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Literature summary for 2.7.11.17 extracted from

  • Magupalli, V.; Mochida, S.; Yan, J.; Jiang, X.; Westenbroek, R.; Nairn, A.; Scheuer, T.; Catterall, W.
    Ca2+-independent activation of Ca2+/Calmodulin-dependent protein kinase II bound to the C-terminal domain of CaV2.1 calcium channels (2013), J. Biol. Chem., 288, 4637-4648.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.17

Activating Compound

Activating Compound Comment Organism Structure
additional information Ca2+-independent activation of Ca2+/calmodulin-dependent protein kinase II bound to the C-terminal domain of CaV2.1 calcium channels Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
coexpression of GST-tagged enzyme with GST-tagged Cav2.1 channels in transfected tsA-201 cells and GST affinity pulldown assay, recombinant expression of MBP-fusion enzyme in Escherichia coli strain BL21 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
CaMKIIN brain-specific CaMKII inhibitor Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Homo sapiens
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + synapsin-1 Homo sapiens
-
 ADP + phopshorylated synapsin-1
-
 ?
additional information Homo sapiens CaMKII binds directly to a site in the C-terminal domain of CaV2.1 channels, autophosphorylation of CaMKII stimulates binding to this site. Autophosphorylated CaMKII can bind to the CaV2.1 channel and synapsin-1 simultaneously. Binding of CaV2.1 to CaMKII induces Ca2+-independent kinase activity, which mediates both autophosphorylation and phosphorylation of synapsin-1 at Ser603. Binding of autophosphorylated CaMKII to GST-tagged CaV2.1(1848–1964) is substantially greater than binding of nonactivated CaMKII. CaM is not required for CaMKII binding to Ca2+channels. Binding of autophosphorylated CaMKII persists after Ca2+/CaM dissociation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein autophosphorylation of CaMKII at Thr286 activates the enzyme, autophosphorylated CaMKII can bind to the CaV2.1 channel and synapsin-1 simultaneously Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + synapsin-1
-
 Homo sapiens ADP + phopshorylated synapsin-1
-
 ?
additional information CaMKII binds directly to a site in the C-terminal domain of CaV2.1 channels, autophosphorylation of CaMKII stimulates binding to this site. Autophosphorylated CaMKII can bind to the CaV2.1 channel and synapsin-1 simultaneously. Binding of CaV2.1 to CaMKII induces Ca2+-independent kinase activity, which mediates both autophosphorylation and phosphorylation of synapsin-1 at Ser603. Binding of autophosphorylated CaMKII to GST-tagged CaV2.1(1848–1964) is substantially greater than binding of nonactivated CaMKII. CaM is not required for CaMKII binding to Ca2+channels. Binding of autophosphorylated CaMKII persists after Ca2+/CaM dissociation Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
Ca2+/calmodulin-dependent protein kinase II
-
 Homo sapiens
CaMKII
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens
Calmodulin CaV2.1(1848–1964) contains an IQ-like motif as part of a bipartite regulatory site that is important for CaM-induced facilitation and inactivation of CaV2.1 channels. IQ-like motifs bind CaM. CaM is not required for CaMKII binding to Ca2+channels Homo sapiens

General Information

General Information Comment Organism
physiological function a complex of CaMKII and CaV2.1 channels is required for short term synaptic plasticity. Calmodulin regulation of Ca2+ channels mediates short term synaptic plasticity and CaMKII bound to CaV2.1 may regulate synaptic plasticity. Binding of CaMKII to CaV2.1 channels induces Ca2+-independent kinase activity Homo sapiens