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Information on EC 3.6.4.6 - vesicle-fusing ATPase
for references in articles please use BRENDA:EC3.6.4.6
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EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.4 Acting on acid anhydrides to facilitate cellular and subcellular movement
3.6.4.6 vesicle-fusing ATPase
IUBMB Comments
A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger’s syndrome.
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
- 3.6.4.6
- snare
-
exocytosis
- syntaxins
- synaptic
- proteasome
-
disassembly
- snap-25
- endosomal
-
neurotransmitter
-
vesicle-associated
-
traffic
-
t-snares
- synaptobrevin
-
presynaptic
- atpases
-
neurotoxin
-
escrt-iii
-
exocytic
-
synaptosome-associated
-
multivesicular
- synapses
-
er-associated
- vamp
-
escrts
- synaptotagmins
-
snare-mediated
- botulinum
-
homotypic
-
cargo
-
dc-stamp
-
reticulum-associated
- nfatc1
- tetanus
-
valosin-containing
-
rankl-induced
-
ampars
-
retrotranslocation
-
four-helix
-
intra-golgi
-
fusogenic
-
neurosecretion
-
exocyst
-
3.6.1.3
-
autophagosome-lysosome
- peroxins
-
bonts
- medicine
- rab3a
-
tail-anchored
- oscar
-
ca2+-triggered
showSynonyms
n-ethylmaleimide-sensitive factor, cdc48, aaa-atpase, n-ethylmaleimide-sensitive fusion protein, atp6v0d2, n-ethylmaleimide sensitive factor, sec18p, sec18, cdc48p, pex1p, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAA ATPase Vps4
AAA-type ATPase
ATP phosphohydrolase
ATPase
ATPase N-ethylmaleimide sensitive factor
Cdc48
dNSF1
LRD6-6
N-ethylmaleimide sensitive factor
N-ethylmaleimide sensitive fusion protein
N-ethylmaleimide sensitive-factor
N-ethylmaleimide-sensitive factor
N-ethylmaleimide-sensitive fusion protein
NEM-sensitive fusion protein
NSF
NSF protein
NSF-1
-
there are two NSF-1 isoforms, which are expressed in distinct tissues through two separate promoters
p97
p97ATPase
peptide p97
essential chaperone in endoplasmic reticulum-associated degradation and organelle biogenesis, contains two ATPases associated with various cellular activities domains (D1 and D2)
Pex1p
Pex6p
SEC18 gene product
SKD1
SKD2 protein
-
-
-
-
Sso0909
SsoVps4
triple-A ATPase
vacuolar protein sorting 4
VCP
vesicle-fusing ATPase
Vesicular-fusion protein NSF
-
-
-
-
Vps4
Vps4p
Vps4p AAA ATPase
N-ethylmaleimide sensitive fusion protein
-
-
-
-
NEM-sensitive fusion protein
-
-
-
-
Vps4p
-
a type I ATPase associated with a variety of cellular activities ATPase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
-
ATP + H2O = ADP + phosphate
Vps4 disassembles the ESCRT-III protein polymer, thereby changing the morphology of the underlying membrane
-
ATP + H2O = ADP + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (vesicle-fusing)
A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (_A_TPase _a_ssociated with a variety of cell _a_ctivities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
-
Substrates: ATPase N-ethylmaleimide sensitive factor may be a common feature in the triggering/regulation of membrane merging during mammalian acrosome reaction
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: the VCP/Cdc48p homologues C41C4.8 and C06A1.1, AAA chaperones, may play a protective role in polyglutamine aggregation
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: essential requirement for NSF in the organization of myelinated axons
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: dNSF-1 is involved in disassembling SNARE-complexes after fusion and before endocytosis
Products: dNSF-1 is involved in disassembling SNARE-complexes after fusion and before endocytosis
?
ATP + H2O
ADP + phosphate
-
Substrates: NSF is important in vesicular trafficking, but neural expression of a dominant negative form of NSF2 induces an unexpected overgrowth of the DRosophila larval neuromuscular synapse
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: a central function of Helar-NSF in developmental process through regulating neurohormonr release
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: the enzyme plays an essential role in intracellular membrane transport events
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: Pex1p possesses two distinct oligomeric forms, a homo-oligomer in the cytosol and a hetero-oligomer on peroxisome membranes, possibly playing distinct functions in peroxisome biogenesis
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: involved in membrane transport through endosome
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: ATPase N-ethylmaleimide sensitive factor may be a common feature in the triggering/regulation of membrane merging during mammalian acrosome reaction
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: NSF is a critical regulator of leukocyte trafficking in vivo
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: N-ethylmaleimide-sensitive factor is required for the synaptic incorporation and removal of 2-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors during cerebellar long-term depression
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: PEX1 is indispensable for biogenesis and maintenance of the peroxisome
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: the enzyme plays a crucial role in the fusion of vesicles with target membranes. NSF-SNAP complexes may be involved in the disassembly of coiled-coil-mediated interactions underlying not only SNARE complexes but also other forms of stable oligomers, and the C-terminal membrane anchoring of NSF-SNAP targets may be mechanistically involved in the dissociation process
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: coordinated action of NSF and PKC regulates GABAB receptor signaling efficacy
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
-
Substrates: ATP in form of MgATP2-
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: Vsp4 is an AAA ATPase which plays a key role in sorting of multivesicular bodies and facilitates transport through endosomes. The beta-domain of Vsp4p plays a critical role in the formation of a Vsp4p ATPase complex that is functional in vivo. The formation of the latter may be a prerequisite for interaction with Vta1p
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
-
Substrates: Vps4 disassembles the ESCRT-III protein polymer, thereby changing the morphology of the underlying membrane. The disassembly reaction causes the ESCRT-III subunits to regain the monomeric conformational state, which is the high-energy state that is poised to reassemble again into the ESCRT-III oligomer for subsequent rounds of membrane scission. When assembled, Vps4 progresses through many ATP hydrolysis cycles without dissociation
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: Vps4 disassembles the ESCRT-III protein polymer, thereby changing the morphology of the underlying membrane
Products: -
Products: -
?
additional information
?
-
-
Substrates: modeling of NSF-mediated disassembly in which the reaction is initiated by a 1:1 interaction between alpha-SNAP and the ternary SNARE complex, followed by NSF binding. Subsequent additional alpha-SNAP binding events may occur as part of a processive disassembly mechanism
Products: -
Products: -
?
additional information
?
-
Substrates: UBX-domain containing cytoplasmic Dictyostelium protein UBXD9 is identified as p97 interaction partner
Products: -
Products: -
?
additional information
?
-
Substrates: UBX-domain containing human protein UBXDTUG/ASPL/UBXD9 is identified as p97 interaction partner
Products: -
Products: -
?
additional information
?
-
-
Substrates: UBX-domain containing human protein UBXDTUG/ASPL/UBXD9 is identified as p97 interaction partner
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity measurement by malachite green-based colorimetric method
Products: -
Products: -
-
additional information
?
-
-
Substrates: activity measurement by malachite green-based colorimetric method
Products: -
Products: -
-
additional information
?
-
-
Substrates: the tombusvirus p33 replication protein interacts with Vps4p and three ESCRT-III proteins
Products: -
Products: -
?
additional information
?
-
Substrates: residues from helix 5 of the Vps2p subunit of ESCRT-III bind to the central pore of an asymmetric Vps4p hexamer in a manner that is dependent upon the presence of flexible nucleotide analogues that can mimic multiple states in the ATP hydrolysis cycle, quantitative binding studies. Vps2p helix 5 peptides bind the Vps4p ATPase cassette. Vps4 substrates are initially recruited by an MIM-MIT interaction that activates the Vps4 central pore to engage substrates and generate force, thereby triggering ESCRT-III disassembly. The Vps4p hexamer binds a single peptide
Products: -
Products: -
?
additional information
?
-
-
Substrates: the tombusvirus p33 replication protein interacts with Vps4p and three ESCRT-III proteins
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
-
Substrates: ATPase N-ethylmaleimide sensitive factor may be a common feature in the triggering/regulation of membrane merging during mammalian acrosome reaction
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: the VCP/Cdc48p homologues C41C4.8 and C06A1.1, AAA chaperones, may play a protective role in polyglutamine aggregation
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: essential requirement for NSF in the organization of myelinated axons
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: NSF is important in vesicular trafficking, but neural expression of a dominant negative form of NSF2 induces an unexpected overgrowth of the DRosophila larval neuromuscular synapse
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: a central function of Helar-NSF in developmental process through regulating neurohormonr release
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: the enzyme plays an essential role in intracellular membrane transport events
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: Pex1p possesses two distinct oligomeric forms, a homo-oligomer in the cytosol and a hetero-oligomer on peroxisome membranes, possibly playing distinct functions in peroxisome biogenesis
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: ATPase N-ethylmaleimide sensitive factor may be a common feature in the triggering/regulation of membrane merging during mammalian acrosome reaction
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: NSF is a critical regulator of leukocyte trafficking in vivo
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: N-ethylmaleimide-sensitive factor is required for the synaptic incorporation and removal of 2-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors during cerebellar long-term depression
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: PEX1 is indispensable for biogenesis and maintenance of the peroxisome
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: the enzyme plays a crucial role in the fusion of vesicles with target membranes. NSF-SNAP complexes may be involved in the disassembly of coiled-coil-mediated interactions underlying not only SNARE complexes but also other forms of stable oligomers, and the C-terminal membrane anchoring of NSF-SNAP targets may be mechanistically involved in the dissociation process
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: coordinated action of NSF and PKC regulates GABAB receptor signaling efficacy
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
-
Substrates: Vps4 disassembles the ESCRT-III protein polymer, thereby changing the morphology of the underlying membrane. The disassembly reaction causes the ESCRT-III subunits to regain the monomeric conformational state, which is the high-energy state that is poised to reassemble again into the ESCRT-III oligomer for subsequent rounds of membrane scission. When assembled, Vps4 progresses through many ATP hydrolysis cycles without dissociation
Products: -
Products: -
?
additional information
?
-
-
Substrates: modeling of NSF-mediated disassembly in which the reaction is initiated by a 1:1 interaction between alpha-SNAP and the ternary SNARE complex, followed by NSF binding. Subsequent additional alpha-SNAP binding events may occur as part of a processive disassembly mechanism
Products: -
Products: -
?
additional information
?
-
Substrates: UBX-domain containing cytoplasmic Dictyostelium protein UBXD9 is identified as p97 interaction partner
Products: -
Products: -
?
additional information
?
-
-
Substrates: the tombusvirus p33 replication protein interacts with Vps4p and three ESCRT-III proteins
Products: -
Products: -
?
additional information
?
-
Substrates: residues from helix 5 of the Vps2p subunit of ESCRT-III bind to the central pore of an asymmetric Vps4p hexamer in a manner that is dependent upon the presence of flexible nucleotide analogues that can mimic multiple states in the ATP hydrolysis cycle, quantitative binding studies. Vps2p helix 5 peptides bind the Vps4p ATPase cassette. Vps4 substrates are initially recruited by an MIM-MIT interaction that activates the Vps4 central pore to engage substrates and generate force, thereby triggering ESCRT-III disassembly. The Vps4p hexamer binds a single peptide
Products: -
Products: -
?
additional information
?
-
-
Substrates: the tombusvirus p33 replication protein interacts with Vps4p and three ESCRT-III proteins
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the protein p47 forms a tight complex with p97, which is essential for the in vitro Golgi reassmbly
-
additional information
-
Vps4 and its cofactor Vta1p/LIP5 function in membrane remodeling events that accompany cytokinesis, multivesicular body biogenesis, and retrovirus budding
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
NSF is a Ca2+-binding protein, GluR2-NSF interactions are inhibited by the presence of 15 micromol/l Ca2+
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ist1
-
subunit of endosomal sorting complex required for the transport III, maximal inhibition at 0.008 or less mM
-
additional information
-
phosphorylation by Pctaire1 attenuates the hexamerization of NSF
-
additional information
-
phosphorylation by Pctaire1 attenuates the hexamerization of NSF
-
additional information
binding of substrates to the central pore of the Vps4 ATPase is autoinhibited by the microtubule interacting and trafficking (MIT) domain, substrate engagement is autoinhibited by the Vps4p-MIT-domain and the inhibition is relieved by binding of either Type 1 or Type 2 MIM elements, which bind the Vps4p MIT domain through different interfaces
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ist1
-
addition of the endosomal sorting complex required for the transport III (ESCRT-III) subunit binding partner of Ist1, Did2, converts ESCRT-III subunit Ist1 from an inhibitor to a stimulator of the enzyme (maximal stimulation at 0.008 or less mM). Mutants Ist1(L168A/Y172A) and Ist1(K135A) hyperstimulate enzyme ATPase activity
-
LIP5F388A
a weak SKD1 interactor, complements the lip5 mutant for heat and salt stress tolerance, most likely due to its overexpression driven by the strong CaMV 35S promoter in the transgenic plants
-
Lyst-interacting protein5
LIP5, interacts strongly with enzyme SKD1 and stimulates the ATPase activity of the enzyme by 4 to 5fold. LIP5 is a positive regulator of enzyme SKD1 in multivesicular bodies biogenesis and is a critical target of the mitogen-activated protein kinases MPK3 and MPK6 and plays an important role in the plant immune system. Disruption of LIP5 causes compromised tolerance to both heat and salt stresses. When compared with wild-type plants, lip5 mutants accumulate increased levels of ubiquitinated protein aggregates and NaCl under heat and salt stresses, respectively. LIP5 is regulated by phosphorylation, overview. Mutation of MPK phosphorylation sites in LIP5 does not affect its interaction with SKD1 but reduces its stability and, as a result, compromises its ability to complement the basal resistance of the lip5 mutants
-
SNARE complex
-
SNARE-stimulated ATP hydrolysis, all four SNARE complexes similarly stimulate the steady-state rate of NSF-catalyzed ATP hydrolysis activity, suggesting that the stimulation of ATPase activity is independent of SNARE primary sequence variation and N-terminal domain architecture
-
Vps2p helix 5 peptide C
stimulates Vps4p ATPase activity and stabilizes the hexamer
-
additional information
-
SKD1 E Vps proteins SBP1 and mVps2 interact with SKD1
-
additional information
-
the protein VCIP135 is essential for p97/p47-mediated membrane fusion
-
additional information
-
Vps4p directly binds Vps20p and Vta1p in vitro
-
additional information
-
activity is dependent upon hexamerisation
-
additional information
-
Ist1, Did2, Vta1 and Vps60 function as a regulatory system that ensures proper recruitment and assembly of ATPase Vps4 on the ESCRT-III protein complex. Directly or indirectly these factors affect ATPase activity of Vps4, suggesting that they also regulate the Vps4 ESCRT-III disassembly activity
-
additional information
binding of substrates to the central pore of the Vps4 ATPase is activated by microtubule interacting and trafficking interacting motifs (MIMs)
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.85
ATP
-
higher order oligomer of the enzyme, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
210576, 210577, 210578, 210579, 210585, 656346, 656763, 667040, 667294, 668578, 669996, 670662, 687536, 687629
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
adult, CDC-48.1:GFP fusion construct is expressed from embryos through to adult worms
brenda
-
N-ethylmaleimide sensitive factor is required for fusion of the Caenorhabditis elegans uterine anchor cell
brenda
additional information
-
mRNA for Hez-NSF is present throughout the embryonic, larval and pupal development
brenda
-
CDC-48.1:GFP fusion construct is expressed from embryos through to adult worms
brenda
-
NFS is primarily expressed in the developing nervous system. At the 14 somite stage, nsf is expressed within cells of the developing trigeminal ganglia, anterior spinal cord, and forebrain. At 20 somites, transcripts are detectable in additional cranial ganglia and throughout the length of the developing spinal cord. By 30 hours post-fertilization, nsf is also visible in regions of the developing midbrain and hindbrain and in the posterior lateral line ganglia. At 48 hours post-fertilization, expression persistes in spinal cord and is present throughout mots of the developing brain and eyes, while at 72 hours post-fertilization, spinal cord expression is less evident. Expression in the posterior lateral line ganglia persists to at least 72 hours post-fertilization
brenda
-
predominantly expressed in larval and adult nervous system, dNSF-1 is abundant in synaptic vesicle fraction and may have a function in synaptic vesicle release
brenda
additional information
-
the expression of two p97 homologues CDC-48.1 and CDC-48.2 is differently regulated and independent of each other
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
localizes mainly in acrosome. ATPase N-ethylmaleimide sensitive factor may be a common feature in the triggering/regulation of membrane merging during mammalian acrosome reaction
-
brenda
-
localizes mainly in acrosome. ATPase N-ethylmaleimide sensitive factor may be a common feature in the triggering/regulation of membrane merging during mammalian acrosome reaction
-
brenda
-
Pex1p possesses two distinct oligomeric forms, a homo-oligomer in the cytosol and a hetero-oligomer on peroxisome membranes, possibly playing distinct functions in peroxisome biogenesis
brenda
-
Pex1p and Pex6p form a stable higher-molecular-mass complex in the cytosol
brenda
-
Pex6p and Pex1p form a stable higher-molecular-mass complex in the cytosol
brenda
NSF requires a peripheral membrane protein to bind Golgi membranes
brenda
-
NSF requires a peripheral membrane protein to bind Golgi membranes
brenda
-
NSF requires a peripheral membrane protein to bind Golgi membranes
brenda
-
NSF requires a peripheral membrane protein to bind Golgi membranes
brenda
-
N-terminal domain of PEX1 is one of the functional modules for membrane binding
brenda
-
NSF requires a peripheral membrane protein to bind membranes
brenda
-
NSF requires a peripheral membrane protein to bind membranes
brenda
-
the Walker A1 motif of Pex1p is essential for Pex1p-pex6p interaction and Pex1p targeting to peroxisomes
brenda
-
membrane, Pex1p possesses two distinct oligomeric forms, a homo-oligomer in the cytosol and a hetero-oligomer on peroxisome membranes, possibly playing distinct functions in peroxisome biogenesis
brenda
-
dNSF-1 is absoluteley required for synaptic transmission in the eye
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
enzyme vacuolar protein sorting 4, Vps4, belongs to the AAA ATPases. Vps4 forms a hexameric complex that disassembles ESCRT-III, allowing recycling of its components, and also plays an active role in scission of the vesicle neck. Vps4 is required for epidermal growth factor receptor signaling even in the absence of Shibire, the Dynamin that internalizes epidermal growth factor receptor from the plasma membrane. In ovarian follicle cells, in contrast, Vps4 does not affect epidermal growth factor receptor signaling, although it is still essential for receptor degradation, Vps4 is not required for EGFR or Notch signaling in follicle cells. Enzyme Vps4 can promote epidermal growth factor receptor activity through an endocytosis-independent mechanism, a non-endocytic and cell type-dependent mechanism. Protein Vps4 is the only energy-utilizing ESCRT component
evolution
human and Dictyostelium p97 share 81% identity and 89% similarity on the amino acid sequence level and have an almost identical order and composition of secondary structure elements
evolution
human and Dictyostelium p97 share 81% identity and 89% similarity on the amino acid sequence level and have an almost identical order and composition of secondary structure elements
evolution
-
the enzyme belongs to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily
evolution
-
the enzyme belongs to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily
-
malfunction
-
inhibition of p97, but not NSF ATPase can be associated with ER/Golgi disruption and apoptosis in alphaSNAP-depleted epithelial cells. AlphaSNAP knockdown does not affect p97 expression, it perturbes a balance between key p97-binding partners. Specifically, expression of syntaxins 5 and 18 are significantly decreased
malfunction
-
deletion of Vps4p in yeast leads to the formation of crescent-like membrane structures instead of the characteristic spherule and vesicle-like structures
malfunction
photoreceptors are largely absent from Vps4 mutant clones in the eye disc, the resulting mutant R8 photoreceptors fail to recruit surrounding cells to differentiate as R1-R7 photoreceptors. Loss of Vps4 disrupts the epidermal growth factor receptor, EGFR, pathway. In imaginal disc cells deficient for enzyme Vps4, EGFR and other receptors accumulate in endosomes, and EGFR target genes are not expressed
malfunction
heterozygous missense mutations of p97 cause at least five human neurodegenerative disorders, i.e. R93C, R155H, and R155C mutations. All human p97 mutations lead to an increase in ATPase activity. p97 point mutations lead to differences in enzymatic activities and molecular interactions, which in the long-term result in a late-onset and progressive multisystem disease
malfunction
-
subunit Atp6v0d2-deficient macrophages have augmented mitochondrial damage, enhanced inflammasome activation and reduced clearance of Salmonella typhimurium
malfunction
p97 point mutations lead to differences in enzymatic activities and molecularinteractions, which in the long-term result in a late-onset and progressive multisystem disease
malfunction
-
rice spl mutant named spl-A (spotted leaf mutant from A814) shows autoimmunity, broad-spectrum disease resistance and growth deterioration including decreased rice quality. A single nucleotide mutation of C1144T leads to change of the 382nd proline to serine in the gene encoding the ATPases associated with diverse cellular activities (AAA)-type ATPase LRD6-6, the mutation is responsible for the phenotype of the spl-A mutant. The immune response of spl-A is activated, and the growth and grain quality are deteriorated
malfunction
-
deletion of Vps4p in yeast leads to the formation of crescent-like membrane structures instead of the characteristic spherule and vesicle-like structures
-
malfunction
-
rice spl mutant named spl-A (spotted leaf mutant from A814) shows autoimmunity, broad-spectrum disease resistance and growth deterioration including decreased rice quality. A single nucleotide mutation of C1144T leads to change of the 382nd proline to serine in the gene encoding the ATPases associated with diverse cellular activities (AAA)-type ATPase LRD6-6, the mutation is responsible for the phenotype of the spl-A mutant. The immune response of spl-A is activated, and the growth and grain quality are deteriorated
-
metabolism
-
vesicle trafficking in eukaryotic cells is facilitated by SNARE-mediated membrane fusion. The ATPase N-ethylmaleimide-sensitive factor, NSF, and the adaptor protein soluble NSF attachment protein, alpha-SNAP, disassemble all SNARE complexes formed throughout different pathways
metabolism
-
the enzyme functions in membrane remodelling and is the only ATP consuming factor of the endosomal sorting complex required for transport (ESCRT) machinery. ATP hydrolysis is required to disassemble ESCRT-III polymers, which releases individual ESCRT-III subunits back into the cytoplasm
physiological function
-
Vps4 functions together with the protein complex ESCRT-III in membrane fission
physiological function
the enzyme provides energy for the ESCRT (endosomal sorting complexes required for transport) pathway
physiological function
-
Vps4p is required for the formation of spherule-like structures induced by tombusvirus replication proteins in yeast. Key role for the conserved Vps4p AAA ATPase, whose canonical function is to disassemble the ESCRT complexes, i.e. endosomal sorting complexes required for transport, and recycle them from the membranes back to the cytosol. Vps4p is recruited to become a permanent component of the viral replicase complexes, it is co-localized with the viral dsRNA and contacts the viral (+)RNA in the intracellular membrane
physiological function
enzyme SKD1 is involved in multivesicular bodies biogenesis, the LIP5-regulated multivesicular bodies biogenesis, MVB, pathway also plays a critical role in plant responses to abiotic stresses. The critical role of LIP5 in plant tolerance to abiotic stresses is dependent on its ability to interact with the enzyme SKD1
physiological function
enzyme vacuolar protein sorting 4, Vps4, interacts with the endosomal sorting complexes required for transport, ESCRT-III, complex to drive the final step of intra-lumenal vesicles formation
physiological function
-
vesicle trafficking in eukaryotic cells is facilitated by SNARE-mediated membrane fusion. The ATPase N-ethylmaleimide-sensitive factor, NSF, and the adaptor protein soluble NSF attachment protein, alpha-SNAP, disassemble all SNARE complexes formed throughout different pathways. SNARE-stimulated ATP hydrolysis. Modeling of NSF-mediated disassembly in which the reaction is initiated by a 1:1 interaction between alpha-SNAP and the ternary SNARE complex, followed by NSF binding. Subsequent additional alpha-SNAP binding events may occur as part of a processive disassembly mechanism
physiological function
the endosomal sorting complexes required for transport (ESCRT) pathway drives reverse topology membrane fission events within multiple cellular pathways, including cytokinesis, multivesicular body biogenesis, repair of the plasma membrane, nuclear membrane vesicle formation, and HIV budding. The AAA ATPase Vps4 is recruited to membrane necks shortly before fission, where it catalyzes disassembly of the ESCRT-III lattice. Vps4 substrates are initially recruited by an MIM-MIT interaction that activates the Vps4 central pore to engage substrates and generate force, thereby triggering ESCRT-III disassembly. Vps2p helix 5 peptides bind the Vps4p ATPase cassette. Two-step model for disassembly of the ESCRT-III complex by Vps4, overview
physiological function
-
subunit ATP6V0D2 is a key component of macrophage-specific autophagosome-lysosome fusion machinery maintaining macrophage organelle homeostasis and, in turn, limiting both inflammation and bacterial infection. The enzyme subunit Atp6v0d2 inhibits inflammasome-dependent colitis. Subunit ATP6V0D1 but not ATP6V0D2 is required for lysosome acidification and maturation in macrophages. Subunit ATP6V0D2, but not ATP6V0D1, forms a complex with VAMP8 and STX17, and is required for the optimal stabilization of this complex in activated macrophages
physiological function
-
the enzyme remodels different endosomal sorting complex required for transport-III filaments or tubular structures. The enzyme catalyzes constriction of CHMP2A-3 tubular filaments leading to membrane constriction
physiological function
-
the enzyme remodels and disassembles endosomal sorting complex required for transport III
physiological function
-
the enzyme is intimately associated with the ESCRT machinery and is essential for the membrane scission cycle. The enzyme is recruited to scission sites by Vps2. By recycling Vps2, the enzyme promotes Snf7 polymerization. Thus, the enzyme is critical for the recycling of ESCRT-III and the replenishment of the soluble cytoplasmic pool
physiological function
-
the enzyme provides energy for the ESCRT (endosomal sorting complexes required for transport) pathway
-
physiological function
-
Vps4p is required for the formation of spherule-like structures induced by tombusvirus replication proteins in yeast. Key role for the conserved Vps4p AAA ATPase, whose canonical function is to disassemble the ESCRT complexes, i.e. endosomal sorting complexes required for transport, and recycle them from the membranes back to the cytosol. Vps4p is recruited to become a permanent component of the viral replicase complexes, it is co-localized with the viral dsRNA and contacts the viral (+)RNA in the intracellular membrane
-
additional information
UBX-domain containing human protein UBXDTUG/ASPL/UBXD9 is identified as p97 interaction partner. Human UBXD9 protein disassembles wild-type, but to a lesser extent mutant, p97 hexamers very efficiently into monomers. Enzyme p97 structure homology modelling using the crystal structure of mouse p97 (PDB entry 3cf2) as template
additional information
-
UBX-domain containing human protein UBXDTUG/ASPL/UBXD9 is identified as p97 interaction partner. Human UBXD9 protein disassembles wild-type, but to a lesser extent mutant, p97 hexamers very efficiently into monomers. Enzyme p97 structure homology modelling using the crystal structure of mouse p97 (PDB entry 3cf2) as template
additional information
UBX-domain containing Dictyostelium protein UBXD9 is identified as p97 interaction partner. Dictyostelium UBXD9 protein disassembles wild-type, but to a lesser extent mutant, p97 hexamers very efficiently into monomers. Enzyme p97 structure homology modelling using the crystal structure of mouse p97 (PDB entry 3cf2) as template
additional information
-
the conserved 382nd amino acid residue proline is essential for the full function of the AAA-type ATPase LRD6-6
additional information
-
the conserved 382nd amino acid residue proline is essential for the full function of the AAA-type ATPase LRD6-6
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42248
50000
42248
2 * 42248, calculated from sequence, the enzyme rapidly interconverts between multiple oligomeric states, it interconverts between dimers and hexamers in the presence of adenosine nucleotides
42248
6 * 42248, calculated from sequence, the enzyme rapidly interconverts between multiple oligomeric states, it interconverts between dimers and hexamers in the presence of adenosine nucleotides
50000
-
recombinant protein, determined by SDS-PAGE and immunoblot analysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homohexamer
oligomer
additional information
dimer
2 * 42248, calculated from sequence, the enzyme rapidly interconverts between multiple oligomeric states, it interconverts between dimers and hexamers in the presence of adenosine nucleotides
dimer
-
2 * 42248, calculated from sequence, the enzyme rapidly interconverts between multiple oligomeric states, it interconverts between dimers and hexamers in the presence of adenosine nucleotides
-
dimer
Vps4p dimers form two distinct heptameric rings and accommodate AAA cassettes in a head-to-head fashion, X-ray crystallography
dimer
-
the enzyme interconverts between dimers and hexamers in the presence of adenosine nucleotides
hexamer
-
3D structures of NSF in its functional cycle are reconstructed: NSF in the ATP state, which is capable of binding substrates, the 20S particle, consisting of the NSF hexamer, three alpha-SNAPs and the SNARE complex and NSF in the ADP state. These structures reveal that the two AAA+ domains of NSF, D1 and D2, are in a parallel arrangement in the full-length NSF hexamer, similarly to p97, as shown in its full-length hexamer crystal structures
hexamer
6 * 42248, calculated from sequence, the enzyme rapidly interconverts between multiple oligomeric states, it interconverts between dimers and hexamers in the presence of adenosine nucleotides
hexamer
-
6 * 42248, calculated from sequence, the enzyme rapidly interconverts between multiple oligomeric states, it interconverts between dimers and hexamers in the presence of adenosine nucleotides
-
hexamer
-
the enzyme interconverts between dimers and hexamers in the presence of adenosine nucleotides
hexamer
eukaryotic Vps4 enzymes comprise the N-terminal MIT domain, an about 40-residue linker, a two-domain AAA ATPase cassette, a beta-domain that is inserted within the small domain of the ATPase cassette, and a C-terminal helix that binds against the large ATPase domain. Vps4 functions as a higher-order oligomer
homohexamer
domain organization and structural information of Dictyostelium p97, overview. The N-terminal region comprising the CDC48 N and CDC48 2 domains is followed by the D1 and D2 domains and the C-terminal extension
oligomer
-
Pex1p possesses two distinct oligomeric forms, a homo-oligomer in the cytosol and a hetero-oligomer on peroxisome membranes, possibly playing distinct functions in peroxisome biogenesis. Interaction of Pex1p with Pex6p confers a conformatinal and dissociation of the Pex1p oligomer
additional information
addition of ATP but not ADP increases the oligomerized population of SKD1
additional information
-
Vps4 exhibits a dynamic structure that is regulated by the nucleotide-binding state. Oligomerization of the enzyme occurs at protein concentrations above 0.0005 mM in vitro whereas the concentration of Vps4 in vivo is 0.0002 mM. In the cytoplasm the enzyme is dimeric and exhibits no ATPase activity. It is recruited to membrane-associated ESCRT-III where it oligomerizes into the active enzyme
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, using 5% (w/v) polyethylene glycol 3350 and 100 mM MES (pH 6.0)
hanging-drop vapour-diffusion method. Preparation of crystals of the N-terminal domain of PEX1. The crystals belong to space group P3(1) or P3(2) with unit-cell parameters a = b = 63.5 A, c = 33.5 A, and contain one protein molecule per crystallographic asymmetric unit. 2.05 A resolution
-
sitting drop vapour diffusion method, at 19°C against a reservoir containing 0.1 M MES buffer (pH 5.9-6.5) and 0.8-1.9 M MgSO4
Vps4p complexes with and without their MIT N-terminal domains and Vta1p cofactors, hanging drop vapour diffusion method, using
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E329Q
-
in contrast to wild-type NFS E329Q mutant is enriched on various structures throughout the cell and is only minimally released by saponin permeabilization
E219K
R154C
naturally occurring mutation, constitutes variations in surface-exposed locations, but does not alter the ATPase activity
R154C/E219K
naturally occurring mutation, constitutes variations in surface-exposed locations. The E219K mutation leads to an almost complete loss of activity, which is partially recuperated in the R154C/E219K double-mutant indicating p97 inter-domain communication
R155C
naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity, and a twofold decreased kd for human protein UBXD9
R155H
naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity, no change in the kd value for human protein UBXD9
R93C
naturally occurring mutation, constitutes variations in surface-exposed locations and leads to increased ATPase activity and a twofold increased kd for human protein UBXD9
D100A
-
mutant to study the Ca2+ sensitivity of the interaction between NSF and the glutamate receptor subunit 2 of AMPAR
D142A
-
mutant to study the Ca2+ sensitivity of the interaction between NSF and the glutamate receptor subunit 2 of AMPAR
E153A
-
mutant to study the Ca2+ sensitivity of the interaction between NSF and the glutamate receptor subunit 2 of AMPAR
E235Q
-
no ATPase activity, mutation leads to perturbation of various membrane transports via endosomes
E305Q
-
mutant assembles into oligomer like wild-type, similar ATPase activity as wild-type
E578Q
-
mutant assembles into oligomer like wild-type, severely impaired ATPase activity
S569A
-
mutation of serine 569 to alanine abolishs the phosphorylation of D2 domain by active Pctaire1
P382S
K251A
K524A
the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme
R359A
the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme
R635A
the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme
S569A
-
mutation of serine 569 to alanine abolishs the phosphorylation of D2 domain by active Pctaire1
E233Q
E243A
site-directed mutagenesis, a pore loop mutant, displays essentially unchanged oligomerization, introducing E243A point mutation increases the affinity of peptide C binding by 3fold, shows reduced ATPase activity compared to the wild-type
E243A/E247A
site-directed mutagenesis, pore loop mutant, displays essentially unchanged oligomerization, the double mutant binds peptides 4fold (peptide C) or 10fold (peptide B) more tightly than wild-type Vps4p, shows reduced ATPase activity compared to the wild-type
E247A
site-directed mutagenesis, a pore loop mutant, displays essentially unchanged oligomerization, introducing E247A point mutation increases the affinity of peptide C binding by 4fold, shows reduced ATPase activity compared to the wild-type
E350Q
G89D
-
higher intrinsic ATPase activity than wild-type, no stimulation by Sec17
K179A
-
no ATP binding, enhanced binding to Vps20p and Vta1p in vitro
R241A
site-directed mutagenesis, a pore loop 2 mutant, does not bind peptides with appreciable affinity
R251A
site-directed mutagenesis, a pore loop 2 adjacent mutant, does not bind peptides with appreciable affinity
T240A
site-directed mutagenesis, a pore loop mutant, displays essentially unchanged oligomerization
W206A
site-directed mutagenesis, a pore loop 1 mutant, does not bind peptides with appreciable affinity
additional information
E219K
naturally occurring mutation, constitutes variations in surface-exposed locations
E219K
naturally occurring mutation, the E219K mutation leads to an almost complete loss of activity
P382S
-
naturally occurring mutation, single nucleotide mutation of C1144T, cloning of the Spl-A gene by combining map-based cloning strategy and BSA sequencing. The mutation impairs LRD6-6 ATPase activity and disrupts its interaction with endosomal sorting complex required for transport (ESCRT)-III subunits OsSNF7.1/7.2/7.3, and thus, leading to compromise of multivesicular bodies (MVBs)-mediated vesicle trafficking and accumulation of ubiquitinated proteins in both leaves and seeds of the rice spl mutant named spl-A. Therefore, the immune response of mutant spl-A is activated, and the growth and grain quality are deteriorated
P382S
-
naturally occurring mutation, single nucleotide mutation of C1144T, cloning of the Spl-A gene by combining map-based cloning strategy and BSA sequencing. The mutation impairs LRD6-6 ATPase activity and disrupts its interaction with endosomal sorting complex required for transport (ESCRT)-III subunits OsSNF7.1/7.2/7.3, and thus, leading to compromise of multivesicular bodies (MVBs)-mediated vesicle trafficking and accumulation of ubiquitinated proteins in both leaves and seeds of the rice spl mutant named spl-A. Therefore, the immune response of mutant spl-A is activated, and the growth and grain quality are deteriorated
-
K251A
the Walker A mutation to the D1 domain alone shows a moderate decrease in ATPase activity, has reduced affinity for nucleotide in the D1 domain and so contains little prebound ADP
K251A
the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme
E233Q
-
no ATP hydrolysis, enhanced binding to Vps20p and Vta1p in vitro
E233Q
-
a mutant protein with very low ATPase activity. In the presence of ADP recombinant mutant enzyme forms dimers. In contrast, the addition of ATP results in the formation of a large complex with at least ten subunits
additional information
construction of Vps4 knockout mutants, loss of Vps4 affects multiple signaling pathways, phenotypes, detailed overview
additional information
-
the spotted leaf mutant which we named spl-A (spotted leaf mutant from A814) is isolated from ethyl methanesulfonate (EMS) treated japonica rice A814 for its visible lesion mimic phenotype on the leaves when growing in the field. The mutation of the Spl-A locus has been previously reported as lesion mimic resembling (lmr), lesion resembling disease 6-6 (lrd6-6) and spotted leaf 4 (spl4) in rice
additional information
-
the spotted leaf mutant which we named spl-A (spotted leaf mutant from A814) is isolated from ethyl methanesulfonate (EMS) treated japonica rice A814 for its visible lesion mimic phenotype on the leaves when growing in the field. The mutation of the Spl-A locus has been previously reported as lesion mimic resembling (lmr), lesion resembling disease 6-6 (lrd6-6) and spotted leaf 4 (spl4) in rice
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-chelating column chromatography and Superdex gel filtration
Ni-NTA column chromatography, DEAE Sepharose column chromatography, and Superdex 75 gel filtration
Ni2+ Sepharose column chromatography, Q-Sepharose column chromatography, and Superdex 200 gel filtration
-
recombinant GST- and His6-tagged Vps4p and Vps4101437 from Saccharomyces cerevisiae strain BY4741
-
recombinant GST-tagged wild-type and mutant p97s from Escherichia coli by glutathione affinity and cleavage of the tag by PreScission protease
recombinant His6-tagged enzyme NSF from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant NSF is purified by nickel-nitrilotriacetic acid-agarose affinity chromatography
-
recombinant GST-tagged wild-type and mutant p97s from Escherichia coli by glutathione affinity and cleavage of the tag by PreScission protease
recombinant GST-tagged wild-type and mutant p97s from Escherichia coli by glutathione affinity and cleavage of the tag by PreScission protease
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA containing the NSF D1 ATPase domain is inserted into the pET28a vector for expression in Escherichia coli BL21 cells
-
constructing of a genomic library from the haploid yeast strain SD228-7 using the Escherichia coli-yeast shuttle vector pCS19
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
full-length, partial cDNA fragments and point mutations of mouse NSF are amplified by PCR and subcloned into different expression vectors including pGEX-6P-2, pETH-32, pcDNA3-His6, and pcDNA3-3HA
-
generation of recombinant truncated His-tagged LRD6-6(125-487)P382S (covering the ATPase domain) protein
-
isolation of PEX2 and PEX6 cDNA, Pex1p expressed in wild-type chinese hamster ovary cells, CHO-K1
-
recombinant expression of GST- and His6-tagged Vps4p and Vps4101437 in Saccharomyces cerevisiae strain BY4741
-
recombinant expression of GST-tagged wild-type and mutant p97 in Escherichia coli strain Arctic express RIL, coexpression with GST-tagged human UBXD9 protein in Escherichia coli in strain BL21Gold (DE3) pLysS
recombinant expression of GST-tagged wild-type and mutant p97 in Escherichia coli strain XL1 Blue, coexpression with GST-tagged Dictyostelium UBXD9 protein
recombinant expression of His6-tagged enzyme NSF in Escherichia coli strain BL21(DE3), coexpression of alpha-SNAP, VAMP2(1-96), syntaxin1A(1-265)-C145S/S249C/K253C, syntaxin1A(191-265)-C145S/S249C/K253C, and SNAP25A
-
SKD1 and GFP5 PCR-amplified fragments are cloned in pBSII KS+ and subsequently subcloned into pMZ215S, and in the binary vectors pCambia 1300 and pbinSRNACatN
-
the vectors YCplac111, pLexA, pET11d and pB42AD are used for cloning and expression of wild-type protein, single domains and various mutants
-
VPS4 gene cloned and overexpressed in Escherichia coli XL1-blue, using a GST fusion vector
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
thr expression of subunit ATP6V0D2 is most inhibited by the addition of lipopolysaccharide
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
HsPEX1 is the causative gene for peroxisome-deficiency autosomal recessive disorders like cerebro-hepato-renal Zellweger syndrome, neonatal adrenoleukodystrophy and infantile refsum disease
medicine
-
diagnosis, HsPex6p mutations are one of the causes of Zellweger syndrome
medicine
-
dysfunction of p97 has serious pathological consequences and has been implicated in a variety of cancers and neurodegenerative deseases
medicine
-
dysfunction of p97 has serious pathological consequences and has been implicated in a variety of cancers and neurodegenerative deseases
medicine
-
dysfunction of p97 has serious pathological consequences and has been implicated in a variety of cancers and neurodegenerative deseases
medicine
-
dysfunction of p97 has serious pathological consequences and has been implicated in a variety of cancers and neurodegenerative deseases
medicine
protozoa
-
dysfunction of p97 has serious pathological consequences and has been implicated in a variety of cancers and neurodegenerative deseases
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Confalonieri, F.; Duguet, M.
A 200-amino acid ATPase module in search of a basic function
Bioessays
17
639-650
1995
Saccharomyces cerevisiae, Sulfolobus acidocaldarius, Homo sapiens, Xenopus laevis, Candida albicans, Drosophila melanogaster, Cricetulus longicaudatus, Mus musculus
brenda
Finken-Eigen, M.; Roehricht, R.A.; Koehrer, K.
The VPS4 gene is involved in protein transport out of a yeast pre-vacuolar endosome-like compartment
Curr. Genet.
31
469-480
1997
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Schizosaccharomyces pombe
brenda
Babst, M.; Sato, T.K.; Banta, L.M.; Emr, S.D.
Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
EMBO J.
16
1820-1831
1997
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Schizosaccharomyces pombe
brenda
Patel, S.; Latterich, M.
The AAA team: related ATPases with diverse functions
Trends Cell Biol.
8
65-71
1998
Saccharomyces cerevisiae, Drosophila melanogaster (P54351), Mus musculus
brenda
Faber, K.N.; Heyman, J.A.; Subramani, S.
Two AAA family peroxins, PpPex1p and PpPex6p, interact with each other in an ATP-dependent manner and are associated with different subcellular membranous structures distinct from peroxisomes
Mol. Cell. Biol.
18
936-943
1998
Homo sapiens, Komagataella pastoris
brenda
Tamura, S.; Shimozawa, N.; Suzuki, Y.; Tsukamoto, T.; Osumi, T.; Fujiki, Y.
A cytoplasmic AAA family peroxin, Pex1p, interacts with Pex6p
Biochem. Biophys. Res. Commun.
245
883-886
1998
Homo sapiens, Rattus norvegicus
brenda
Babst, M.; Wendland, B.; Estepa, E.J.; Emr, S.D.
The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
EMBO J.
17
2982-2993
1998
Saccharomyces cerevisiae
brenda
Imamura, A.; Tamura, S.; Shimozawa, N.; Suzuki, Y.; Zhang, Z.; Tsukamoto, T.; Orii, T.; Kondo, N.; Osumi, T.; Fujiki, Y.
Temperature-sensitive mutation in PEX1 moderates the phenotypes of peroxisome deficiency disorders
Hum. Mol. Genet.
7
2089-2094
1998
Homo sapiens
brenda
Meyer, H.H.; Kondo, H.; Warren, G.
The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97
FEBS Lett.
437
255-257
1998
Saccharomyces cerevisiae, Xenopus laevis, Rattus norvegicus
brenda
Yoshimori, T.; Yamagata, F.; Yamamoto, A.; Mizushima, N.; Kabeya, Y.; Nara, A.; Miwako, I.; Ohashi, M.; Ohsumi, M.; Ohsumi, Y.
The mouse SKD1, a homologue of yeast Vps4p, is required for normal endosomal trafficking and morphology in mammalian cells
Mol. Biol.
11
747-763
2000
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Collins, C.S.; Kalish, J.E.; Morrell, J.C.; McCaffery, J.M.; Gould, S.J.
The peroxisome biogenesis factors pex4p, pex22p, pex1p, and pex6p act in the terminal steps of peroxisomal matrix protein import
Mol. Cell. Biol.
20
7516-7526
2000
Komagataella pastoris
brenda
Horsnell, W.G.; Steel, G.J.; Morgan, A.
Analysis of NSF mutants reveals residues involved in SNAP binding and ATPase stimulation
Biochemistry
41
5230-5235
2002
Saccharomyces cerevisiae
brenda
Uchiyama, K.; Jokitalo, E.; Kano, F.; Murata, M.; Zhang, X.; Canas, B.; Newman, R.; Rabouille, C.; Pappin, D.; Freemont, P.; Kondo, H.
VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo
J. Cell Biol.
159
855-866
2002
Rattus norvegicus
brenda
Yeo, S.C.; Xu, L.; Ren, J.; Boulton, V.J.; Wagle, M.D.; Liu, C.; Ren, G.; Wong, P.; Zahn, R.; Sasajala, P.; Yang, H.; Piper, R.C.; Munn, A.L.
Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae
J. Cell Sci.
116
3957-3970
2003
Saccharomyces cerevisiae
brenda
Fujita, H.; Umezuki, Y.; Imamura, K.; Ishikawa, D.; Uchimura, S.; Nara, A.; Yoshimori, T.; Hayashizaki, Y.; Kawai, J.; Ishidoh, K.; Tanaka, Y.; Himeno, M.
Mammalian class E Vps proteins, SBP1 and mVps2/CHMP2A, interact with and regulate the function of an AAA-ATPase SKD1/Vps4B
J. Cell Sci.
117
2997-3009
2004
Mus musculus
brenda
Mohtashami, M.; Stewart, B.A.; Boulianne, G.L.; Trimble, W.S.
Analysis of the mutant Drosophila N-ethylmaleimide sensitive fusion-1 protein in comatose reveals molecular correlates of the behavioural paralysis
J. Neurochem.
77
1407-1417
2001
Drosophila melanogaster
brenda
Whiteheart, S.W.; Matveeva, E.A.
Multiple binding proteins suggest diverse functions for the N-ethylmaleimide sensitive factor
J. Struct. Biol.
146
32-43
2004
Homo sapiens
brenda
Dalal, S.; Rosser, M.F.N.; Cyr, D.M.; Hanson, P.I.
Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway
Mol. Biol. Cell
15
637-648
2004
Cricetulus griseus, Mus musculus
brenda
Liu, C.; Hu, B.
Alterations of N-ethylmaleimide-sensitive ATPase following transient cerebral ischemia
Neuroscience
128
767-774
2004
Rattus norvegicus
brenda
Littleton, J.T.; Barnard, R.J.; Titus, S.A.; Slind, J.; Chapman, E.R.; Ganetzky, B.
SNARE-complex disassembly by NSF follows synaptic-vesicle fusion
Proc. Natl. Acad. Sci. USA
98
12233-12238
2001
Drosophila melanogaster
brenda
Shiozawa Kumik, S.K.; Maita Nobu, M.N.; Tomii Kentar, T.K.; Seto Azus, S.A.; Goda Natsuk, G.N.; Akiyama Yutak, A.Y.; Shimizu Toshiyuk, S.T.; Shirakawa Masahir, S.M.; Hiroaki Hidekaz, H.H.
Crystallographic characterization of the N-terminal domain of PEX1
Acta Crystallogr. Sect. D
60
2098-2099
2004
Mus musculus
brenda
Ramalho-Santos, J.; Schatten, G.
Presence of N-ethyl maleimide sensitive factor (NSF) on the acrosome of mammalian sperm
Arch. Androl.
50
163-168
2004
Bos taurus, Mus musculus
brenda
Fan, W.; Fujiki, Y.
A temperature-sensitive CHO pex1 mutant with a novel mutation in the AAA Walker A1 motif
Biochem. Biophys. Res. Commun.
345
1434-1439
2006
Cricetulus griseus
brenda
Yamauchi, S.; Yamanaka, K.; Ogura, T.
Comparative analysis of expression of two p97 homologues in Caenorhabditis elegans
Biochem. Biophys. Res. Commun.
345
746-753
2006
Caenorhabditis elegans
brenda
Xu, W.; Zhang, Q.; Denlinger, D.L.
A novel member of the NSF family in the corn earworm, Helicoverpa zea: molecular cloning, developmental expression, and tissue distribution
Biochim. Biophys. Acta
1759
186-190
2006
Helicoverpa zea
brenda
Woods, I.G.; Lyons, D.A.; Voas, M.G.; Pogoda, H.M.; Talbot, W.S.
nsf is essential for organization of myelinated axons in zebrafish
Curr. Biol.
16
636-648
2006
Danio rerio
brenda
Choi Jaebo, C.J.; Richards Keri , R.K.; Cinar Hediye Nes, C.H.; Newman Anna , N.A.
N-ethylmaleimide sensitive factor is required for fusion of the C. elegans uterine anchor cell
Dev. Biol.
297
87-102
2006
Caenorhabditis elegans
brenda
Pontier, S.M.; Lahaie, N.; Ginham, R.; St-Gelais, F.; Bonin, H.; Bell, D.J.; Flynn, H.; Trudeau, L.E.; McIlhinney, J.; White, J.H.; Bouvier, M.
Coordinated action of NSF and PKC regulates GABAB receptor signaling efficacy
EMBO J.
25
2698-2709
2006
Rattus norvegicus
brenda
Vajjhala, P.R.; Wong, J.S.; To, H.Y.; Munn, A.L.
The beta domain is required for Vps4p oligomerization into a functionally active ATPase
FEBS J.
273
2357-2373
2006
Saccharomyces cerevisiae
brenda
Rosenkranz, K.; Birschmann, I.; Grunau, S.; Girzalsky, W.; Kunau, W.H.; Erdmann, R.
Functional association of the AAA complex and the peroxisomal importomer
FEBS J.
273
3804-3815
2006
Saccharomyces cerevisiae
brenda
Shiozawa Kumik, S.K.; Goda Natsuk, G.N.; Shimizu Toshiyuk, S.T.; Mizuguchi Kenj, M.K.; Kondo Naom, K.N.; Shimozawa Nobuyuk, S.N.; Shirakawa Masahir, S.M.; Hiroaki Hidekaz, H.H.
The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97
FEBS J.
273
4959-4971
2006
Mus musculus
brenda
Laviolette, M.J.; Nunes, P.; Peyre, J.B.; Aigaki, T.; Stewart, B.A.
A genetic screen for suppressors of Drosophila NSF2 neuromuscular junction overgrowth
Genetics
170
779-792
2005
Drosophila sp. (in: flies)
brenda
Cui, S.Y.; Zhang, W.Q.; Xu, W.H.
Spatial and temporal expression of N-ethylmaleimide-sensitive factor gene in the nervous system of the cotton bollworm, Helicoverpa armigera
Insect Biochem. Mol. Biol.
36
603-609
2006
Helicoverpa armigera
brenda
Tamura, S.; Yasutake, S.; Matsumoto, N.; Fujiki, Y.
Dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p
J. Biol. Chem.
281
27693-27704
2006
Homo sapiens
brenda
Martin, H.G.; Henley, J.M.; Meyer, G.
Novel putative targets of N-ethylmaleimide sensitive fusion protein (NSF) and alpha/beta soluble NSF attachment proteins (SNAPs) include the Pak-binding nucleotide exchange factor betaPIX
J. Cell. Biochem.
99
1203-1215
2006
Rattus norvegicus
brenda
Morrell, C.N.; Matsushita, K.; Lowenstein, C.J.
A novel inhibitor of N-ethylmaleimide-sensitive factor decreases leukocyte trafficking and peritonitis
J. Pharmacol. Exp. Ther.
314
155-161
2005
Mus musculus
brenda
Yamanaka, K.; Okubo, Y.; Suzaki, T.; Ogura, T.
Analysis of the two p97/VCP/Cdc48p proteins of Caenorhabditis elegans and their suppression of polyglutamine-induced protein aggregation
J. Struct. Biol.
146
242-250
2004
Caenorhabditis elegans
brenda
Steinberg, J.P.; Huganir, R.L.; Linden, D.J.
N-ethylmaleimide-sensitive factor is required for the synaptic incorporation and removal of AMPA receptors during cerebellar long-term depression
Proc. Natl. Acad. Sci. USA
101
18212-18216
2004
Mus musculus
brenda
Platta, H.W.; Debelyy, M.O.; El Magraoui, F.; Erdmann, R.
The AAA peroxins Pex1p and Pex6p function as dislocases for the ubiquitinated peroxisomal import receptor Pex5p
Biochem. Soc. Trans.
36
99-104
2008
Homo sapiens
brenda
Beuron, F.; Dreveny, I.; Yuan, X.; Pye, V.E.; McKeown, C.; Briggs, L.C.; Cliff, M.J.; Kaneko, Y.; Wallis, R.; Isaacson, R.L.; Ladbury, J.E.; Matthews, S.J.; Kondo, H.; Zhang, X.; Freemont, P.S.
Conformational changes in the AAA ATPase p97-p47 adaptor complex
EMBO J.
25
1967-1976
2006
Rattus norvegicus
brenda
Jung, C.H.; Yang, Y.S.; Kim, J.S.; Shin, J.I.; Jin, Y.S.; Shin, J.Y.; Lee, J.H.; Chung, K.M.; Hwang, J.S.; Oh, J.M.; Shin, Y.K.; Kweon, D.H.
A search for synthetic peptides that inhibit soluble N-ethylmaleimide sensitive-factor attachment receptor-mediated membrane fusion
FEBS J.
275
3051-3063
2008
Rattus norvegicus
brenda
Zhao, C.; Slevin, J.T.; Whiteheart, S.W.
Cellular functions of NSF: not just SNAPs and SNAREs
FEBS Lett.
581
2140-2149
2007
Drosophila melanogaster, Drosophila melanogaster (P46461), Rattus norvegicus, Saccharomyces cerevisiae, Mammalia
brenda
Liu, Y.; Cheng, K.; Gong, K.; Fu, A.K.; Ip, N.Y.
Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein: implications in the regulation of its hexamerization and exocytosis
J. Biol. Chem.
281
9852-9858
2006
Mus musculus, Rattus norvegicus
brenda
Oh, E.; Heise, C.J.; English, J.M.; Cobb, M.H.; Thurmond, D.C.
WNK1 is a novel regulator of Munc18c-syntaxin 4 complex formation in soluble NSF attachment protein receptor (SNARE)-mediated vesicle exocytosis
J. Biol. Chem.
282
32613-32622
2007
Mus musculus
brenda
Hanley, J.G.
NSF binds calcium to regulate its interaction with AMPA receptor subunit GluR2
J. Neurochem.
101
1644-1650
2007
Mammalia
brenda
Pye, V.E.; Dreveny, I.; Briggs, L.C.; Sands, C.; Beuron, F.; Zhang, X.; Freemont, P.S.
Going through the motions: The ATPase cycle of p97
J. Struct. Biol.
156
12-28
2006
Saccharomyces cerevisiae, Drosophila melanogaster, Arabidopsis thaliana, Archaea, protozoa
brenda
Cui, S.Y.; Xu, W.H.
Molecular characterization and functional distribution of N-ethylmaleimide-sensitive factor in Helicoverpa armigera
Peptides
27
1226-1234
2006
Helicoverpa armigera
brenda
Haas, T.J.; Sliwinski, M.K.; Martinez, D.E.; Preuss, M.; Ebine, K.; Ueda, T.; Nielsen, E.; Odorizzi, G.; Otegui, M.S.
The Arabidopsis AAA ATPase SKD1 is involved in multivesicular endosome function and interacts with its positive regulator lyst-interacting protein5
Plant Cell
19
1295-1312
2007
Arabidopsis thaliana
brenda
Briggs, L.C.; Baldwin, G.S.; Miyata, N.; Kondo, H.; Zhang, X.; Freemont, P.S.
Analysis of nucleotide binding to p97 reveals the properties of a tandem AAA hexameric ATPase
J. Biol. Chem.
283
13745-13752
2008
Rattus norvegicus (P46462)
brenda
Fisher, E.A.; Lapierre, L.R.; Junkins, R.D.; McLeod, R.S.
The AAA-ATPase p97 facilitates degradation of apolipoprotein B by the ubiquitin-proteasome pathway
J. Lipid Res.
49
2149-2160
2008
Homo sapiens
brenda
Hartmann, C.; Chami, M.; Zachariae, U.; de Groot, B.L.; Engel, A.; Gruetter, M.G.
Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p
J. Mol. Biol.
377
352-363
2008
Saccharomyces cerevisiae (P52917), Saccharomyces cerevisiae
brenda
Yu, Z.; Gonciarz, M.D.; Sundquist, W.I.; Hill, C.P.; Jensen, G.J.
Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p
J. Mol. Biol.
377
364-377
2008
Saccharomyces cerevisiae
brenda
Inoue, M.; Kamikubo, H.; Kataoka, M.; Kato, R.; Yoshimori, T.; Wakatsuki, S.; Kawasaki, M.
Nucleotide-dependent conformational changes and assembly of the AAA ATPase SKD1/VPS4B
Traffic
9
2180-2189
2008
Mus musculus (P46467)
brenda
Naydenov, N.G.; Harris, G.; Brown, B.; Schaefer, K.L.; Das, S.K.; Fisher, P.B.; Ivanov, A.I.
Loss of soluble N-ethylmaleimide-sensitive factor attachment protein alpha (alphaSNAP) induces epithelial cell apoptosis via down-regulation of Bcl-2 expression and disruption of the Golgi
J. Biol. Chem.
287
5928-5941
2012
Homo sapiens
brenda
Chang, L.F.; Chen, S.; Liu, C.C.; Pan, X.; Jiang, J.; Bai, X.C.; Xie, X.; Wang, H.W.; Sui, S.F.
Structural characterization of full-length NSF and 20S particles
Nat. Struct. Mol. Biol.
19
268-275
2012
Cricetinae
brenda
Hill, C.P.; Babst, M.
Structure and function of the membrane deformation AAA ATPase Vps4
Biochim. Biophys. Acta
1823
172-181
2012
Saccharomyces cerevisiae
brenda
Monroe, N.; Han, H.; M.D., Gonciarz; Eckert, D.M.; Karren, M.A.; Whitby, F.G.; Sundquist, W.I.; Hill, C.P.
The oligomeric state of the active Vps4 AAA ATPase
J. Mol. Biol.
426
510-525
2013
Saccharolobus solfataricus (Q97ZJ7), Saccharolobus solfataricus, Saccharomyces cerevisiae, Saccharolobus solfataricus P2 (Q97ZJ7)
brenda
Legent, K.; Liu, H.H.; Treisman, J.E.
Drosophila Vps4 promotes epidermal growth factor receptor signaling independently of its role in receptor degradation
Development
142
1480-1491
2015
Drosophila melanogaster (Q9Y162)
brenda
Vivona, S.; Cipriano, D.J.; OLeary, S.; Li, Y.H.; Fenn, T.D.; Brunger, A.T.
Disassembly of all SNARE complexes by N-ethylmaleimide-sensitive factor (NSF) is initiated by a conserved 1:1 interaction between alpha-soluble NSF attachment protein (SNAP) and SNARE complex
J. Biol. Chem.
288
24984-24991
2013
Cricetulus griseus
brenda
Han, H.; Monroe, N.; Votteler, J.; Shakya, B.; Sundquist, W.I.; Hill, C.P.
Binding of substrates to the central pore of the Vps4 ATPase is autoinhibited by the microtubule interacting and trafficking (MIT) domain and activated by MIT interacting motifs (MIMs)
J. Biol. Chem.
290
13490-13499
2015
Saccharomyces cerevisiae (P52917)
brenda
Wang, F.; Yang, Y.; Wang, Z.; Zhou, J.; Fan, B.; Chen, Z.
A critical role of Lyst-interacting protein5, a positive regulator of multivesicular body biogenesis, in plant responses to heat and salt stresses
Plant Physiol.
169
497-511
2015
Arabidopsis thaliana (Q9ZNT0)
brenda
Barajas, D.; Martin, I.F.; Pogany, J.; Risco, C.; Nagy, P.D.
Noncanonical role for the host Vps4 AAA+ ATPase ESCRT protein in the formation of Tomato bushy stunt virus replicase
PLoS Pathog.
10
e1004087
2014
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Xia, Y.; Liu, N.; Xie, X.; Bi, G.; Ba, H.; Li, L.; Zhang, J.; Deng, X.; Yao, Y.; Tang, Z.; Yin, B.; Wang, J.; Jiang, K.; Li, Z.; Choi, Y.; Gong, F.; Cheng, X.; OShea, J.J.; Chae, J.J.; Laurence, A.; Yang, X.P.
The macrophage-specific V-ATPase subunit ATP6V0D2 restricts inflammasome activation and bacterial infection by facilitating autophagosome-lysosome fusion
Autophagy
15
960-975
2019
Mus musculus
brenda
Caillat, C.; Maity, S.; Miguet, N.; Roos, W.H.; Weissenhorn, W.
The role of VPS4 in ESCRT-III polymer remodeling
Biochem. Soc. Trans.
47
441-448
2019
Homo sapiens
brenda
Rijal, R.; Arhzaouy, K.; Strucksberg, K.; Cross, M.; Hofmann, A.; Schroeder, R.; Clemen, C.; Eichinger, L.
Mutant p97 exhibits species-specific changes of its ATPase activity and compromises the UBXD9-mediated monomerisation of p97 hexamers
Eur. J. Cell Biol.
95
195-207
2016
Homo sapiens (P55072), Homo sapiens, Dictyostelium discoideum (Q75JI3)
brenda
Alonso Y Adell, M.; Migliano, S.M.; Teis, D.
ESCRT-III and Vps4 a dynamic multipurpose tool for membrane budding and scission
FEBS J.
283
3288-3302
2016
Homo sapiens
brenda
Tan, J.; Davies, B.A.; Payne, J.A.; Benson, L.M.; Katzmann, D.J.
Conformational changes in the endosomal sorting complex required for the Transport III subunit ist1 lead to distinct modes of ATPpase Vps4 regulation
J. Biol. Chem.
290
30053-30065
2015
Saccharomyces cerevisiae
brenda
Schoeneberg, J.; Pavlin, M.R.; Yan, S.; Righini, M.; Lee, I.H.; Carlson, L.A.; Bahrami, A.H.; Goldman, D.H.; Ren, X.; Hummer, G.; Bustamante, C.; Hurley, J.H.
ATP-dependent force generation and membrane scission by ESCRT-III and Vps4
Science
362
1423-1428
2018
Homo sapiens
brenda
Yin, J.; Zhang, C.; Zhang, Q.; Long, F.; Hu, W.; Zhou, Y.; Mou, F.; Zhong, Y.; Wu, B.; Zhu, M.; Zou, L.; Zhu, X.
A single amino acid substitution in the AAA-type ATPase LRD6-6 activates immune responses but decreases grain quality in rice
Front. Plant Sci.
15
1451897
2024
Oryza sativa Japonica Group, Oryza sativa Japonica Group A814
brenda
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