
-
enzyme is essential for budding clathrin-coated vesicles from the plasma membrane
-
?
GTP + H2O
GDP + phosphate
-
plays an essential role in synaptic vesicle recycling
-
?
GTP + H2O
GDP + phosphate
-
plays an essential role in synaptic vesicle recycling
-
?
GTP + H2O
GDP + phosphate
-
involved in clathrin-mediated endocytosis and other vesicular trafficking processes, dynamin has a mechanochemical function in vesicle scission, the GTPase activity of dynamin and the resulting conformation change are essential for endocytosis
-
-
?
GTP + H2O
GDP + phosphate
-
involved in membrane vesiculation
-
-
?
GTP + H2O
GDP + phosphate
-
enzyme plays an important role in the recycling of synaptic vesicles. Different dynamin domains contribute to axonal transport and the sequestration of a pool of dynamin molecules in synaptic cytosol
-
?
GTP + H2O
GDP + phosphate
-
the large GTPase dynamin is involved in membrane tubulation and vesiculation, it associates with the spindle midzone and is required for cytokinesis
-
-
?
GTP + H2O
GDP + phosphate
-
DYN-1 mediates the signaling of the CED-1 pathway by organizing an intracellular vesicle pool and promoting vesicle delivery to phagocytic cups and phagosomes to support pseudopod extension and apoptotic cell degradation
-
-
?
GTP + H2O
GDP + phosphate
involved in vesicle scission
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
involved in vesicle scission
-
-
?
GTP + H2O
GDP + phosphate
Drosophila sp. (in: flies)
-
-
-
-
?
GTP + H2O
GDP + phosphate
Drosophila sp. (in: flies)
-
dynein light chain 1 regulates dynamin-mediated F-actin assembly during sperm individualization in Drosophila
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
regulates late events in clathrin-coated vescicle formation, GTP hydrolysis is required for vesicle detachment, a concerted conformational change resulting from coordinated GTP hydrolysis by the dynamin oligomer might by sufficient to generate force
-
?
GTP + H2O
GDP + phosphate
-
dynamin is a regulatory GTPase in endocytosis of the glucose transporter GLUT4
-
?
GTP + H2O
GDP + phosphate
-
critical step in fission of coated pits to form coated vesicles
-
?
GTP + H2O
GDP + phosphate
-
plays an essential role in synaptic vesicle recycling
-
?
GTP + H2O
GDP + phosphate
-
dynamin 2 can act as a signal transducing GTPase affecting transcriptional regulation
-
?
GTP + H2O
GDP + phosphate
-
dynamin plays a role in clathrin-mediated endocytosis, it plays a role in vesicle budding, dynamin is specifically required for endocytic coated vesicle formation and its GTP binding and hydrolysis activities are required to form constricted coated pits and, subsequently, for coated vesicle budding
-
-
?
GTP + H2O
GDP + phosphate
-
GTP hydrolysis is required for clathrin-mediated endocytosis in vivo
-
-
?
GTP + H2O
GDP + phosphate
-
plays a role in clathrin-mediated endocytosis, the endocytically active GTPase dynamin plays a role in the regulation of Trypanosoma cruzi invasion of nonphagocytic cells, dynamin acts as a limiting factor in allowing trypomastigotes to invade host cells
-
-
?
GTP + H2O
GDP + phosphate
-
dynamin is required for the clathrin-independent endocytosis of gamma cytokine receptor
-
-
?
GTP + H2O
GDP + phosphate
-
dynamin-2 facilitates fas protein translocation from the Golgi apparatus via the trans-Golgi network to the cell surface
-
-
?
GTP + H2O
GDP + phosphate
-
GTPase dynamin is required for budding of clathrin-coated vesicles from plasma membrane. Auxilin cooperates with dynamin during vesicle formation. DEscription of four assays that monitor auxilin-dynamin interactions
-
-
?
GTP + H2O
GDP + phosphate
-
involved in vesicle scission
-
-
?
GTP + H2O
GDP + phosphate
-
the dynein/dynactin complex plays an unexpected role in the regulation of mitochondrial morphology in living cells, by controlling the recruitment of Drp1 to these organelles
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
NtDRP3 can bind to and bundle both microtubules and actin filaments in vitro
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
GTPase is required for endocytosis
-
-
?
GTP + H2O
GDP + phosphate
-
the enzyme is involved in membrane constriction and fission during receptor-mediated endocytosis and synaptic vesicle endocytosis
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
regulates late events in clathrin-coated vescicle formation, GTP hydrolysis is required for vesicle detachment, a concerted conformational change resulting from coordinated GTP hydrolysis by the dynamin oligomer might by sufficient to generate force
-
?
GTP + H2O
GDP + phosphate
-
dynamin 2 can act as a signal transducing GTPase affecting transcriptional regulation
-
?
GTP + H2O
GDP + phosphate
-
enzyme is involved in endocytosis
-
?
GTP + H2O
GDP + phosphate
-
enzyme is involved in endocytosis
-
?
GTP + H2O
GDP + phosphate
-
enzyme is involved in endocytosis
-
?
GTP + H2O
GDP + phosphate
-
dynamin I phosphorylation by protein kinase C and dephosphorylation by calcineurin serve as molecular switches to control nerve terminal vesicle recycling
-
?
GTP + H2O
GDP + phosphate
-
through its ability to oligomerize, dynamin appears to form a structural collar around the neck of caveolae that hydrolyzes GTP to mediate internalization via the fission of caveolae from the plasma membrane to form free transport vesicles
-
?
GTP + H2O
GDP + phosphate
-
dynamin forms a Src kinase-sensitive complex with Cbl and regulates podosomes and osteoclast activity
-
-
?
GTP + H2O
GDP + phosphate
-
GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
-
-
?
GTP + H2O
GDP + phosphate
-
the role of dynamin in the assembly and function of podosomes and invadopodia
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
additional information
?
-
-
DRP5 is involved in cytokinesis
-
-
?
additional information
?
-
-
dynamin is a midbody protein associated with membrane remodelling that is also required for cytokinesis. Dynamin may also function as a link between the plasma membrane and actin filaments through interactions with proteins like Abp1, profilin, or cortacin. Alternatively, dynamin assembled on plasma membranes can act as structural component that organizes and stabilizes acti filaments at the furrow membrane, therefore being a platform from which the contractile ring forms.
-
-
?
additional information
?
-
dynamin is a midbody protein associated with membrane remodelling that is also required for cytokinesis. Dynamin may also function as a link between the plasma membrane and actin filaments through interactions with proteins like Abp1, profilin, or cortacin. Alternatively, dynamin assembled on plasma membranes can act as structural component that organizes and stabilizes acti filaments at the furrow membrane, therefore being a platform from which the contractile ring forms.
-
-
?
additional information
?
-
dynamin regulates the focal exocytosis of endomembranes at the site of phagocytosis and accumulates on the nascent phagosome in a complex with inactive Vps34 and Rab5-GDP
-
-
?
additional information
?
-
-
dynamin regulates the focal exocytosis of endomembranes at the site of phagocytosis and accumulates on the nascent phagosome in a complex with inactive Vps34 and Rab5-GDP
-
-
?
additional information
?
-
-
dynamin is a midbody protein associated with membrane remodelling that is also required for cytokinesis. Dynamin may also function as a link between the plasma membrane and actin filaments through interactions with proteins like Abp1, profilin, or cortacin. Alternatively, dynamin assembled on plasma membranes can act as structural component that organizes and stabilizes acti filaments at the furrow membrane, therefore being a platform from which the contractile ring forms.
-
-
?
additional information
?
-
the dynamin isoform DlpB is involved in cytokinesis
-
-
?
additional information
?
-
the dynamin isoform DlpB is involved in cytokinesis
-
-
?
additional information
?
-
the dynamin isoform DlpB is involved in cytokinesis
-
-
?
additional information
?
-
-
the dynamin isoform DlpB is involved in cytokinesis
-
-
?
additional information
?
-
the dynamin isoform DlpC is involved in cytokinesis
-
-
?
additional information
?
-
the dynamin isoform DlpC is involved in cytokinesis
-
-
?
additional information
?
-
the dynamin isoform DlpC is involved in cytokinesis
-
-
?
additional information
?
-
-
the dynamin isoform DlpC is involved in cytokinesis
-
-
?
additional information
?
-
the dynamin isoforms DlpA is involved in cytokinesis
-
-
?
additional information
?
-
the dynamin isoforms DlpA is involved in cytokinesis
-
-
?
additional information
?
-
the dynamin isoforms DlpA is involved in cytokinesis
-
-
?
additional information
?
-
-
the dynamin isoforms DlpA is involved in cytokinesis
-
-
?
additional information
?
-
-
dynamin is a midbody protein associated with membrane remodelling that is also required for cytokinesis. Dynamin may also function as a link between the plasma membrane and actin filaments through interactions with proteins like Abp1, profilin, or cortacin. Alternatively, dynamin assembled on plasma membranes can act as structural component that organizes and stabilizes acti filaments at the furrow membrane, therefore being a platform from which the contractile ring forms.
-
-
?
additional information
?
-
-
feline infectious peritonitis virus enters monocytes through a clathrin- and caveolae-independent pathway that strongly depends on dynamin
-
-
?
additional information
?
-
-
dynamin 2 regulates granule exocytosis during natural killer cell-mediated cytotoxicity
-
-
?
additional information
?
-
-
dynamin assembles at the necks of budded vesicles in vivo and functions in membrane fission, dynamin alone is sufficient to catalyze membrane fission and vesiculation from a fluid membrane reservoir
-
-
?
additional information
?
-
-
dynamin is critically involved in membrane fission during endocytosis, dynamin acts as a catalyst of membrane remodelling bringing membrane nanotubes to the point of spontaneous fission via creation of regulated curvature constraints
-
-
?
additional information
?
-
-
dynamin is involved in histamine H2 receptor endocytosis
-
-
?
additional information
?
-
-
MUC1-CT endocytosis is dynamin dependent
-
-
?
additional information
?
-
Pichinde virus infection of host cells is dependent on cellular dynamin 2
-
-
?
additional information
?
-
-
sorting nexin 9-induced tubulation is antagonized dynamin 2, sorting nexin 9 binds dynamin 2 and N-WASP, and this interaction regulates the tubulating activity of SNX9 in conjunction with the actin cytoskeleton
-
-
?
additional information
?
-
the complete HIV-1 particle transfer from the effector cells to target primary T CD4+ lymphocytes requires the presence of dynamin
-
-
?
additional information
?
-
-
the PH domain binds acidic phospholipids in the cytosolic leaflet of the plasma membrane, and phosphatidylinositol-4,5-bisphosphate in particular, via a positively charged surface at the foot of the dynamin hairpin. The membrane interaction is strengthened by charge-dependent association with other negatively charged phospholipids and by avidity afforded by dynamin polymerization
-
-
?
additional information
?
-
MxA recognizes Thogoto virus nucleocapsid proteins independently of nucleotide binding, while both nucleotide binding and hydrolysis are required for the antiviral activity against Thogoto, influenza, and La Crosse viruses. GTP binding facilitates formation of stable MxA assemblies associated with endoplasmic reticulum membranes, whereas nucleotide hydrolysis promotes dynamic redistribution of MxAfrom cellular membranes to viral targets
-
-
?
additional information
?
-
-
MxA recognizes Thogoto virus nucleocapsid proteins independently of nucleotide binding, while both nucleotide binding and hydrolysis are required for the antiviral activity against Thogoto, influenza, and La Crosse viruses. GTP binding facilitates formation of stable MxA assemblies associated with endoplasmic reticulum membranes, whereas nucleotide hydrolysis promotes dynamic redistribution of MxAfrom cellular membranes to viral targets
-
-
?
additional information
?
-
dynamin 2 is required for actin assembly in phagocytosis in Sertoli cells, dynamin 2 is involved in PI(4,5)P2-induced actin polymerisation during phagocytosis
-
-
?
additional information
?
-
-
dynamin is required for budding of clathrin-coated vesicles from the plasma membrane, functional dynamin is required for muramyl dipeptide-induced internalization and signaling
-
-
?
additional information
?
-
-
the PH domain binds acidic phospholipids in the cytosolic leaflet of the plasma membrane, and phosphatidylinositol-4,5-bisphosphate in particular, via a positively charged surface at the foot of the dynamin hairpin. The membrane interaction is strengthened by charge-dependent association with other negatively charged phospholipids and by avidity afforded by dynamin polymerization
-
-
?
additional information
?
-
-
in addition to the GTPase domain, neurolastin also has an E3 ubiquitin ligase domain, the enzyme shows E3 ligase activity in an in vitro ubiquitination assay
-
-
?
additional information
?
-
-
dynamin interacts with the Gigantea gene in vivo
-
-
?
additional information
?
-
-
Arp2/3-mediated actin polymerization regulates the accessibility of cortactin to dynamin 2 and implies a novel mechanism by which cortactin and dynamin drive the fission of clathrin-coated pits in an actin polymerization dependent manner
-
-
?
additional information
?
-
dynamin 2 is specifically required for clathrin-mediated endocytosis in fibroblastoid cells, p75 export from the Golgi, and PDGF-stimulated macropinocytosis and cytokinesis, but not for other endocytic pathways, clathrin-mediated endocytosis and p75 exocytosis are efficiently rescued by reintroduction of dynamin 2, but not dynamin 1, suggesting that these two isoforms function differentially in vesicular trafficking in nonneuronal cells. Both isoforms rescue macropinocytosis and cytokinesis, suggesting that dynamin function in these processes may be mechanistically distinct from its role in clathrin-mediated endocytosis. Although all four dynamin 2 splice variants can equally restore clathrin-mediated endocytosis, dynamin 2ba and dynamin 2bb are more effective at restoring p75 exocytosis.
-
-
?
additional information
?
-
dynamin 2 is specifically required for clathrin-mediated endocytosis in fibroblastoid cells, p75 export from the Golgi, and PDGF-stimulated macropinocytosis and cytokinesis, but not for other endocytic pathways, clathrin-mediated endocytosis and p75 exocytosis are efficiently rescued by reintroduction of dynamin 2, but not dynamin 1, suggesting that these two isoforms function differentially in vesicular trafficking in nonneuronal cells. Both isoforms rescue macropinocytosis and cytokinesis, suggesting that dynamin function in these processes may be mechanistically distinct from its role in clathrin-mediated endocytosis. Although all four dynamin 2 splice variants can equally restore clathrin-mediated endocytosis, dynamin 2ba and dynamin 2bb are more effective at restoring p75 exocytosis.
-
-
?
additional information
?
-
dynamin 2 is specifically required for clathrin-mediated endocytosis in fibroblastoid cells, p75 export from the Golgi, and PDGF-stimulated macropinocytosis and cytokinesis, but not for other endocytic pathways, clathrin-mediated endocytosis and p75 exocytosis are efficiently rescued by reintroduction of dynamin 2, but not dynamin 1, suggesting that these two isoforms function differentially in vesicular trafficking in nonneuronal cells. Both isoforms rescue macropinocytosis and cytokinesis, suggesting that dynamin function in these processes may be mechanistically distinct from its role in clathrin-mediated endocytosis. Although all four dynamin 2 splice variants can equally restore clathrin-mediated endocytosis, dynamin 2ba and dynamin 2bb are more effective at restoring p75 exocytosis.
-
-
?
additional information
?
-
-
dynamin is a binding partner of histamine H2 receptor, agonist-induced internalization of histamine H2 receptor and activation of extracellular signal-regulated kinases are dynamin-dependent. Dynamin is not involved in adenylate cyclase activation or desensitisation.
-
-
?
additional information
?
-
LOX-1 internalisation is regulated by dynamin-2
-
-
?
additional information
?
-
-
the PH domain binds acidic phospholipids in the cytosolic leaflet of the plasma membrane, and phosphatidylinositol-4,5-bisphosphate in particular, via a positively charged surface at the foot of the dynamin hairpin. The membrane interaction is strengthened by charge-dependent association with other negatively charged phospholipids and by avidity afforded by dynamin polymerization
-
-
?
additional information
?
-
Drp6 does not participate in nuclear protein import
-
-
?
additional information
?
-
-
DrpB is required during replication to generate vesicles for the regulated secretory pathway that form the unique secretory organelles, DrpB is required for the transport of secretory proteins
-
-
?
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(1R,2R)-2-(aminomethyl)-N,N-diethyl-1-phenyl-cyclopropane-1-carboxamide
-
milnacipran
(2-chloro-6-methylpyrimidin-4-yl)butylamine
-
(2-chloro-6-methylpyrimidin-4-yl)cyclohexylamine
-
(2-chloro-6-methylpyrimidin-4-yl)cyclopropylmethylpropylamine
-
(2-chloro-6-methylpyrimidin-4-yl)decylamine
-
(2-chloro-6-methylpyrimidin-4-yl)dimethylamine
-
(2-chloro-6-methylpyrimidin-4-yl)ethylamine
-
(2-chloro-6-methylpyrimidin-4-yl)hexylamine
-
(2-chloro-6-methylpyrimidin-4-yl)octylamine
-
(2-chloro-6-methylpyrimidin-4-yl)propylamine
-
(2-chloro-6-methylpyrimidin-4-yl)tetradecylamine
-
(2E)-2-cyano-N-(3-[[(2E)-2-cyano-3-(3,4-dimethoxyphenyl)prop-2-enoyl]amino]propyl)-3-(3,4-dihydroxyphenyl)prop-2-enamide
-
-
(2E)-2-cyano-N-(3-[[(2E)-2-cyano-3-(4-hydroxyphenyl)prop-2-enoyl]amino]propyl)-3-(3,4-dihydroxyphenyl)prop-2-enamide
-
-
(2E)-2-cyano-N-(3-[[(2E)-2-cyano-3-phenylprop-2-enoyl]amino]propyl)-3-(3,4-dihydroxyphenyl)prop-2-enamide
-
-
(2E,2'E)-N,N'-(2-hydroxypropane-1,3-diyl)bis[2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enamide]
-
-
(2E,2'E)-N,N'-(2-phenoxypropane-1,3-diyl)bis[2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enamide]
-
-
(2E,2'E)-N,N'-(2-propoxypropane-1,3-diyl)bis[2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enamide]
-
-
(3S-trans)-3-((1,3-benzodioxol-5-yloxy)methyl)-4-(4-fluorophenyl)-piperidine
-
paroxetine
(4-chloro-6-methylpyrimidin-2-yl)(1-cyclopropylmethylpropyl)amine
-
(4-chloro-6-methylpyrimidin-2-yl)-dimethylamine
-
(4-chloro-6-methylpyrimidin-2-yl)butylamine
-
(4-chloro-6-methylpyrimidin-2-yl)cyclohexylamine
-
(4-chloro-6-methylpyrimidin-2-yl)decylamine
-
(4-chloro-6-methylpyrimidin-2-yl)hexylamine
-
(4-chloro-6-methylpyrimidin-2-yl)octylamine
-
(4-chloro-6-methylpyrimidin-2-yl)propylamine
-
(4-chloro-6-methylpyrimidin-2-yl)tetradecylamine
-
(5Z)-3-(prop-2-en-1-yl)-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-(2H-chromen-3-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-(3,5-dichlorobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-(4-bromobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-(biphenyl-4-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-[4-[3-(dimethylamino)propoxy]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-ethyl-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-3-benzyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-3-benzyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2H-chromen-3-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2H-chromen-3-ylmethylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2H-chromen-3-ylmethylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3,5-dichlorobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3,5-dichlorobenzylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3,5-dichlorobenzylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(4-bromobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(4-bromobenzylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(4-bromobenzylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(biphenyl-4-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(biphenyl-4-ylmethylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(biphenyl-4-ylmethylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
1,2,3,4,10,14b-hexahydro-2-methyldibenzo[c,f]pyrazino[1,2-a]azepine
-
mianserin
1-[3-(dimethylamino)propyl]-1-(4-fluorophenyl)-1,3-dihydro[2]benzofuran-5-carbonitrile
-
citalopram
10,11-dihydro-5-[3-(methylamino)propyl]-5H-dibenz[b,f]azepine
-
desipramine
2,5-bis(2-(dimethylamino)ethylamino)-1,4-benzoquinone
-
-
2,5-bis(2-(hydroxymethyl)anilino)-1,4-benzoquinone
-
-
2,5-bis(2-bromoanilino)-1,4-benzoquinone
-
-
2,5-bis(2-carboxyanilino)-1,4-benzoquinone
-
-
2,5-bis(3-bromopropylamino)-1,4-benzoquinone
-
-
2,5-bis(3-carboxyanilino)-1,4-benzoquinone
-
-
2,5-bis(3-hydroxyanilino)-1,4-benzoquinone
-
-
2,5-bis(3-methoxyanilino)-1,4-benzoquinone
-
-
2,5-bis(3-methoxypropylamino)-1,4-benzoquinone
-
-
2,5-bis(4-(hydroxymethyl)phenylamino)-1,4-benzoquinone
-
-
2,5-bis(4-carboxyanilino)-1,4-benzoquinone
-
-
2,5-bis(4-carboxybenzylamino)-1,4-benzoquinone
-
-
2,5-bis(4-hydroxyanilino)-1,4-benzoquinone
-
-
2,5-bis(4-hydroxybenzylamino)-1,4-benzoquinone
-
-
2,5-bis(4-methoxyanilino)-1,4-benzoquinone
-
-
2,5-bis(4-methoxybenzylamino)-1,4-benzoquinone
-
-
2,5-bis(hexylamino)-1,4-benzoquinone
-
-
2,5-bis(phenylamino)-1,4-benzoquinone
-
-
2,5-bis-(benzylamino)-1,4-benzoquinone
-
-
2-((8-chlorodibenzo(b,f)thiepin-10-yl)oxy)-N,N-dimethylethylamine
-
zotepine
2-(2-carboxyanilino)-1,4-naphthoquinone
-
-
2-(2-dimethylaminoethyl)-4-N-(didecylamino)-6-methylpyrimidine
-
2-(3-(hydroxymethyl)anilino)-1,4-naphthoquinone
-
-
2-(3-hydroxyanilino)-1,4-naphthoquinone
-
-
2-(4-(hydroxymethyl)anilino)-1,4-naphthoquinone
-
-
2-(4-hydroxyanilino)-1,4-naphthoquinone
-
-
2-(4-hydroxybenzylamino)-1,4-naphthoquinone
-
-
2-chloro-4-(2-dimethylaminopropylamine)-6-methylpyrimidine
-
2-chloro-5-methyl-4-(4-methylpiperazin-1-yl)pyrimidine
-
2-chloro-N-(4-methoxybenzyl)-6-methylpyrimidin-4-amine
-
2-cyano-3-(3,4-dihydroxyphenyl)acrylic acid 2-[2-cyano-3-(3,4-dihydroxyphenyl)acryloyloxy]butyl ester
-
IC50: 0.061 mM
2-cyano-3-(3,4-dihydroxyphenyl)acrylic acid 2-[2-cyano-3-(3,4-dihydroxyphenyl)acryloyloxy]ethyl ester
-
IC50: 0.042 mM
2-cyano-3-(3,4-dihydroxyphenyl)acrylic acid 2-[2-cyano-3-(3,4-dihydroxyphenyl)acryloyloxy]propyl ester
-
IC50: 0.038 mM
2-cyano-N-[2-[2-cyano-3-(3,4,5-trihydroxyphenyl)acryloylamino]ethyl]-3-(3,4,5-trihydroxyphenyl)acrylamide
-
IC50: 0.0017 mM
2-cyano-N-[2-[2-cyano-3-(3,4-dihydroxy-4-methoxyphenyl)acryloylamino]ethyl]-3-(3,4-dihydroxy-5-methoxyphenyl) acrylamide
-
IC50: 0.009 mM
2-cyano-N-[3-[2-cyano-3-(3,4,5-trihydroxyphenyl)acryloylamino]hexyl]-3-(3,4,5-trihydroxyphenyl)acrylamide
-
IC50: 0.006 mM
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxy-5-methoxy-phenyl)acryloylamino]hexyl]-3-(3,4-dihydroxy-5-methoxyphenyl)acrylamide
-
IC50: 0.08 mM
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxy-5-methoxy-phenyl)acryloylamino]pentyl]-3-(3,4-dihydroxy-5-methoxyphenyl)acrylamide
-
IC50: 0.008 mM
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxy-5-methoxyphenyl)acryloylamino]butyl]-3-(3,4-dihydroxy-5-methoxyphenyl)acrylamide
-
IC50: 0.008 mM
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxy-5-methoxyphenyl)acryloylamino]propyl]-3-(3,4-dihydroxy-5-meth-oxyphenyl)acrylamide
-
IC50: 0.005 mM
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxyphenyl)acryloylamino]-2-hydroxypropyl]-3-(3,4-dihydroxyphenyl)acrylamide
-
IC50: 0.0051 mM
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxyphenyl)acryloylamino]-propyl] 3-[4-(3-trifluoromethyl-3H-diazirin-3-yl)phenyl]acrylamide
-
-
3-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-ylidene)-N-methyl-1-propanamine
-
nortriptyline
3-(2-chloro-10H-phenothiazin-10-yl)-N,N-dimethyl-propan-1-amine
-
chlorpromazine
3-(4-azidophenyl)-2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxyphenyl)acryloylamino]propyl]acrylamide
-
-
3-(5,6-dihydrobenzo[b][1]benzazepin-11-yl)-N,N-dimethylpropan-1-amine
-
imipramine
3-(9-chloro-5,6-dihydrobenzo[b][1]benzazepin-11-yl)-N,N-dimethylpropan-1-amine
-
clomipramine
3-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
-
3-[(5Z)-4-oxo-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(2H-chromen-3-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(3,5-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(biphenyl-4-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
4-(2-dimethylaminoethyl)-2-N-(didecylamino)-6-methylpyrimidine
-
4-(N,N-dimethyl-N-butyl-N-ethyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione methanesulfonate
-
-
4-(N,N-dimethyl-N-dodecyl-N-ethyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione bromide
-
-
4-(N,N-dimethyl-N-dodecyl-N-ethyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione methanesulfonate
-
-
4-(N,N-dimethyl-N-dodecyl-N-propyl)-4-aza-10-oxa-6-ethyltricyclo[5.2.1]decane-3,5-dione methanesulfonate
-
-
4-(N,N-dimethyl-N-dodecyl-N-propyl)-4-aza-10-oxa-6-methyltricyclo[5.2.1]decane-3,5-dione methanesulfonate
-
-
4-(N,N-dimethyl-N-dodecyl-N-propyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione bromide
-
-
4-(N,N-dimethyl-N-dodecyl-N-propyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione methanesulfonate
-
-
4-(N,N-dimethyl-N-octadecyl-N-ethyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione bromide
-
-
4-(N-methyl-N-ethylpiperidine)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione methanesulfonate
-
-
4-amino-3-sulfo-N-(2-(dimethylamino)ethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-(piperazin-1-yl)ethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-aminobenzyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-aminoethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-carboxyethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-mercaptoethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-methoxyethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(3-aminobenzyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(3-hydroxyphenyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(3-hydroxypropyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(4-aminobenzyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(4-carboxybenzyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(4-hydroxybenzyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(4-hydroxyphenyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(4-methoxyphenyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(5-hydroxyhexyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(5-hydroxypentyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(carboxymethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(phenethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-benzyl-1,8-naphthalimide
-
4-amino-3-sulfo-N-phenyl-1,8-naphthalimide
-
4-azido-N-(2-[2-cyano-3-(3,4-dihydroxyphenyl)acryloylamino]-1-[[2-cyano-3-(3,4-dihydroxyphenyl)acryloylamino]methyl]ethyl)-2,3,5,6-tetrafluorobenzamide
-
-
4-chloro-6-methyl-2-(4-methylpiperazin-1-yl)pyrimidine
-
4-chloro-N-(4-methoxybenzyl)-6-methylpyrimidin-2-amine
-
4-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
-
4-[4-(4-chlorophenyl)-4-hydroxy-1-piperidyl]-1-(4-fluorophenyl)-butan-1-one
-
haloperidol
5H-dibenz[b,f]azepine-5-carboxamide
-
carbamazepine
Arc/Arg3.1
enhances dynamin polymerization and GTPase activity. The activity-regulated cytoskeleton-associated protein, Arc, is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc facilitates the polymerization of Dyn2 and stimulates its GTPase activity under physiologic conditions (37°C and 100 mM NaCl). At lower ionic strength Arc also stabilizes preformed Dyn2 polymers against GTP-dependent disassembly, thereby prolonging assembly-dependent GTP hydrolysis catalyzed by Dyn2. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214). At physiologic ionic strength, Arc facilitates Dyn2 self-assembly but does not prevent GTP-dependent Dyn2 disassembly, which is expected to suppress rather than activate endocytosis
-
beta,gamma-methyleneguanosine-5'-monophosphate
-
-
bis-tyrphostin
-
potent inhibitor of the phospholipid-stimulated GTPase activity of dynamin
Ca2+
-
inhibits dynamin I GTPase activity after stimulation by phosphorylation or by phospholipids but not after stimulation a glutathione S-transferase-SH3 fusion protein containing the SH3-domain of phosphoinositide 3-kinase
catechol-acrylamide
-
IC50: 0.0051 mM
cyclosporin A
treating BL-3 cells with 0.005 mM cyclosporine depletes mitochondrial dynamin-2
dynamin inhibitory peptide
-
-
-
fluvoxamine
-
a noncompetitive inhibitor of dynamin I with respect to GTP and a competitive inhibitor with respect to L-phosphatidylserine
guanylyl-iminodiphosphate
-
-
heterotrimeric G protein betagamma subunit complex
-
methyl 2-phenyl-2-(2-piperidyl)acetate
-
methylphenidate
mitochondrial division inhibitor
-
selectively inhibits the mitochondrial division dynamin, is a selective inhibitor of the mitochondrial division dynamin-related GTPase Drp1, and has no effect on either basal or assembly-stimulated rates of GTP hydrolysis for dynamin-1
-
myristyl trimethyl ammonium bromide
-
standard inhibitor of dynamin I
N'-(2-chloro-6-methylpyrimidin-4-yl)ethane-1,2-diamine
-
N'-(4-Chloro-6-methylpyrimidin-2-yl)-ethane-1,2-diamine
-
N-(2-diethylaminoethyl)-2-methoxy-5-methylsulfonyl-benzamide
-
tiapride
N-(2-hydroxyethyl)-1,8-naphthalimide
-
N-benzyl-2-chloro-6-methylpyrimidin-4-amine
-
N-benzyl-4-chloro-6-methylpyrimidin-2-amine
-
N-decyl-N'-(2-dimethylaminoethyl)-pyrimidine-4,6-diamine
-
N-dodecyl-N'-(2-dimethylaminoethyl)pyrimidine-4,6-diamine
-
N-methyl-3-phenyl-3-[4-(trifluoromethyl)phenoxy]-propan-1-amine
-
fluoxetine
N-methyl-9,10-ethanoanthracene-9(10H)-propanamine
-
maprotiline
N-[(1-ethylpyrrolidin-2-yl)methyl]-2-methoxy-5-sulfamoyl-benzamide
-
sulpiride
N-[2-[[(2E)-2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enoyl]amino]-1-([[(2E)-2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enoyl]amino]methyl)ethyl]benzamide
-
-
N1-(4-chloro-6-methylpyrimidin-2-yl)-N3,N3-dimethylpropane-1,3-diamine
-
N2-(2-dimethylaminoethyl)-6-methyl-N4-octadecylpyrimidine-2,4-diamine
-
N2-(2-dimethylaminoethyl)-6-methyl-N4-propylpyrimidine-2,4-diamine
-
N2-(2-dimethylaminoethyl)-6-methyl-N4-tetradecylpyrimidine-2,4-diamine
-
N2-(2-dimethylaminoethyl)-N4-decyl-6-methylpyrimidine-2,4-diamine
-
N2-(2-dimethylaminoethyl)-N4-hexyl-6-methylpyrimidine-2,4-diamine
-
N2-(2-dimethylaminoethyl)-N4-octyl-6-methylpyrimidine-2,4-diamine
-
N2-benzyl-N4-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N2-butyl-N4-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N2-cyclohexyl-N4-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N2-cyclopropylmethyl-N4-(2-dimethylamin-ethyl)-6-methyl-N2-propylpyrimidine-2,4-diamine
-
N2-decyl-N4-(2-dimethylaminoethyl)pyrimidine-2,4-diamine
-
N2-dodecyl-N4-(2-dimethylaminoethyl)-pyrimidine-2,4-diamine
-
N2-sec-butyl-N4-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-6-methyl-N2-octadecylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-6-methyl-N2-propylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-6-methyl-N2-tetradecylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-N2-decyl-6-methylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-N2-hexyl-6-methylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-N2-octyl-6-methylpyrimidine-2,4-diamine
-
N4-Benzyl-N2-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N4-butyl-N2-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N4-cyclohexyl-N2-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N4-cyclopropylmethyl-N2-(2-dimethylamin-ethyl)-6-methyl-N2-propylpyrimidine-2,4-diamine
-
N4-decyl-N2-(2-dimethylaminoethyl)pyrimidine-2,4-diamine
-
N4-dodecyl-N2-(2-dimethylaminoethyl)pyrimidine-2,4-diamine
-
N4-sec-butyl-N2-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
oligomeric beta-amyloid
-
induces dynamin 1 cleavage and depletion, 0.001 mM of A-705253 potently inhibits oligomeric beta-amyloid-induced dynamin 1 cleavage
-
sec-butyl-(2-chloro-6-methylpyrimidin-4-yl)amine
-
sec-butyl-(4-chloro-6-methylpyrimidin-2-yl)amine
-
sertraline
-
a mixed type inhibitor with respect to both GTP and L-phosphatidylserine
[(5Z)-4-oxo-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(2H-chromen-3-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(3,5-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(biphenyl-4-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[2-(2-chloro-6-methylpyrimidin-4-ylamino)ethyl]carbamic acid tert-butyl ester
-
[2-(4-chloro-6-methylpyrimidin-2-ylamino)ethyl]carbamic acid tert-butyl ester
-
dynasore
-
interferes in vitro with Drp1 (the mitochondrial dynamin) activity of dynamin 2, acts as a potent inhibitor of endocytic pathways known to depend on dynamin by rapidly blocking coated vesicle formation; interferes in vitro with the GTPase activity of dynamin1, acts as a potent inhibitor of endocytic pathways known to depend on dynamin by rapidly blocking coated vesicle formation; interferes in vitro with the GTPase activity of dynamin 2, acts as a potent inhibitor of endocytic pathways known to depend on dynamin by rapidly blocking coated vesicle formation
dynasore
-
noncompetitive inhibitor of dynamin GTPase activity
dynasore
-
specific inhibitor of dynamin GTP hydrolysis
dynasore
dynamin specific inhibitor
dynasore
a dynamin inhibitor
dynasore
dynamin specific inhibitor
heterotrimeric G protein betagamma subunit complex
-
oligomerization of dynamin prevents inhibition
-
heterotrimeric G protein betagamma subunit complex
-
oligomerization of dynamin prevents inhibition
-
additional information
-
rhodadyns are a class of small molecule inhibitors of dynamin GTPase activity
-
additional information
fragment-based in silico screening against dynamin I GTPase activity identified the 1,8-naphthalimide framework as a potential scaffold for the design of new inhibitors targeting the GTP binding pocket of dynI. Structure-based design, synthesis and subsequent optimization resulted in the development of a library of 1,8-naphthalimide derivatives. Development of optimised GTP-competitive lead Naphthaladyn compound for the further development of naphthalimide-based dynI GTPase inhibitor. Molecular docking and molecular modelling representation of the predicted binding pose of naphthalimide 4-amino-3-sulfo-N-(2-aminoethyl)-1,8-naphthalimide within the GTP binding pocket of dynI, crystal structure, PDB ID 3ZYCS
-
additional information
computational approach of binding site identification, docking, and interaction energy calculations to design a library of aminopyrimidine analogues targeting site-2 of the pleckstrin homology (PH) domain. Synthesis and evaluation of pyrimidine-based inhibitors of dynamin I GTPase activity, competitive inhibition at the pleckstrin homology domain, overview. The optimized analogues show low micromolar inhibition against both dynamin I and CME and off-target effects at the cholecystokinin, dopamine D2, histamine H1 and H2, melanocortin, melatonin, muscarinic M1 and M3, neurokinin, opioid KOP and serotonin receptors. No inhibition by (4-chloro-6-methylpyrimidin-2-yl)ethylamine at 0.3 mM
-
additional information
-
development of quinone analogues as dynamin GTPase inhibitors, docking study and molecular modelling, overview. No or poor inhibition by 2,5-bis(2-methylanilino)-1,4-benzoquinone, 2,5-bis(2-methoxyanilino)-1,4-benzoquinone, 2,5-bis(3-(hydroxymethyl)phenylamino)-1,4-benzoquinone, 2,5-b+F49is(2-hydroxyethylamino)-1,4-benzoquinone, 2,5-bis(3-hydroxypropylamino)-1,4-benzoquinone, 2,5-bis(4-hydroxybutylamino)-1,4-benzoquinone, 2,5-bis(2-methoxyethylamino)-1,4-benzoquinone, 2,5-bis(2-(methylthio)ethylamino)-1,4-benzoquinone, 2,5-bis(2-chloroethylamino)-1,4-benzoquinone, 2,5-bis(2-bromoethylamino)-1,4-benzoquinone, 2,5-bis(3-chloropropylamino)-1,4-benzoquinone, 2,5-bis(3-pyridylmethylamino)-1,4-benzoquinone, 2,5-bis(4-methylbenzylamino)-1,4-benzoquinone, 2,5-bis(4-fluorobenzylamino)-1,4-benzoquinone, 2,5-bis(4-bromobenzylamino)-1,4-benzoquinone, 2,5-bis(4-chlorobenzylamino)-1,4-benzoquinone, 2,5-bis(phenethylamino)-1,4-benzoquinone, 2,5-bis(ethylamino)-1,4-benzoquinone, 2,5-bis(propylamino)-1,4-benzoquinone, 2,5-bis(butylamino)-1,4-benzoquinone, 2,5-bis(pentylamino)-1,4-benzoquinone, 2,5-bis(isopentylamino)-1,4-benzoquinone, 2,5-bis(allylamino)-1,4-benzoquinone, 2-(2-hydroxyethylamino)-1,4-naphthoquinone, 2-(3-hydroxypropylamino)-1,4-naphthoquinone, 2-(anilino)-1,4-naphthoquinone, 2-(3-carboxyanilino)-1,4-naphthoquinone, 2-(4-carboxyanilino)-1,4-naphthoquinone, 2-(benzylamino)-1,4-naphthoquinone, and 2-(4-methoxybenzylamino)-1,4-naphthoquinone
-
additional information
-
depolarization of primary neurons includes direct association of receptor-type protein tyrosine phosphatase PTP-NP with dynamin-1 within 30 s. This association results in significant inhibition of dynamin-1 GTPase activity (about 75% inhibition). Mutation within the phosphatase domain of PTP-NP (PTP-NP(D947A)) abolishes the direct interaction of PTP-NP with dynamin-1 and fails to inhibit dynamin-1 GTPase activity
-
additional information
-
human Drp1 is knocked down in HeLa cells by the specific siRNA
-
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1-O-(1,2-di-O-palmitoyl-sn-glycerol-3-benzyloxyphosphoryl)-D-myo-inositol 3,4,5-triphosphate
amphiphysin
-
stimulation of dynamin GTPase activity
-
anionic liposome
-
potent stimulation of dynamin GTPase activity at low ionic strength, activator interacts with the highly basic C-terminal proline/arginine-rich domain of dynamin via ionic interactions that are essentially abrogated at physiologic ionic strength
-
antibodies
-
stimulate by crosslinking through the C-terminal proline-rich domain of dynamin
-
endogenouse rat brain vesicles
-
cooperative interactions between dynamin molecules are responsible for the apparent activation of GTPase observed
-
ionomycin
a calcium ionophore, causes rapid mitochondrial accumulation of actin filaments followed by Drp1 accumulation at the fission site, and increases fission rate
L-phosphatidylserine
-
binds the pleckstrin homology domain of dynamin and enhances its GTPase activity
-
lipid tubule
-
stimulate GTPase activity
-
liposome
liposome-stimulated GTPase activity of Dyn1
-
Mff protein
mitocjondrial protein Mff alone causes only a slight increase in Drp1 GTPase activity at the concentrations tested, while the combination of Mff and actin filaments causes a substantial increase in Drp1 activity, far beyond the additive effects of either Mff or actin alone
-
mitochondrial fission factor
-
phosphatidylglycerol
-
stimulates
phosphatidylinositol
-
stimulates
phosphatidylinositol 3,4-bisphosphate
-
weak activation, binds to the pleckstrin homology domain
phosphatidylinositol 4,5-bisphosphate
-
activates the GTPase activity of dynamin, specific for D-5 phosphoinositides, activation mechanism, activates also in the presence of 100-130 mM NaCl, the interactions are mediated by the dynamin pleckstrin homology domain
phosphatidylinositol-4,5-bisphosphate
phosphatidylserine
-
stimulates
phosphatidylserine liposomes
-
-
-
phospholipase D
-
PLD function as a GTPase activating protein, GAP, through its phox homology domain, PX, which directly activates the GTPase domain of dynamin
-
SH3 domain-containing protein
-
activates the GTPase activity of dynamin, activation mechanism
-
1-O-(1,2-di-O-palmitoyl-sn-glycerol-3-benzyloxyphosphoryl)-D-myo-inositol 3,4,5-triphosphate
-
activates, binds to the pleckstrin homology domain
1-O-(1,2-di-O-palmitoyl-sn-glycerol-3-benzyloxyphosphoryl)-D-myo-inositol 3,4,5-triphosphate
-
activates the GTPase activity of dynamin, specific for D-5 phosphoinositides, activation mechanism, activates also in the presence of 100-130 mM NaCl, the interactions are mediated by the dynamin pleckstrin homology domain
actin
actin filaments bind purified Drp1 and increase GTPase activity in a manner that is synergistic with the mitochondrial protein Mff, suggesting a role for direct Drp1/actin interaction
actin
actin filaments increase Drp1's GTPase activity eith a 3.5fold increase. The assembly of filaments of actin is the signal to Drp1 to accumulate on mitochondria and for fission
Arc/Arg3.1
enhances dynamin polymerization and GTPase activity. The activity-regulated cytoskeleton-associated protein, Arc, is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc facilitates the polymerization of Dyn2 and stimulates its GTPase activity under physiologic conditions (37°C and 100 mM NaCl). At lower ionic strength Arc also stabilizes preformed Dyn2 polymers against GTP-dependent disassembly, thereby prolonging assembly-dependent GTP hydrolysis catalyzed by Dyn2. Arc also increases the GTPase activity of Dyn3, an isoform of implicated in dendrite remodeling, but does not affect the activity of Dyn1, a neuron-specific isoform involved in synaptic vesicle recycling. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214). While residues 195-214 may contribute to dynamin binding, additional binding determinants are likely to be present in the N-terminal portion of Arc. Arc stimulates the assembly-dependent GTPase activity of isozymes Dyn2 and Dyn3. The effect of Arc on GTPase activity of dynamin mirrors its effect on dynamin assembly as measured by turbidity
-
Arc/Arg3.1
enhances dynamin polymerization and GTPase activity. The activity-regulated cytoskeleton-associated protein, Arc, is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc increases the GTPase activity of Dyn3, an isoform of implicated in dendrite remodeling. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214). Arc stimulates the assembly-dependent GTPase activity of isozymes Dyn2 and Dyn3. The effect of Arc on GTPase activity of dynamin mirrors its effect on dynamin assembly as measured by turbidity
-
cardiolipin
Drp1 binding to anionic lipids such as cardiolipin increases its GTPase activity
cardiolipin
stimulates Drp1, synergistically with mitochondrial fission factor
cardiolipin
stimulates Drp1, synergistically with mitochondrial fission factor
Grb2
-
activates, binds to carboxyl-terminal proline/arginine-rich domain. Grb2 and phosphatidylinositol 4,5-bisphosphate together increase the dynamin GTPase activity up to 4fold higher than that obtained by these activators tested separately
-
Mff-proteoliposome
lipid-stimulated GTPase activity
-
Mff-proteoliposome
lipid-stimulated GTPase activity
-
microtubule
-
potent stimulation of dynamin GTPase activity at low ionic strength, activator interacts with the highly basic C-terminal proline/arginine-rich domain of dynamin via ionic interactions that are essentially abrogated at physiologic ionic strength
-
microtubule
-
activates GTPase activity
-
microtubules
-
activates, binds to carboxyl-terminal proline/arginine-rich domain
-
microtubules
-
stimulates
-
microtubules
-
cooperative interactions between dynamin molecules are responsible for the apparent activation of GTPase observed
-
microtubules
-
accelerates GTPase activity up to 150fold, about 4fold activation of ATPase activity
-
mitochondrial fission factor
Mff, stimulates Drp1 independently of, but synergistically with cardiolipin
-
mitochondrial fission factor
Mff, stimulates Drp1 independently of, but synergistically with cardiolipin
-
phosphatidylinositol-4,5-bisphosphate
-
activates
phosphatidylinositol-4,5-bisphosphate
-
best activator, binds to the pleckstrin homology domain. Grb2 and phosphatidylinositol 4,5-bisphosphate together increase the dynamin GTPase activity up to 4fold higher than that obtained by these activators tested separately
phosphatidylinositol-4,5-bisphosphate
-
activates
phosphatidylinositol-4,5-bisphosphate
-
binds the pleckstrin homology domain of dynamin and enhances its GTPase activity
Phospholipid
-
mixed-lineage kinase 2-SH2 domain binds dynamin and greatly enhances activation of GTPase by phospholipid
Phospholipid
-
mixed-lineage kinase 2-SH2 domain binds dynamin and greatly enhances activation of GTPase by phospholipid
Phospholipid
-
stimulates GTPase activity of dynamin
Phospholipid
-
acidic phospholipids, cooperative interactions between dynamin molecules are responsible for the apparent activation of GTPase observed
Phospholipid
-
mixed-lineage kinase 2-SH2 domain binds dynamin and greatly enhances activation of GTPase by phospholipid
SH3 domains
-
stimulates
-
SH3 domains
-
stimulation by several recombinant SH3 domains, binding through proline-rich sequence motifs
-
additional information
-
dynamin is activated by the facilitation of its self-association, GTPase activity is stimulated by any factor that induces the formation of appropriately oriented dynamin polymers, not activated by phosphatidylinositol 4-phosphate or 1-O-(1,2-di-O-palmitoyl-sn-glycerol-3-benzyloxyphosphoryl)-D-myo-inositol 3,4-diphosphate
-
additional information
-
oligomerization of dynamin stimulates its GTPase activity
-
additional information
-
dynamin can self-assemble forming higher order structures such as rings and spirals that exhibit up to 100fold stimulated GTPase activity, conformational changes in the active site accompany self-assembly
-
additional information
-
robust stimulation of dynamin's GTPase activity upon polymerization
-
additional information
interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
-
additional information
-
robust stimulation of dynamin's GTPase activity upon polymerization
-
additional information
-
dynamin I and II are stimulated by self-assembly, dynamin II has a greater propensity for self-assembly than neuronal dynamin I
-
additional information
-
the GAP function of PLD1-PX stimulates the GTPase activity of dynamin by increasing dynamin self-assembly
-
additional information
-
robust stimulation of dynamin's GTPase activity upon polymerization
-
additional information
activity-regulated cytoskeleton-associated protein, Arc (Arc/Arg3.1) is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc does not affect the activity of Dyn1, a neuron-specific isoform involved in synaptic vesicle recycling, in contrast to the other Dyn isozymes, Arc stimulates the assembly-dependent GTPase activity of Dyn2 and Dyn3. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214)
-
additional information
activity-regulated cytoskeleton-associated protein, Arc (Arc/Arg3.1) is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc does not affect the activity of Dyn1, a neuron-specific isoform involved in synaptic vesicle recycling, in contrast to the other Dyn isozymes, Arc stimulates the assembly-dependent GTPase activity of Dyn2 and Dyn3. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214)
-
additional information
activity-regulated cytoskeleton-associated protein, Arc (Arc/Arg3.1) is an immediate-early gene product implicated in various forms of synaptic plasticity. Arc promotes endocytosis of AMPA type glutamate receptors and regulates cytoskeletal assembly in neuronal dendrites. Bacterially-expressed His6-Arc does not affect the activity of Dyn1, a neuron-specific isoform involved in synaptic vesicle recycling, in contrast to the other Dyn isozymes, Arc stimulates the assembly-dependent GTPase activity of Dyn2 and Dyn3. Analysis of recombinant full-length mouse Arc and of His6-tagged fragments, including Arc-N (residues 1-227), Arc-C (residues 228-396), and Arc-(DELTA195-214)
-
additional information
interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
-
additional information
-
interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.1
(1R,2R)-2-(aminomethyl)-N,N-diethyl-1-phenyl-cyclopropane-1-carboxamide
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.044
(2E)-2-cyano-N-(3-[[(2E)-2-cyano-3-(3,4-dimethoxyphenyl)prop-2-enoyl]amino]propyl)-3-(3,4-dihydroxyphenyl)prop-2-enamide
Ovis aries
-
in 10 mM Tris, 10 mM NaCl, 2 mM Mg2, at 30°C
0.051
(2E)-2-cyano-N-(3-[[(2E)-2-cyano-3-(4-hydroxyphenyl)prop-2-enoyl]amino]propyl)-3-(3,4-dihydroxyphenyl)prop-2-enamide
Ovis aries
-
in 10 mM Tris, 10 mM NaCl, 2 mM Mg2, at 30°C
0.146
(2E)-2-cyano-N-(3-[[(2E)-2-cyano-3-phenylprop-2-enoyl]amino]propyl)-3-(3,4-dihydroxyphenyl)prop-2-enamide
Ovis aries
-
in 10 mM Tris, 10 mM NaCl, 2 mM Mg2, at 30°C
0.0051
(2E,2'E)-N,N'-(2-hydroxypropane-1,3-diyl)bis[2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enamide]
Ovis aries
-
in 10 mM Tris, 10 mM NaCl, 2 mM Mg2, at 30°C
0.5
(2E,2'E)-N,N'-(2-phenoxypropane-1,3-diyl)bis[2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enamide]
Ovis aries
-
IC50 above 0.5 mM, in 10 mM Tris, 10 mM NaCl, 2 mM Mg2, at 30°C
0.5
(2E,2'E)-N,N'-(2-propoxypropane-1,3-diyl)bis[2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enamide]
Ovis aries
-
IC50 above 0.5 mM, in 10 mM Tris, 10 mM NaCl, 2 mM Mg2, at 30°C
0.0234
(3S-trans)-3-((1,3-benzodioxol-5-yloxy)methyl)-4-(4-fluorophenyl)-piperidine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.05
(5Z)-3-benzyl-5-(3,5-dichlorobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.134
(5Z)-3-benzyl-5-(4-bromobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0074
(5Z)-3-benzyl-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.022
(5Z)-3-benzyl-5-[4-[3-(dimethylamino)propoxy]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0074
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.053
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-3-benzyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.09
(5Z)-5-(2H-chromen-3-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0075
(5Z)-5-(3,5-dichlorobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.031
(5Z)-5-(3,5-dichlorobenzylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0031
(5Z)-5-(3,5-dichlorobenzylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.043
(5Z)-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0055
(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.029
(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0051
(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0045
(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0071
(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.1
1,2,3,4,10,14b-hexahydro-2-methyldibenzo[c,f]pyrazino[1,2-a]azepine
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
1-[3-(dimethylamino)propyl]-1-(4-fluorophenyl)-1,3-dihydro[2]benzofuran-5-carbonitrile
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
10,11-dihydro-5-[3-(methylamino)propyl]-5H-dibenz[b,f]azepine
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.3
2,5-bis(2-(dimethylamino)ethylamino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.3
2,5-bis(2-(hydroxymethyl)anilino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.387
2,5-bis(2-bromoanilino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.0502
2,5-bis(2-carboxyanilino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.58
2,5-bis(3-bromopropylamino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.0254
2,5-bis(3-carboxyanilino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.0579
2,5-bis(3-hydroxyanilino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.3
2,5-bis(3-methoxyanilino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.116
2,5-bis(3-methoxypropylamino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.0215
2,5-bis(4-(hydroxymethyl)phenylamino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.0106
2,5-bis(4-carboxyanilino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.029
2,5-bis(4-carboxybenzylamino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.0111
2,5-bis(4-hydroxyanilino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.112
2,5-bis(4-hydroxybenzylamino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.3
2,5-bis(4-methoxyanilino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.17
2,5-bis(4-methoxybenzylamino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.3
2,5-bis(hexylamino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.273
2,5-bis-(benzylamino)-1,4-benzoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.314
2-(2-carboxyanilino)-1,4-naphthoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.0303
2-(3-(hydroxymethyl)anilino)-1,4-naphthoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.109
2-(3-hydroxyanilino)-1,4-naphthoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.0295
2-(4-(hydroxymethyl)anilino)-1,4-naphthoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.0224
2-(4-hydroxyanilino)-1,4-naphthoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.15
2-(4-hydroxybenzylamino)-1,4-naphthoquinone
Ovis aries
-
pH and temperature not specified in the publication
0.264
2-chloro-4-(2-dimethylaminopropylamine)-6-methylpyrimidine
Homo sapiens
pH and temperature not specified in the publication
0.061
2-cyano-3-(3,4-dihydroxyphenyl)acrylic acid 2-[2-cyano-3-(3,4-dihydroxyphenyl)acryloyloxy]butyl ester
Ovis aries
-
IC50: 0.061 mM
0.042
2-cyano-3-(3,4-dihydroxyphenyl)acrylic acid 2-[2-cyano-3-(3,4-dihydroxyphenyl)acryloyloxy]ethyl ester
Ovis aries
-
IC50: 0.042 mM
0.038
2-cyano-3-(3,4-dihydroxyphenyl)acrylic acid 2-[2-cyano-3-(3,4-dihydroxyphenyl)acryloyloxy]propyl ester
Ovis aries
-
IC50: 0.038 mM
0.0017
2-cyano-N-[2-[2-cyano-3-(3,4,5-trihydroxyphenyl)acryloylamino]ethyl]-3-(3,4,5-trihydroxyphenyl)acrylamide
Ovis aries
-
IC50: 0.0017 mM
0.009
2-cyano-N-[2-[2-cyano-3-(3,4-dihydroxy-4-methoxyphenyl)acryloylamino]ethyl]-3-(3,4-dihydroxy-5-methoxyphenyl) acrylamide
Ovis aries
-
IC50: 0.009 mM
0.006
2-cyano-N-[3-[2-cyano-3-(3,4,5-trihydroxyphenyl)acryloylamino]hexyl]-3-(3,4,5-trihydroxyphenyl)acrylamide
Ovis aries
-
IC50: 0.006 mM
0.08
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxy-5-methoxy-phenyl)acryloylamino]hexyl]-3-(3,4-dihydroxy-5-methoxyphenyl)acrylamide
Ovis aries
-
IC50: 0.08 mM
0.008
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxy-5-methoxy-phenyl)acryloylamino]pentyl]-3-(3,4-dihydroxy-5-methoxyphenyl)acrylamide
Ovis aries
-
IC50: 0.008 mM
0.008
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxy-5-methoxyphenyl)acryloylamino]butyl]-3-(3,4-dihydroxy-5-methoxyphenyl)acrylamide
Ovis aries
-
IC50: 0.008 mM
0.005
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxy-5-methoxyphenyl)acryloylamino]propyl]-3-(3,4-dihydroxy-5-meth-oxyphenyl)acrylamide
Ovis aries
-
IC50: 0.005 mM
0.0051
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxyphenyl)acryloylamino]-2-hydroxypropyl]-3-(3,4-dihydroxyphenyl)acrylamide
Ovis aries
-
IC50: 0.0051 mM
0.0369
2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxyphenyl)acryloylamino]-propyl] 3-[4-(3-trifluoromethyl-3H-diazirin-3-yl)phenyl]acrylamide
Ovis aries
-
in 10 mM Tris, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0372
2-[(8-chlorodibenzo[b,f]thiepin-10-yl)oxy]-N,N-dimethylethanamine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.064
3-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-ylidene)-N-methyl-1-propanamine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0472
3-(2-chloro-10H-phenothiazin-10-yl)-N,N-dimethyl-propan-1-amine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0064
3-(4-azidophenyl)-2-cyano-N-[3-[2-cyano-3-(3,4-dihydroxyphenyl)acryloylamino]propyl]acrylamide
Ovis aries
-
in 10 mM Tris, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
3-(5,6-dihydrobenzo[b][1]benzazepin-11-yl)-N,N-dimethylpropan-1-amine
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0299
3-(9-chloro-5,6-dihydrobenzo[b][1]benzazepin-11-yl)-N,N-dimethylpropan-1-amine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.3
3-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.0235
3-[(5Z)-5-(2H-chromen-3-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0044
3-[(5Z)-5-(3,5-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.096
3-[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.042
3-[(5Z)-5-(biphenyl-4-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.048
3-[(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.01
3-[(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.404
4-(N,N-dimethyl-N-butyl-N-ethyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione methanesulfonate
Ovis aries
-
-
0.0085
4-(N,N-dimethyl-N-dodecyl-N-ethyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione bromide
Ovis aries
-
-
0.0089
4-(N,N-dimethyl-N-dodecyl-N-ethyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione methanesulfonate
Ovis aries
-
-
0.0068
4-(N,N-dimethyl-N-dodecyl-N-propyl)-4-aza-10-oxa-6-ethyltricyclo[5.2.1]decane-3,5-dione methanesulfonate
Ovis aries
-
-
0.0118
4-(N,N-dimethyl-N-dodecyl-N-propyl)-4-aza-10-oxa-6-methyltricyclo[5.2.1]decane-3,5-dione methanesulfonate
Ovis aries
-
-
0.0084
4-(N,N-dimethyl-N-dodecyl-N-propyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione bromide
Ovis aries
-
-
0.0112
4-(N,N-dimethyl-N-dodecyl-N-propyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione methanesulfonate
Ovis aries
-
-
0.0023
4-(N,N-dimethyl-N-octadecyl-N-ethyl)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione bromide
Ovis aries
-
-
0.043
4-(N-methyl-N-ethylpiperidine)-4-aza-10-oxatricyclo[5.2.1]decane-3,5-dione methanesulfonate
Ovis aries
-
-
0.509
4-amino-3-sulfo-N-(2-(dimethylamino)ethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.155
4-amino-3-sulfo-N-(2-aminobenzyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.3
4-amino-3-sulfo-N-(2-aminoethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.094
4-amino-3-sulfo-N-(2-carboxyethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.193
4-amino-3-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.088
4-amino-3-sulfo-N-(3-aminobenzyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.159
4-amino-3-sulfo-N-(3-hydroxyphenyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.093
4-amino-3-sulfo-N-(3-hydroxypropyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.123
4-amino-3-sulfo-N-(4-aminobenzyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.0185
4-amino-3-sulfo-N-(4-carboxybenzyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.0448
4-amino-3-sulfo-N-(4-hydroxybenzyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.296
4-amino-3-sulfo-N-(4-hydroxyphenyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.113
4-amino-3-sulfo-N-(5-hydroxyhexyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.062
4-amino-3-sulfo-N-(5-hydroxypentyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.0191
4-amino-3-sulfo-N-(carboxymethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.0703
4-amino-3-sulfo-N-benzyl-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.3
4-amino-3-sulfo-N-phenyl-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.5
4-azido-N-(2-[2-cyano-3-(3,4-dihydroxyphenyl)acryloylamino]-1-[[2-cyano-3-(3,4-dihydroxyphenyl)acryloylamino]methyl]ethyl)-2,3,5,6-tetrafluorobenzamide
Ovis aries
-
IC50 above 0.5 mM, in 10 mM Tris, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.3
4-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.1
4-[4-(4-chlorophenyl)-4-hydroxy-1-piperidyl]-1-(4-fluorophenyl)-butan-1-one
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
5H-dibenz[b,f]azepine-5-carboxamide
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0017
bis-tyrphostin
Ovis aries
-
in 10 mM Tris, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0051
catechol-acrylamide
Ovis aries
-
IC50: 0.0051 mM
0.0147
fluvoxamine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
methyl 2-phenyl-2-(2-piperidyl)acetate
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0241
myristyl trimethyl ammonium bromide
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
N-(2-diethylaminoethyl)-2-methoxy-5-methylsulfonyl-benzamide
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0334
N-methyl-3-phenyl-3-[4-(trifluoromethyl)phenoxy]-propan-1-amine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0211
N-methyl-9,10-ethanoanthracene-9(10H)-propanamine
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.1
N-[(1-ethylpyrrolidin-2-yl)methyl]-2-methoxy-5-sulfamoyl-benzamide
Mus musculus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.5
N-[2-[[(2E)-2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enoyl]amino]-1-([[(2E)-2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enoyl]amino]methyl)ethyl]benzamide
Ovis aries
-
IC50 above 0.5 mM, in 10 mM Tris, 10 mM NaCl, 2 mM Mg2, at 30°C
0.327
N1-(4-chloro-6-methylpyrimidin-2-yl)-N3,N3-dimethylpropane-1,3-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0073
sertraline
Mus musculus
-
in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C
0.0055
[(5Z)-5-(3,5-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.073
[(5Z)-5-(biphenyl-4-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0123
[(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0034
[(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
additional information
additional information
Homo sapiens
IC50 values, overview
-
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evolution
enzyme AtDRP1A belongss to the DRP1 dynamin-related subfamily of the superfamily of GTPases. Dynamins and other structurally related family members primarily consist of a GTPase domain, a middle domain and a GTPase effector domain, which regulates and responds to hydrolysis of the GTPase domain. The GED and the Nand C-termini of the GTPase domain form a so-called three-helical bundle signalling element that regulates dynamin function
evolution
-
neurolastin is a unique dynamin family GTPase with a RING domain, sequence analysis shows that neurolastin has a C3HC4-type RING domain and key residues important for zinc coordination are conserved
evolution
the enzyme belongs to the dynamin superfamily
evolution
the enzyme is a member of the dynamin superfamily that comprises a family of conserved GTPases. Most dynamin superfamily members contain five conserved GTP-binding motifs (G1-5), similar to small Ras-like GTPases
evolution
the OPA1 gene encodes a mitochondrial protein that belongs to the dynamins family, with which it shares three conserved regions: a GTPase domain, a middle domain, and a GTPase effector domain (GED) containing a coiled-coil domain (CC2), overview
evolution
the OPA1 gene encodes a mitochondrial protein that belongs to the dynamins family, with which it shares three conserved regions: a GTPase domain, a middle domain, and a GTPase effector domain (GED) containing a coiled-coil domain (CC2), overview
evolution
dynamin is the prototype of a family of large multidomain GTPases. Dynamins and dynamin related proteins constitute a large family of atypical multidomain GTPases that share the common properties of low affinity for guanine nucleotides, high rate of GTP hydrolysis and the ability to oligomerize into helical structures
evolution
neurolastin is a dynamin family GTPase. It also contains a RING domain and exhibits both GTPase and E3 ligase activities
evolution
there are three dynamin isoforms in mammalian cells: dynamin1 (neuronal isoform), dynamin2 (ubiquitous isoform) and dynamin3 (a testis, lung and brain isoform). All the dynamin isoforms share similar domain structures aligned from N-terminus to C-terminus: a GTPase domain, a middle domain, a PH domain, a GTPase effector domain (GED) and PRD domain
evolution
there are three dynamin isoforms in mammalian cells: dynamin1 (neuronal isoform), dynamin2 (ubiquitous isoform) and dynamin3 (a testis, lung and brain isoform). All the dynamin isoforms share similar domain structures aligned from N-terminus to C-terminus: a GTPase domain, a middle domain, a PH domain, a GTPase effector domain (GED) and PRD domain
malfunction
-
a dynamin-1 mutant with increased GTPase activity results in transient deformations consistent with rapid fusion pore widening after exocytosis, while a Dyn1 mutant with decreased activity slows fusion pore widening by stabilizing postfusion granule membrane deformations
malfunction
-
deletion of dynamin middle domain blocks binding to gamma-tubulin and impairs entry into mitosis, but does not affect endocytosis
malfunction
-
dynamin gene mutations are responsible for the temperature-sensitive paralytic phenotype of Drosophila melanogaster shibire mutants. The mutants show paralysis resulting from the neuronal activity-dependent depletion of synaptic vesicles, which is accompanied by the accumulation of arrested collared endocytic pits at the presynaptic plasma membrane
malfunction
-
dynamin mutants with impaired GTP binding and/or hydrolysis cycles have dominant-negative effects on endocytosis. Also PH-domain mutants that impair phosphoinositide binding exert dominant-negative effects on clathrin-mediated endocytosis. Dynamin lacking the PRD cannot rescue endocytic defects in dynamin-knockout fibroblasts
malfunction
-
dynamin mutants with impaired GTP binding and/or hydrolysis cycles have dominant-negative effects on endocytosis. Also PH-domain mutants that impair phosphoinositide binding exert dominant-negative effects on clathrin-mediated endocytosis. Dynamin lacking the PRD cannot rescue endocytic defects in dynamin-knockout fibroblasts
malfunction
-
dynamin mutants with impaired GTP binding and/or hydrolysis cycles have dominant-negative effects on endocytosis. Also PH-domain mutants that impair phosphoinositide binding exert dominant-negative effects on clathrin-mediated endocytosis. Dynamin lacking the PRD cannot rescue endocytic defects in dynamin-knockout fibroblasts. Multiple unique missense mutations, or short deletions, within the middle, PH and stalk domains of dynamin 2 in patients with two autosomal-dominant genetic conditions are involved in the Charcot-Marie-Tooth disease and centronuclear myopathy, while dynamin 1 might be involved in epilepsy
malfunction
-
middle domain mutants G350D, R365S and PH, lacking the putative PH-like domain, severely impair the GTPase activity, but have no obvious effects on protein tetramerization and liposome-binding properties, these mutants probably affect protein intra-molecular interactions
malfunction
-
the absence of Sey1p results in the endoplasmic reticulum undergoing delayed fusion in vivo and proteoliposomes containing purified Sey1p fused in a GTP-dependent manner in vitro, phenotypes, overview
malfunction
centronuclear myopathy is a genetically heterogeneous disorder associated with general skeletal muscle weakness, type I fiber predominance and atrophy, and abnormally centralized nuclei. Autosomal dominant centronuclear myopathy is due to mutations in the large GTPase dynamin 2. In addition to centronuclear myopathy, dissimilar DNM2 mutations are associated with Charcot-Marie-Tooth peripheral neuropathy (CMTD1B and CMT2M), suggesting a tissue-specific impact of the mutations, possible clinical overlap, phenotypes, overview
malfunction
deletion of Sey1p protein in cells results in unbranched endoplasmic reticulum, delayed endoplasmic reticulum fusion, or even endoplasmic reticulum fragmentation. Deletion of Sey1p results in decreased virulence
malfunction
dysregulation of enzyme Drp1 is associated with abnormal mitochondrial dynamics and neuronal damage
malfunction
mutated Glu81 and Glu82 in the unique 16-residue insertion of the enzyme influence the activity significantly. Mutations of Gln34, Ser35, and Asp190 in the predicted assembly interface interfer with dimerization of the GTPase domain induced by a transition state analogue and lead to a loss of the lipid-stimulated GTPase activity
malfunction
mutations in OPA1 are responsible for type 1 dominant optic atrophy (ADOA1), alterations of mitochondrial distribution and morphology contribute to ADOA1 pathogenesis, physiopathological relevance, overview. In addition to mitochondrial fragmentation, downregulation of OPA1 increases cell sensitivity to spontaneous and induced apoptosis. Enzyme overexpression by inhibiting cytochrome c release, protects cells from apoptosis induced by intrinsic stimuli. Haploinsufficiency is the main pathomechanism in ADOA1
malfunction
R386G mutation in dynamin 1 middle domain reduces GTPase activity and oligomer stability in the absence of lipids. Vesicle formed in endocytosis are smaller in enzyme mutant R386G cells compared to wild-type
malfunction
silencing of OPA1 reduces induced lipolysis within the differentiated adipocytes
malfunction
inhibition of dynamin2 function, using either RNA interference (RNAi) or the dynamin specific inhibitor Dynasore, causes defects in invadopodia formation and suppresses invasive activity of T24 bladder cancer cells
malfunction
inhibition of dynamin2 function, using either RNA interference (RNAi) or the dynamin specific inhibitor Dynasore, causes defects in invadopodia formation and suppresses invasive activity of T24 bladder cancer cells
malfunction
neurolastin knockout animals have fewer dendritic spines and exhibit a reduction in functional synapses
malfunction
suppression of either INF2 or myosin IIA causes an 50% decrease in fission rate, whereas Drp1 suppression or expression of the dominant-negative Drp1 K38A mutant cause near-complete inhibition. In addition, suppression of either INF2 or myosin IIA reduces mitochondrially-associated Drp1 puncta, with a moderate reduction of total Drp1 puncta (2.7fold for both INF2 and myosin IIA) and a larger reduction in high threshold puncta (6.7fold and 8.3fold, respectively). LatA treatment also causes a reduction in mitochondrially-associated Drp1 puncta, although the degree of high threshold reduction is not as great as for INF2 or myosin IIA suppression
malfunction
the pleckstrin homology domain (PHD) conformational switch is impaired by a centronuclear myopathy-causing disease mutation, S619L, highlighting the physiological significance of its role in regulating dynamin function
metabolism
-
GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events throughout the cell
metabolism
-
GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events throughout the cell
metabolism
-
GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events throughout the cell
metabolism
-
GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events throughout the cell
metabolism
-
GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events throughout the cell
metabolism
enzyme Sey1p can replace the dynamin-like GTPase atlastin (ATL) in mammalian cells
metabolism
plant-specific dynamin-related proteins play crucial roles in cell-plate formation, endocytosis or exocytosis, protein sorting to the vacuole and plasma membrane and the division of mitochondria and chloroplasts
metabolism
the enzyme is a key regulator of mitochondrial fission
metabolism
the small group of dynamin-like GTPases (Guanosine-Triphosphate hydrolase) as central regulators of mitochondrial morphology and cristae remodeling, apoptosis, calcium signaling, and metabolism
metabolism
the small group of dynamin-like GTPases as central regulators of mitochondrial morphology and cristae remodeling, apoptosis, calcium signaling, and metabolism
physiological function
-
dynamin 2 GTPase is a key player in membrane traffic and clathrin-mediated endocytosis, molecular mechanism, overview. It also regulates the dynamic instability of microtubules by a membrane traffic-independent mechanism. Dynamin may play a key role in cell cycle progression by regulating the microtubules
physiological function
-
dynamin drives membrane fission, mechanism, overview. Dynamin is directly involved in the generation of an endocytic vesicle requiring the recruitment of various proteins from the cytosol that orchestrate the bending inward of the plasma membrane to form a deeply invaginated bud and subsequently promote its fission. Dynamin assembles into helical polymers at the necks of budding vesicles and its GTP hydrolysis-dependent conformational change promotes fission of the underlying tubular membrane to generate a free endocytic vesicle. It acts at fission sites for clathrin-mediated endocytosis. Diverse roles for dynamin-like proteins at membrane interfaces, overview. Dynamin is also implicated in some clathrin-independent endocytic pathways, overview. Dynamin affects signalling. Dynamin participates in synaptic vesicle recycling at neuronal synapses. Dynamin interacts both directly and indirectly with the cytoskeleton, overview. Dynamin 2 concentrates at sites of abscission and is implicated in the completion of cytokinesis
physiological function
-
dynamin drives membrane fission, mechanism, overview. Dynamin is directly involved in the generation of an endocytic vesicle requiring the recruitment of various proteins from the cytosol that orchestrate the bending inward of the plasma membrane to form a deeply invaginated bud and subsequently promote its fission. Dynamin assembles into helical polymers at the necks of budding vesicles and its GTP hydrolysis-dependent conformational change promotes fission of the underlying tubular membrane to generate a free endocytic vesicle. It acts at fission sites for clathrin-mediated endocytosis. Diverse roles for dynamin-like proteins at membrane interfaces, overview. Dynamin is also implicated in some clathrin-independent endocytic pathways, overview. Dynamin interacts both directly and indirectly with the cytoskeleton, overview. Dynamin affects signalling. Dynamin participates in synaptic vesicle recycling at neuronal synapses. Dynamin 2 concentrates at sites of abscission and is implicated in the completion of cytokinesis
physiological function
-
dynamin drives membrane fission, mechanism, overview. Dynamin is directly involved in the generation of an endocytic vesicle requiring the recruitment of various proteins from the cytosol that orchestrate the bending inward of the plasma membrane to form a deeply invaginated bud and subsequently promote its fission. Dynamin assembles into helical polymers at the necks of budding vesicles and its GTP hydrolysis-dependent conformational change promotes fission of the underlying tubular membrane to generate a free endocytic vesicle. It acts at fission sites for clathrin-mediated endocytosis. Dynamin interacts both directly and indirectly with the cytoskeleton, overview
physiological function
-
dynamin drives membrane fission, mechanism, overview. Dynamin is directly involved in the generation of an endocytic vesicle requiring the recruitment of various proteins from the cytosol that orchestrate the bending inward of the plasma membrane to form a deeply invaginated bud and subsequently promote its fission. Dynamin assembles into helical polymers at the necks of budding vesicles and its GTP hydrolysis-dependent conformational change promotes fission of the underlying tubular membrane to generate a free endocytic vesicle. It acts at fission sites for clathrin-mediated endocytosis. Dynamin interacts both directly and indirectly with the cytoskeleton, overview
physiological function
-
dynamin drives membrane fission, mechanism, overview. Dynamin-related protein 1, DRP1, is important for the fission of mitochondria and peroxisomes. Dynamin is directly involved in the generation of an endocytic vesicle requiring the recruitment of various proteins from the cytosol that orchestrate the bending inward of the plasma membrane to form a deeply invaginated bud and subsequently promote its fission. Dynamin assembles into helical polymers at the necks of budding vesicles and its GTP hydrolysis-dependent conformational change promotes fission of the underlying tubular membrane to generate a free endocytic vesicle. It acts at fission sites for clathrin-mediated endocytosis. Diverse roles for dynamin-like proteins at membrane interfaces, overview. Dynamin is also implicated in some clathrin-independent endocytic pathways, overview. Dynamin interacts both directly and indirectly with the cytoskeleton, overview. Dynamin affects signalling. Dynamin participates in synaptic vesicle recycling at neuronal synapses. Dynamins 1 and 3 play an important part in the endocytosis of neurotransmitter receptors, overview. Dynamin 2 concentrates at sites of abscission and is implicated in the completion of cytokinesis
physiological function
-
dynamin is a master regulator of membrane fission in endocytosis. In addition to its role in endocytosis, GTPase activity of dynamin regulates the rapidity of fusion pore expansion from tens of milliseconds to seconds after fusion. Membrane-sculpting repertoire of dynamin to include the regulation of immediate postfusion events in exocytosis that control the rate of release of soluble granule contents
physiological function
-
dynamin-like protein 1, DLP-1, is involved in the fission of mitochondrial outer membranes, a process that helps to maintain mitochondrial morphology and to reduce the accumulation of functional and structural defects in mitochondria
physiological function
-
Seyp1 mediates homotypic membrane fusion required to maintain endoplasmic reticulum morphology, overview
physiological function
-
dynamin family GTPases are key membrane remodeling mechanoenzymes. Neurolastin, a dynamin family GTPase, regulates excitatory synapses and spine density. Neurolastin affects endosome size via its RING domain. It is important for excitatory neurotransmission
physiological function
dynamin plays an important role in membrane fission during endocytosis. The dynammin GTPase is important for dynamin oligomer complex dissociation in absence of lipids
physiological function
human dynamin-1-like protein is a GTP-driven molecular machine that segregates mitochondria and peroxisomes, catalytic mechanism involving dimerization of their GTPase domains, overview
physiological function
interaction between the enzyme's GTPase domain and its GED domain is important for regulating dynamin function
physiological function
myxovirus resistance proteins are key mediators of the interferon-induced innate immune response in vertebrates, role of nucleotide binding and GTPase domain dimerization in dynamin-like myxovirus resistance protein A for GTPase activation and antiviral activity. GTP binding allows GTPase domain dimerization and membrane-associated assembly of MxA, but it is not sufficient to induce a sustained antiviral effect
physiological function
OPA1 mediates adrenergic control of lipolysis by functioning as a cytosolic A-kinase anchoring protein (AKAP), on the hemimembrane that envelops the lipid droplet. Enzyme is OPA1 a regulator of mitochondrial inner membrane fusion and cristae remodeling, role of OPA1 in mtDNA maintenance and mitochondrial energetics. Enzyme regulation, m-AAA protease controls both cleavage and turn-over of OPA1, OMA1 is activated upon attenuation of its proteolytic degradation, overview
physiological function
OPA1 mediates adrenergic control of lipolysis by functioning as a cytosolic A-kinase anchoring protein (AKAP), on the hemimembrane that envelops the lipid droplet. Enzyme is OPA1 a regulator of mitochondrial inner membrane fusion and cristae remodeling, role of OPA1 in mtDNA maintenance and mitochondrial energetics. Enzyme regulation, m-AAA protease controls both cleavage and turnover of OPA1, OMA1 is activated upon attenuation of its proteolytic degradation, overview
physiological function
the enzyme mediates homotypic membrane fusion of the endoplasmic reticulum, GTP hydrolysis is not essential but accelerates the fusion reaction, the proposed mechanism demonstrates a common scheme for fusion mediated by dynamin-like GTPases and reveals that the stalk domain of Sey1p possesses unique functional features. The linkage of opposing membranes through GTP binding-induced dimerization may be sufficient to promote Sey1p-mediated fusion. GTPase-based endoplasmic reticulum fusogens play critical physiological roles
physiological function
the large GTPase dynamin 2 is a mechanochemical enzyme regulating cytoskeleton and membrane trafficking in cells. The enzyme acts as a mechanochemical enzyme involved in membrane fission, and is therefore a key player for endosome formation and membrane trafficking from the plasma membrane and the trans-Golgi network
physiological function
the mechano-enzyme dynamin-related protein 1 plays an important role in mitochondrial fission and is implicated in cell physiology
physiological function
coordinated conformational changes regulate dynamin function and couple membrane binding, oligomerization, and GTPase activity during dynamin-catalyzed membrane fission
physiological function
distinct splice variants of dynamin-related protein 1 differentially utilize mitochondrial fission factor as an effector of cooperative GTPase activity
physiological function
distinct splice variants of dynamin-related protein 1 differentially utilize mitochondrial fission factor as an effector of cooperative GTPase activity
physiological function
Dyn1 is a neuron-specific isoform involved in synaptic vesicle recycling
physiological function
dynamin is a key player in clathrin-mediated endocytosis, where it cleaves off vesicles from membranes using the energy from GTP hydrolysis
physiological function
dynamin is a large GTPase essential for membrane fission in clathrin-mediated endocytosis. There are three dynamin isoforms in mammalian cells. Isozyme dynamin2 GTPase contributes to invadopodia formation in invasive bladder cancer cells. Cancer cell invasion is mediated by actin-based membrane protrusions termed invadopodia. Invadopodia consist of core F-actin bundles associated with adhesive and proteolytic machineries promoting cell invasion by degrading extracellular matrix (ECM). Formation of the F-actin core in invadopodia is regulated by various actin-binding proteins including Arp2/3 complex and cortactin. Dynamin GTPase localizes to the invadopodia and is implicated in cancer cell invasion. Dynamin2 contributes to bladder cancer invasion by controlling invadopodia formation in bladder cancer cells
physiological function
dynamin is a large GTPase essential for membrane fission in clathrin-mediated endocytosis. There are three dynamin isoforms in mammalian cells. Isozyme dynamin2 GTPase contributes to invadopodia formation in invasive bladder cancer cells. Cancer cell invasion is mediated by actin-based membrane protrusions termed invadopodia. Invadopodia consist of core F-actin bundles associated with adhesive and proteolytic machineries promoting cell invasion by degrading extracellular matrix (ECM). Formation of the F-actin core in invadopodia is regulated by various actin-binding proteins including Arp2/3 complex and cortactin. Dynamin GTPase localizes to the invadopodia and is implicated in cancer cell invasion. Dynamin2 contributes to bladder cancer invasion by controlling invadopodia formation in bladder cancer cells
physiological function
mitochondrial fission is mediated by the dynamin-related GTPases Dnm1/Drp1 (yeast/mammals), which form spirals around constricted sites on mitochondria. Additional membrane-associated adaptor proteins (Fis1, Mdv1, Mff, and MiDs) are required to recruit these GTPases from the cytoplasm to the mitochondrial surface. Adaptors regulate mitochondrial dynamin assembly for membrane scission. An adaptor protein alters the architecture of a mitochondrial dynamin GTPase polymer in a manner that can facilitate membrane constriction and severing activity. Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
physiological function
mitochondrial fission is mediated by the dynamin-related GTPases Dnm1/Drp1 (yeast/mammals), which form spirals around constricted sites on mitochondria. Additional membrane-associated adaptor proteins (Fis1, Mdv1, Mff, and MiDs) are required to recruit these GTPases from the cytoplasm to the mitochondrial surface. Adaptors regulate mitochondrial dynamin assembly for membrane scission. An adaptor protein alters the architecture of a mitochondrial dynamin GTPase polymer in a manner that can facilitate membrane constriction and severing activity. Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
physiological function
neurolastin, a dynamin family GTPase, translocates to mitochondria upon neuronal stress and alters mitochondrial morphology in vivo. It is specifically expressed in the brain and is important for synaptic transmission
physiological function
the large GTPase dynamin mediates membrane fission during clathrin-mediated endocytosis (CME)
physiological function
the large GTPase dynamin mediates membrane fission during clathrin-mediated endocytosis (CME). Dynamin GTPase Drp1 plays a critical role during mitochondrial fission, cytosolic Drp1 is recruited directly to fission sites immediately prior to fission. Progressive maturation of Drp1 oligomers on mitochondria through incorporation of smaller mitochondrially-bound Drp1 units. Maturation of a stable Drp1 oligomer does not forcibly lead to fission. Drp1 oligomers also translocate directionally along mitochondria. Drp1 is in dynamic equilibrium on mitochondria in a fission-independent manner, and fission factors such as actin filaments target productive oligomerization to fission sites. The assembly of filaments of actin is the signal to Drp1 for fission. Differential affinities of Drp1 oligomeric states for actin filaments
additional information
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effects of transiently expressed Dyn1WT on membrane topological changes following granule fusion in bovine adrenal chromaffin cells, overview. Expression of dynamin GTPase mutants altered the speed of NPY-Cer release
additional information
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human ATL1 can functionally replace Sey1p in yeast
additional information
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proper domain-domain interactions are important for DLP-1 GTPase activity
additional information
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structure-function relationship, overview. Many proteins that bind dynamin's Pro-rich domain via an SRC homology 3 domain also contain Bin-amphiphysin-Rvs, i.e. BAR, domains, which are protein modules with curvature-generating and -sensing properties
additional information
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structure-function relationship, overview. Many proteins that bind dynamin's Pro-rich domain via an SRC homology 3 domain also contain Bin-amphiphysin-Rvs, i.e. BAR, domains, which are protein modules with curvature-generating and -sensing properties
additional information
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structure-function relationship, overview. The C-terminal Pro-rich region, PRD, contains an array of PXXP amino acid motifs, which interact with many SH3 domain-containing proteins to localize dynamin at endocytic sites and coordinate dynamin's function with these other factors during endocytosis. Many proteins that bind dynamin's Pro-rich domain via an SRC homology 3 domain also contain Bin-amphiphysin-Rvs, i.e. BAR, domains, which are protein modules with curvature-generating and -sensing properties
additional information
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structure-function relationship, overview. The C-terminal Pro-rich region, PRD, contains an array of PXXP amino acid motifs, which interact with many SH3 domain-containing proteins to localize dynamin at endocytic sites and coordinate dynamin's function with these other factors during endocytosis. Many proteins that bind dynamin's Pro-rich domain via an SRC homology 3 domain also contain Bin-amphiphysin-Rvs, i.e. BAR, domains, which are protein modules with curvature-generating and -sensing properties
additional information
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structure-function relationship, overview. The C-terminal Pro-rich region, PRD, contains an array of PXXP amino acid motifs, which interact with many SH3 domain-containing proteins to localize dynamin at endocytic sites and coordinate dynamin's function with these other factors during endocytosis. Many proteins that bind dynamin's Pro-rich domain via an SRC homology 3 domain also contain Bin-amphiphysin-Rvs, i.e. BAR, domains, which are protein modules with curvature-generating and -sensing properties
additional information
detailed structure-function analysis of human OPA1 enzyme, overview
additional information
dynI GTPase domain, important loops close to the GTP binding site, structure overview. The sulfonate moiety has a Mg2+ coordinator within the GTP binding pocket
additional information
enzyme Drp1 shares structural and functional similarities with dynamin 1 with respect to domain organization, ability to self-assemble into spiral-like oligomers and GTP-cycle-dependent membrane scission. The enzyme has an additional unstructured region between the middle domain and GTPase effector domain
additional information
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enzyme Drp1 shares structural and functional similarities with dynamin 1 with respect to domain organization, ability to self-assemble into spiral-like oligomers and GTP-cycle-dependent membrane scission. The enzyme has an additional unstructured region between the middle domain and GTPase effector domain
additional information
homology modeling and comparison to human dynamin1 GTPase structure, overview. Most of the residues in the catalytic center are highly conserved between MxA and dynamin, for example the G4 loop mediating specificity for guanine binding
additional information
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homology modeling and comparison to human dynamin1 GTPase structure, overview. Most of the residues in the catalytic center are highly conserved between MxA and dynamin, for example the G4 loop mediating specificity for guanine binding
additional information
the enzyme has a long stalk-like, helical bundle domain. Structures of the cytosolic domain of Sey1p, overview. Enzyme CytSey1p consists of an N-terminal GTPase domain and a long, stalk-like, helical domain connected by a linker region. In the dimer, the GTPase domains interact with one another in such a way that the nucleotide binding sites face each other. The linker regions of the two Sey1p molecules cross one another, allowing a close association of the tops of the stalk domains. The stalk domain is composed of four three-helix bundles, with the last helix of each bundle extending into the first helix of the next bundle. The catalytic residues is S68 in caSey1p, which adopts a different rotamer conformation after the cleavage of the gamma-phosphate bond, which in turn causes some minor local rearrangements
additional information
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the enzyme has a long stalk-like, helical bundle domain. Structures of the cytosolic domain of Sey1p, overview. Enzyme CytSey1p consists of an N-terminal GTPase domain and a long, stalk-like, helical domain connected by a linker region. In the dimer, the GTPase domains interact with one another in such a way that the nucleotide binding sites face each other. The linker regions of the two Sey1p molecules cross one another, allowing a close association of the tops of the stalk domains. The stalk domain is composed of four three-helix bundles, with the last helix of each bundle extending into the first helix of the next bundle. The catalytic residues is S68 in caSey1p, which adopts a different rotamer conformation after the cleavage of the gamma-phosphate bond, which in turn causes some minor local rearrangements
additional information
the GTPase domain of the enzyme is structurally related to that of dynamin and binds the nucleotide 5'-guanylyl-imidodiphosphate (GMP-PNP) via five highly conserved motifs, whereas the BSE folds into a pocket at the opposite side. Residues essential for the GTPase reaction are Lys38, Ser39 and Ser40 in the phosphate binding loop, Thr59 from switch I, Asp146 and Gly149 from switch II, Lys216 and Asp218 in the G4 element, as well as Asn246 in the G5 element. Conformational changes upon GTP-binding in the active site, and overall structure of the DNM1L GTPase-GED fusion protein, overview
additional information
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the GTPase domain of the enzyme is structurally related to that of dynamin and binds the nucleotide 5'-guanylyl-imidodiphosphate (GMP-PNP) via five highly conserved motifs, whereas the BSE folds into a pocket at the opposite side. Residues essential for the GTPase reaction are Lys38, Ser39 and Ser40 in the phosphate binding loop, Thr59 from switch I, Asp146 and Gly149 from switch II, Lys216 and Asp218 in the G4 element, as well as Asn246 in the G5 element. Conformational changes upon GTP-binding in the active site, and overall structure of the DNM1L GTPase-GED fusion protein, overview
additional information
analysis of the structural changes through the hydrolytic cycle, the GDP state, the GTP state, the transition state, and the nucleotide-free state of dynamin 1, detailed overview. The G domain of dynamin 1 contains five nucleotide binding motifs G1 to G5. G1 comprises the residues 38GGQSAGKS45 and is also known as P-loop or Walker A motif; G2 describes the loop containing the conserved residue T65 and is also called switch I or Walker Bmotif. G3 comprises residues 136DLPG139 and is also called switch II. G4 comprises residues 205TKLD208. G5 comprises residues 236NRSQKDIDGKK246 and is known as the dynamin specific loop (DSL). Interactions of TSL and especially CSL restrict the conformational flexibility of switch II to ensure efficient positioning during catalysis
additional information
Drp1 isoforms exhibit differential GTPase activities, comparison of splice variants, overview. Human isozyme Drp1-short exhibits greater cooperative GTPase activities relative to rat Drp1-long
additional information
Drp1 isoforms exhibit differential GTPase activities, comparison of splice variants, overview. Human isozyme Drp1-short exhibits greater cooperative GTPase activities relative to rat Drp1-long
additional information
structure-function analysis using dynamin2 deletion fragments identifies the proline/arginine-rich domain (PRD) of dynamin2 as indispensable for invadopodia formation and invasiveness of cancer cells
additional information
structure-function analysis using dynamin2 deletion fragments identifies the proline/arginine-rich domain (PRD) of dynamin2 as indispensable for invadopodia formation and invasiveness of T24 cells
additional information
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structure-function analysis using dynamin2 deletion fragments identifies the proline/arginine-rich domain (PRD) of dynamin2 as indispensable for invadopodia formation and invasiveness of T24 cells
additional information
the BSE and PHD are mobile elements necessary for dynamin function. Hydrogen-deuterium exchange coupled with mass spectrometry revealed global nucleotide- and membrane-binding-dependent conformational changes, as well as the existence of an allosteric relay element in the a2S helix of the dynamin stalk domain. FRET analyses detect large movements of the pleckstrin homology domain (PHD) from a closed conformation docked near the stalk to an open conformation able to interact with membranes. PHD movements function as a conformational switch to regulate dynamin self-assembly, membrane binding, and fission. The wild-type isozyme Dyn2 exhibits greater curvature dependence for membrane binding than wild-type isozyme Dyn1
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monomer
-
1 * isolated GTPase domain, SDS-PAGE
oligomer
in solution, Drp1 exists in a number of oligomeric states, including dimers, tetramers, and higher-order oligomers. Actin filaments can organize Drp1 into a productive oligomer
?
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x * 100000, about, Western blot analysis
?
x * 40923, nucleotide-free GTPase-GTPase effector domain fusion protein of Drp1, mass spectrometry
dimer
2 * 78000-85000, recombinant enzyme, SDS-PAGE
dimer
-
Sey1p undergoes GTP-dependent dimerization
heterotetramer
-
Dyn1 can interfere with Dyn2 or Dyn2 mutants, Dyn2-Dyn1, Dyn2S45N-Dyn1 and Dyn2-Dyn1I690K heteromers are formed
heterotetramer
-
Dyn2 can interfere with Dyn2 mutants or Dyn1, Dyn2-Dyn1, Dyn2S45N-Dyn1 and Dyn2-Dyn1I690K heteromers are formed
homotetramer
-
-
tetramer
dimer of dimers, 4 * 39000, crystal structure analysis
tetramer
-
a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions
tetramer
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a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions
tetramer
-
4 * 80000, SDS-PAGE, 4 * 45000, isolated PH-like domain, SDS-PAGE
tetramer
-
a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions. The tetrameric form of dynamin, which can be abundant in solution, may be an intermediate in higher-order assembly
tetramer
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a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions. The tetrameric form of dynamin, which can be abundant in solution, may be an intermediate in higher-order assembly
tetramer
-
dynamin dimers need to oligomerize into tetramers for efficient GTP binding
tetramer
-
a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions. The tetrameric form of dynamin, which can be abundant in solution, may be an intermediate in higher-order assembly
additional information
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dynamin is characterized by a tetramer/monomer equilibrium. Dynamin molecules must be in proper conformation or orientation if they are to form an active oligomer
additional information
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oligomerization of dynamin stimulates its GTPase activity
additional information
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structure-function relationship, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
enzyme Sey1p forms a side-by-side dimer in complex with GMP-PNP or GDP/AIF4-, but is monomeric with GDP. The dimerization of caSey1p involves a hydrophobic patch on top of the GTPase domain, including a conserved L257 within the guanine cap, and several hydrophilic interactions along the GTPase interface. The stalk domains also pack against each other in the dimer
additional information
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enzyme Sey1p forms a side-by-side dimer in complex with GMP-PNP or GDP/AIF4-, but is monomeric with GDP. The dimerization of caSey1p involves a hydrophobic patch on top of the GTPase domain, including a conserved L257 within the guanine cap, and several hydrophilic interactions along the GTPase interface. The stalk domains also pack against each other in the dimer
additional information
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structure-function relationship, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
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dynamin can self-assemble forming higher order structures such as rings and spirals that exhibit up to 100fold stimulated GTPase activity
additional information
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oligomerization (large soluble oligomers with a molecular mass of 600000 da) is mediated by the GTPase effector domain. Structural characterization of the large soluble oligomers of the GTPase effector domain of dynamin
additional information
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DLP-1 contains a GTPase domain, a middle domain, a putative PH-like domain, and a GTPase effector domain, GED
additional information
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structure-function relationship, overview. Dynamin polymerization results from the apposition of dimers via stalk-tip interactions, mechanism, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
dimerization of MxA via a GTPase domain interface is required for GTP hydrolysis and antiviral activity. Residues in the catalytic center of MxA and the nucleotide itself are essential for G domain dimerization and catalytic activation
additional information
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dimerization of MxA via a GTPase domain interface is required for GTP hydrolysis and antiviral activity. Residues in the catalytic center of MxA and the nucleotide itself are essential for G domain dimerization and catalytic activation
additional information
dynamin 2 is a multidomain protein composed of an N-terminal GTPase domain, a middle domain (MID), a pleckstrin homology (PH) domain, a GTPase effector domain (GED), and a C-terminal prolinearginine-rich domain (PRD)
additional information
all dynamin isoforms share similar domain structures aligned from N-terminus to C-terminus: a GTPase domain, a middle domain, a PH domain, a GTPase effector domain (GED) and PRD domain
additional information
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all dynamin isoforms share similar domain structures aligned from N-terminus to C-terminus: a GTPase domain, a middle domain, a PH domain, a GTPase effector domain (GED) and PRD domain
additional information
Drp1 isoforms exhibit differential oligomerization propensities in solution and distinct helical geometry on cardiolipin-containing membranes, analysis of Drp1-short, Drp1-A-only, and Drp1-B-only by gel filtration
additional information
dynamin can be subdivided into five domains: the N-terminal GTPase domain (G domain), the bundle signalling element (BSE), the stalk, the pleckstrin homology domain (PH domain), and the proline-rich domain (PRD). The G domain binds and hydrolyses GTP. The BSE is a three-helix bundle originating from the termini of the G domain and from a more C-terminal helix that fold back towards the N-terminus
additional information
enzyme domain structure, overview. Hydrogen-deuterium exchange kinetics reveal long-range nucleotide- and/or membrane-binding-driven conformational changes in dynamin
additional information
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structure-function relationship, overview. Dynamin polymerization results from the apposition of dimers via stalk-tip interactions, mechanism, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
the enzyme's middle domain is involved in the formation of functional oligomers. Wild-type enzyme forms oligomers, while enzyme mutant R386G prefers to form monomers
additional information
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assembly into higher order structures such as rings or spirals
additional information
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dynamin is a multidomain protein that self-assembles into higher order structures resembling rings during endocytosis
additional information
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structure-function relationship, overview. Dynamin polymerization results from the apposition of dimers via stalk-tip interactions, mechanism, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
all dynamin isoforms share similar domain structures aligned from N-terminus to C-terminus: a GTPase domain, a middle domain, a PH domain, a GTPase effector domain (GED) and proline/arginine-rich domain (PRD) domain
additional information
Drp1 isoforms exhibit differential oligomerization propensities in solution and distinct helical geometry on cardiolipin-containing membranes, analysis of Drp1-long, Drp1-A-only, and Drp1-B-only by gel filtration
additional information
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Sey1p dimerizes in the presence of GDP AlFx
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K75A
-
dominant-negative mutant of DRP5
P77L
-
edr3 mutant, GTP hydrolysis is blocked, but not GTP binding
K142A
-
mutation in the GTPase domain of dynamin, mutant has a moderately impaired GTPase activity, kinetics
R66A
-
mutation in the GTPase domain of dynamin, kinetics
S45N
-
mutation in the GTPase domain of dynamin, mutant is defective in GTP binding, kinetics
T141Q
-
mutation in the GTPase domain of dynamin, mutant is partially inhibited in its GTPase activity, kinetics
T65A
-
mutation in the GTPase domain of dynamin, very low GTPase activity, kinetics
L233A
site-directed mutagensis, the mutation drastically reduces the dimerization, GTPase activity, and fusion activity of scSey1p
G363D
-
mutant shows dominant-negative activity to normal DLP1, mutation causes lipid transport deficiency
D146A
site-directed mutagenesis
D190A
site-directed mutagenesis
D218A
site-directed mutagenesis
D250N
site-directed mutagenesis, a monomeric mutant, loss of nucleotide binding
D253N
site-directed mutagenesis, a monomeric mutant
DynII690K
-
point mutation to render Dyn1 defective in oligomerization and self-assembly
E81A
site-directed mutagenesis
E81A/E82A
site-directed mutagenesis
G149A
site-directed mutagenesis
G255E
site-directed mutagenesis, a monomeric mutant
G350D
-
middle domain mutant, the mutant shows impaired GTPase activity, but unaffected protein tetramerization and liposome-binding properties
I697A
-
mutation inhibits oligomerization substantially
K216A
site-directed mutagenesis
K83A
site-directed mutagenesis, the mutant shows reduced dimerization
M527D
site-directed mutagenesis, a monomeric mutant
M527D/D250N
site-directed mutagenesis, a monomeric mutant
M527D/D250N/D253N
site-directed mutagenesis, a monomeric mutant
M527D/D253N
site-directed mutagenesis, a monomeric mutant
M527D/K83A
site-directed mutagenesis, a monomeric mutant
M527D/T103A
site-directed mutagenesis, a monomeric mutant
N246A
site-directed mutagenesis
Q34A
site-directed mutagenesis
R365S
-
middle domain mutant, the mutant shows impaired GTPase activity, but unaffected protein tetramerization and liposome-binding properties
R399A
-
the mutant displays a severe defect in quaternary structure in solution and on membranes, no detectable membrane tubulation is observed with R399A, nor is R399A capable of mediating membrane fission, R399A is also unable to inhibit fission catalyzed by wild type dynamin
S35A
site-directed mutagenesis
S39A
site-directed mutagenesis
S40A
site-directed mutagenesis
S45N
-
the mutant is defective in GTP binding
S619L
site-directed mutagenesis, the pleckstrin homology domain (PHD) conformational switch is impaired by the centronuclear myopathy-causing disease mutation. The temperature-sensitive phenotype of the Dyn1S619L mutant reflects temperature-sensitive changes in the steady-state conformation(s) adopted by the PHD
S61A
-
mutation lowers the rate of assembly-stimulated GTP hydrolysis without altering the Km for GTP, kinetic data
T103A
site-directed mutagenesis, a monomeric mutant
T141A
-
mutation increases the rate of assembly-stimulated GTP hydrolysis without altering the Km for GTP, kinetic data
T59A
site-directed mutagenesis
T65A
-
mutation dramatically lowers both the rate of assembly-stimulated GTP hydrolysis and the affinity for GTP, kinetic data
T65D
-
mutation dramatically lowers both the rate of assembly-stimulated GTP hydrolysis and the affinity for GTP, kinetic data
T65H
-
mutation dramatically lowers both the rate of assembly-stimulated GTP hydrolysis and the affinity for GTP, kinetic data
V268M
site-directed mutagenesis, the mutant shows reduced dimerization
Y354C
site-directed mutagenesis, interaction analysis with Dyn2L354C-IAEDANS mutant, membrane binding and consequent opening of PHD in mutants Dyn1Y354C-IAEDANS and Dyn2L354C-IAEDANS, overview
C83S/C103S
site-directed mutagenesis
C85A
-
site-directed mutagenesis, a dominant-negative mutant
D273A
OPA1 missense mutation associated with autosomal dominant optic atrophy
E270K
OPA1 missense mutation associated with autosomal dominant optic atrophy
GST-Dyn1-C
-
single domain of dynamin-1, constructed for the identification of the interaction domains between dynamin-1 and TULP1
GST-Dyn1-N
-
single domain of dynamin-1, constructed for the identification of the interaction domains between dynamin-1 and TULP1
GST-Dyn1-PRD
-
single domain of dynamin-1, constructed for the identification of the interaction domains between dynamin-1 and TULP1
H97W
-
site-directed mutagenesis, a RING mutant
K301A
loss of function mutation within the G1 GTP-binding domain
K44A
-
dominant-negative dynamin mutant
OPA1Q285STOP
naturally occuring mutation, heterozygous mutant mice, carrying either a premature stop codon (OPA1Q285STOP/+) or an in-frame deletion of 27 amino acids (OPA1Q329-355del/+) in the GTPase domain, are based on haploinsufficiency since both models show a 50% reduction in OPA1 protein expression
Q329-355del
naturally occuring mutation, heterozygous mutant mice, carrying either a premature stop codon (OPA1Q285STOP/+) or an in-frame deletion of 27 amino acids (OPA1Q329-355del/+) in the GTPase domain, are based on haploinsufficiency since both models show a 50% reduction in OPA1 protein expression
R340Q
-
site-directed mutagenesis, GTPase inactive mutant
R386G
site-directed mutagenesis, replacement of Arg386 with Gly in dynamin 1 middle domain reduces GTPase activity and oligomer stability in the absence of lipids, while in presence of phosphatidylserine liposomes, the intermolecular interactions of dynamin 1 are not affected. The mutant is a monomer with reduced GTPase activity compared to the wild-type enzyme
Dyn2DELTAPRD
-
truncation mutant lacking the C-terminal proline-arginine-rich domain, PRD
Dyn2I684K
-
point mutation to render Dyn2 defective in oligomerization and self-assembly
Dyn2I684KDELTAPRD
-
point mutation to render Dyn2 defective in oligomerization and self-assembly
Dyn2S45N
-
point mutation to render Dyn2 defective in GTP binding
Dyn2S45N/I684K
-
point mutations to render Dyn2 defective in GTP binding and in oligomerization and self-assembly
I690K
-
mutant is assembly incompetent and inactive for endocytosis
K38A
-
dominant-negative mutant
K44E
-
dominant-negative form of dynamin
K694A
-
mutant of dynamin that increases the rate of endocytosis owing to impaired assembly into higher order structures
R59A
-
kcat is 1.5fold lower than wild-type value, KM is 5.2fold higher than wild-type value
R59K
-
kcat is 3fold lower than wild-type value, KM is 2fold higher than wild-type value
S126A
-
mutation in the potential recognition site for Cdk1/cyclin B
S136A
-
mutation in the potential recognition site for Cdk1/cyclin B
S585A
-
exogenous expression of unphosphorylated mutant S585A leads to reduced mitotic mitochondrial fragmentation
S71A
-
mutation in the potential recognition site for Cdk1/cyclin B
A592V
-
the mutant acts similar to the wild-type enzyme
K50A
-
the mutant shows reduced GTPase activity compared to the wild-type and is unable to mediate proteoliposomal fusion
T141A
-
the Dyn1mutant shows increased GTPase activity and GTP affinity, the frequency of endocytosis after fusion events is increased to 22% compared to 17% in cells not expressing the recombinant protein, the mutant enhances transferrin internalization
T65A
-
the Dyn1mutant shows greatly reduced GTPase activity and reduced GTP affinity, the frequency of endocytosis after fusion events is decreased to 7% compared to 17% in cells not expressing the recombinant protein, the mutant reuces transferrin internalization
K38A
site-directed mutagenesis
K38A
-
a GTPase null mutant
K38A
site-directed mutagenesis, enzymatically inactive mutant
K44A
-
mutant defective in GTP binding and hydrolysis, mutation in the first of three nucleotide binding elements, in HeLa cells overexpressing mutant dynamin, coated pits fail to become constricted and coated vesicles fail to bud, so that endocytosis via both transferrin and EGF receptors is potently inhibited, these cells accumulate long tubules, many of which remain connected to the plasma membrane, detailed biochemical and morphological analysis of the functional consequences of overexpression of the dynamin mutant
K44A
-
mutant defective in GTP binding and hydrolysis, the Trypanosoma cruzi invasion of nonphagocytic cells is completely abolished by overexpression of the dominant negative mutant of dynamin K44A
K44A
-
GTPase-deficient mutant
K44A
dominant negative mutant
K44A
dominant-negative dynamin mutant
K44A
-
dominant-negative mutants of dynamin, the mutant is defective in its GTP binding site, effectively blocking dynamin-mediated endocytosis at a stage after the initiation of the coat assembly and preceding the sequestration into deeply invaginated coated pits
K44A
-
mutant of dynamin that cannot bind GTP
K44A
dominant-negative dynamin mutant
K44A
mutant with reduced the GTP binding affinity and therefore impaired the GTPase activity
K44A
the dominant-negative mutation locks the protein in a membrane-associated GTP-bound state, thus blocking plasma membrane scission
K44A
-
a dominant-negative mutation, blocks cytokinesis and membrane trafficking, but does not affect endocytosis, the mutant has no effect on microtubules
additional information
generation of an AtDRP1A fusion protein consisting of residues 1-316 of the GTPase domain and residues 585-606 of GED fused by a flexible linker with the primary sequence HGTDSRV as suggested from human dynamin
additional information
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generation of an AtDRP1A fusion protein consisting of residues 1-316 of the GTPase domain and residues 585-606 of GED fused by a flexible linker with the primary sequence HGTDSRV as suggested from human dynamin
additional information
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point mutants of the GTPase effector domain of dynamin
additional information
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dyn-1 temperature-sensitive mutant dyn-1(ky51)
additional information
generation of a truncation mutant comprising residues 1-692. The mutant is truncated before the first transmembrane region
additional information
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generation of a truncation mutant comprising residues 1-692. The mutant is truncated before the first transmembrane region
additional information
Drosophila sp. (in: flies)
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mutations in shibire, the Drosophila dynamin, cause temperature-sensitive defects in endocytosis. The ts2 mutation, which occurs in the switch 2 region of dynamins GTPase domain, compromises GTP binding affinity. Three second-site suppressor mutations, one in the switch 1 region of the GTPase domain and two in the GTPase effector domain, dynamins putative GAP, fully rescue the shi ts2 defects in synaptic vesicle recycling
additional information
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effect of dynamin GTPase domain mutations on GTP binding, GTP hydrolysis and clathrin-mediated endocytosis
additional information
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deletion of the PH-like domain totally abolishes the GTPase activity of the mutant. The DLP-1 G350D and the R365S mutations do not markedly impact DLP-1 tetramer, nor are the reduced GTPase activities a consequence of the loss of the protein's quaternary structure
additional information
analysis of nucleotide binding, dimerization, and GTPase activities of the enzyme mutants, overview
additional information
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analysis of nucleotide binding, dimerization, and GTPase activities of the enzyme mutants, overview
additional information
identification of mutations of the enzyme involved in centronuclear myopathy and Charcot-Marie-Tooth peripheral neuropathy, genotype-phenotype correlations, overview
additional information
recombinant short isoform of OPA1 (discussed below) assembles into higher order oligomers on the surface of cardiolipin-containing liposomes
additional information
Drp1-A-only (712 aa, 699 aax0413-aa A-insert) and Drp1-B-only (742 aa, 755 aa, 13-aa A-insert) are introduced in the Drp1-short isozyme. A- and B-insert sequences both suppress Drp1 GTPase activity, with the B-insert exerting the most dominant inhibitory effect on these interactions
additional information
engineering of dynamin constructs locked in either the closed or open state by chemical cross-linking or deletion mutagenesis. Design of dynamin mutants to restrict the PHD in the closed (Dyn1Closed) or open (Dyn1DELTADELTA) state. The stimulation of GTPase activity of Dyn1DELTADELTA mutant by liposomes is reduced compared to the wild-type enzyme. Ability of wild-type Dyn1, and mutant Dyn1CC and Dyn1Closed to catalyze membrane fission and vesicle release from SUPER templates, overview
additional information
gene DNM2 knockout by RNAi in T24 cells
additional information
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gene DNM2 knockout by RNAi in T24 cells
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partial shRNA suppression of endogenous Drp1 (gDrp-U2OS). GFP-Drp1 functionally compensates for endogenous Drp1 in these cells. gDrp-U2OS cells maintain 1.64fold total Drp1 levels compared to control U2OS cells, with 56% endogenous Drp1 and 44% GFP-Drp1. The fission rates of control U2OS and gDrp1-U2OS cells are statistically similar. A second clone displaying undetectable endogenous Drp1 levels and GFP-Drp1 levels about 3.5fold higher than control Drp1 levels shows similar mitochondrial fission frequency compared to control cells. By live-cell confocal microscopy, much of the GFP-Drp1 in gDrp-U2OS cells appears diffuse in the cytoplasm
additional information
the enzyme is cloned with Tom20 used as an N-terminal mitochondrial outer membrane anchor, or amino acids 131-155 of yeast Fis1 used as a C-terminal mitochondrial outer membrane anchor
additional information
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construction of neurolastin knockout mice
additional information
GFP-dynamin-2-(1-786), a truncated mutant lacking a C-terminal portion of the proline rich domain, localizes along microtubules in interphase HeLa cells
additional information
Drp1-A-only (712 aa, 699 aax0413-aa A-insert) and Drp1-B-only (742 aa, 755 aa, 13-aa A-insert) are introduced in the Drp1-long isozyme. A- and B-insert sequences both suppress Drp1 GTPase activity, with the B-insert exerting the most dominant inhibitory effect on these interactions
additional information
truncation of the proline/arginine-rich domain (PRD) of isozyme dynamin2
additional information
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construction of mutant Sey1-DELTATM by replacement of the transmembrane domains of Sey1, amino acids 681-727, with a 12-amino acid linker, the mutant rans as a monomer in the absence of nucleotide or in the presence of GDP but as a dimer in the presence of GDP and AlFx as a mimic of the transition state of nucleotide hydrolysis
additional information
recombinant expression of human enzyme Drp1 from plasmid pRS415-DNM1 in Saccharomyces cerevisiae strain JSY9612 lacking all fission proteins (MATa, can1, ade2, trp1, ura3, his3, leu2, pep4::HIS3, prb1::LEU2, bar1::HISG, lys2::GAL1/10-GAL4), coexpression with Saccharomyces cerevisiae mitochondrial fission 1 protein, Fis1 (UniProt ID P40515). Identification of the minimal combination of DRPs and adaptors sufficient for mitochondrial fission. Yeast Fis1 is dispensable for mitochondrial membrane scission. Mdv1, Mff, and MiDs paired individually with their respective DRPs are interchangeable, in that each is sufficient to catalyze fission. Importantly, coassembly of an MiD protein with Drp1 dramatically decreases the diameter of the Drp1 structures formed
additional information
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recombinant expression of human enzyme Drp1 from plasmid pRS415-DNM1 in Saccharomyces cerevisiae strain JSY9612 lacking all fission proteins (MATa, can1, ade2, trp1, ura3, his3, leu2, pep4::HIS3, prb1::LEU2, bar1::HISG, lys2::GAL1/10-GAL4), coexpression with Saccharomyces cerevisiae mitochondrial fission 1 protein, Fis1 (UniProt ID P40515). Identification of the minimal combination of DRPs and adaptors sufficient for mitochondrial fission. Yeast Fis1 is dispensable for mitochondrial membrane scission. Mdv1, Mff, and MiDs paired individually with their respective DRPs are interchangeable, in that each is sufficient to catalyze fission. Importantly, coassembly of an MiD protein with Drp1 dramatically decreases the diameter of the Drp1 structures formed
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a 6-His N-terminal-tagged human dynamin2, lacking the C-terminal proline-rich domain, is constructed, cloned into the pET28a vector for expression in Escherichia coli BL21DE3 cells
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a CHO-K1 cDNA library in the pSPORT vector is screened, the PCR product, derived from a positive clone, is cloned using the vectors pcDNA3.1Zeo+Myc6-, pcDNA3.1Zeo+Flag-, pcDNA3.1Zeo+HA2-, and pGEX6P-2, DLP1 cDNA from ZP121 is subcloned into pGEM-Teasy
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adenovirus expressing the dynamin mutant K44A is constructed
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DNA encoding the full-length Dnm1 protein is cloned into the pMALc2x vector for expression in Escherichia coli Rosetta cells
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Dyn1 expression in bovine adrenal chromaffin cells, coexpression with granule marker VMAT2-pH, the amount of dynamin on the plasma membrane in dynamin-transfected cells was increased 2.5 to 3.5 times compared with endogenous dynamin in nontransfected cells
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expressed in a fibroblastoid cell line and in embryonic stem cells
expressed in HEK-293 cells
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expressed in umbilical cord blood CD34+ cells
expression in COS-7 cells
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expression of dynamin II in Tn5 cells
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expression of GFP-tagged or V5/His-tagged wild-type and K44A mutant dynamin 2aa in HeLa cells
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expression of GST-tagged wild-type and mutant GST-SEY1 in Escherichia coli strain BL21
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expression of His-tagged DLP-1 isozyme 2 in Escherichia coli strain C41 (DE3)
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expression of wild-type and K44A mutant dynamin in HeLa cells
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expression of wild-type and K44A mutant dynamin-1 in HeLa cells and in Sf9 cells
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for identification of the EDR3 gene a cosmid library using BAC F27H5 DNA is constructed, for investigation of the subcellular localization a green fluorescent protein fusion to the N-terminus of DRP1E is used
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gene Dnm1, recombinant expression of C-terminally His6-tagged isozyme Dyn1 in Spodoptera frugiperda Sf9 cells
gene DNM1, recombinant expression of Drp1 containing an N-terminal PreScission protease cleavage site and a FLAG-One-Strep-tag (IBA) from plasmid pRS415-DNM1 in Saccharomyces cerevisiae strain JSY9612 lacking all fission proteins (MATa, can1, ade2, trp1, ura3, his3, leu2, pep4::HIS3, prb1::LEU2, bar1::HISG, lys2::GAL1/10-GAL4), coexpression with Saccharomyces cerevisiae mitochondrial fission 1 protein, Fis1 (UniProt ID P40515)
gene DNM1, recombinant expression of the dynamin 1 GTPase domain GG1 from modified pGEX-4T1 vector containing a TEV protease site. The fragments are connected by a linker composed of eight amino acid residues (KHGTDSRV) in Escherichia coli strain BL21 (DE3)
gene DNM2, enzyme expression analysis
gene DNM2, enzyme expression analysis, recombinant expression of GFP-tagged isozyme dynamin2 in human T24 cells
gene Dnm2, recombinant expression of C-terminally His6-tagged isozyme Dyn2 in Spodoptera frugiperda Sf9 cells
gene Dnm3, recombinant expression of C-terminally His6-tagged isozyme Dyn3 in Spodoptera frugiperda Sf9 cells
gene DNMTL1, recombinant expression of the splice variants of Drp1 in Escherichia coli strain BL21 Star (DE3)
gene for dynamin1, expression in HEK293-cre4 cells
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gene Rnf112, recombinant expression of C-terminally HA-tagged enzyme in transgenic C83S/C103S mutant mice and in HeLa cells, and of GFP-tagged enzyme from pEGFP-N1 vector in transgenic mice
His-tagged dynamin I is expressed in Escherichia coli Rosetta2 (DE3) cells
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human dynamin is expressed in SF9 insect cells, using the Bac-to-Bac baculovirus expression system a full-length cDNA encoding human dynamin1 containing a 6His-tag is subcloned into pFastBac, a bacmid is generated after transposition in Escherichia coli
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into the pFLAG-CMV-2 vector, five functional dynamin domains, GTPase, Middle, pleckstrin homology, GTPase effector and proline rich, are subcloned into pGEX-4T2
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into the pT-Adv vector, into pET-15b for expression in Escherichia coli BL21DE3codon-plus cells, a 711 bp fragment corresponding to the GTPase N-terminal domain into pET-22b, and into the pSynXIV VI+X3 vector for recombinat expression in the BEV system
overexpression in Chineses hamster ovary cells
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overexpression of human neuronal dynamin in Sf9 insect cells
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recombinant expression of C-terminally His6-tagged wild-type and mutants of DNM1L isoform 2
recombinant expression of GST- and His-tagged MxA in Escherichia coli strain BL21(DE3)
recombinant expression of HA-tagged neurolastin in HEK cells, recombinant expression of GST-tagged wild-type and mutant enzymes in HeLa cells
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recombinant expression of His6-tagged or FLAG-tagged wild-type and mutant enzymes in HeLa cells
recombinant expression of N-terminally Strep-tagged Drp1 with an HRV3C protease site from pET16b vector in Escherichia coli strain BL21 Star (DE3), stable recombinant expression of GFP-tagged DrpI in U2OS cells with partial shRNA suppression of endogenous Drp1 (gDrp-U2OS), GFP-Drp1 functionally compensates for endogenous Drp1 in these cells
recombinant expression of nucleotide-free GTPase-GTPase effector domain fusion protein of enzyme Drp1, and wild-type and mutant full-length enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of the GST-tagged chimeric fusion protein of AtDRP1A fusion protein in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
recombinant expression of truncated enzyme Sey1p(1-692) in Escherichia coli, recombinant expressioj of Myc-tagged scSey1p in COS-7 cells and immunolocalization study
the cDNA of rat Drp1 is subcloned into pEGFP-N1 and p3xFLAG-CMV-10 for transfection of HeLa cells, and in pET28a for expression in Escherichia coli
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the full-length mouse dynamin-1 cDNA isolated from retina is subcloned into the pGEX-2TK vector, the construct is used to generate three different dynamin-1 domain constructs, the N-terminal domain, aa 1-520, the proline-rich domain, aa 750-814, and the C-terminal domain, aa 521-814
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the vectors pcDNA3.1 and pADT3T7tet are used, recombinant adenoviruses are produced in HEK293-Cre cells
wild-type and mutant dynamin is expressed using the baculovirus pBac 4 system, expression in COS-7 cells
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wild-type mOPA1 and its mutants are subcloned into the mammalian expression vector pCNX2 for transfection of COS-7 cells
expressed in a fibroblastoid cell line and in embryonic stem cells
expressed in a fibroblastoid cell line and in embryonic stem cells
gene DNMTL1, recombinant expression of the splice variants of Drp1 in Escherichia coli strain BL21 Star (DE3)
gene DNMTL1, recombinant expression of the splice variants of Drp1 in Escherichia coli strain BL21 Star (DE3)
the vectors pcDNA3.1 and pADT3T7tet are used, recombinant adenoviruses are produced in HEK293-Cre cells
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the vectors pcDNA3.1 and pADT3T7tet are used, recombinant adenoviruses are produced in HEK293-Cre cells
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