Premium
Autophosphorylation of calmodulin kinase II: functional aspects
Author(s) -
Bronstein J.M.,
Farber D.B.,
Wasterlain C.G.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80228-9
Subject(s) - autophosphorylation , calmodulin , protein kinase a , chemistry , biochemistry , kinase , phosphorylation , substrate level phosphorylation , microbiology and biotechnology , biophysics , enzyme , biology
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.