Autophosphorylation of calmodulin kinase II: functional aspects

FEBS Letters

Bronstein, J.M.²  Farber, D.B.³  Wasterlain, C.G.¹ 

[1] Brain Research Institute, UCLA School of Medicine, Center for the Health Sciences, Los Angeles, CA 90024, USA;Departments of Neuroscience, UCLA School of Medicine, Center for the Health Sciences, Los Angeles, CA 90024, USA;Jules Stein Eye Institute, UCLA School of Medicine, Center for the Health Sciences, Los Angeles, CA 90024, USA

关键词: Autophosphorylation;    Calmodulin kinase II;    SynapsinI;    Ca2+;    Protein kinase;   

DOI  :  10.1016/0014-5793(86)80228-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown