Autophosphorylation of calmodulin kinase II: functional aspects.
Autophosphorylation of purified calmodulin kinase II dramatically inhibited protein kinase activity and enhanced substrate selectivity. Inhibition was observed over a wide range of calmodulin concentrations but calmodulin binding was unaffected. Autophosphorylation of calmodulin kinase II may be a mechanism for limiting phosphorylation to physiological substrates and terminating some of calcium's actions in synaptic events.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000249:Adenosine Monophosphate / Q000378:metabolism; D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002147:Calmodulin / Q000378:metabolism*; D004027:Diencephalon / Q000201:enzymology / Q000502:physiology; D006801:Humans; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity; D013687:Telencephalon / Q000201:enzymology / Q000502:physiology
D002147:Calmodulin; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases