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Natural Substrates
Commentary (Nat. Sub.)
2.7.11.17
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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(18481964) 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
2.7.11.17
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in terms of substrate specificity, the consensus sequences for phosphorylation by CaMKI, CaMKII, and CaMKIV are quite similar, and hence these kinases sometimes phosphorylate the same substrates, for example cAMP-response element-binding protein. Expression of Camk2g and Camk2d, but not Camk1 or Camk4, in Camk2g-/- eggs leads to degradation of exogenously expressed EMI2
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