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Calmodulin Inhibition of Brain Membrane Phosphorylation
Author(s) -
Thayer Stanley A.,
Lemon Robert H.,
Fairhurst Alan S.
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb09056.x
Subject(s) - calmodulin , phosphorylation , phosphatase , protein kinase a , protein phosphorylation , kinase , biochemistry , microbiology and biotechnology , calcium , chemistry , biology , biophysics , enzyme , organic chemistry
Calmodulin has been found to inhibit the phosphorylation of rat brain membrane proteins of molecular weight 14,900–18,900 in a dose‐dependent manner. This phenomenon was seen under conditions in which calmodulin simultaneously produced a stimulatory effect on the phosphorylation of proteins of molecular weight 51,000 and above. This inhibition required calcium, but was not sensitive to cyclic AMP or increasing ATP concentration and was not due to activation of a phosphatase. These results suggest either that calmodulin induces its inhibitory effects on phosphorylation by an indirect mechanism via a presently unknown pathway, or that in addition to the kinase stimulated by calmodulin, there exists another distinct kinase which is inhibited by calmodulin.