Calmodulin Inhibition of Brain Membrane Phosphorylation

Stanley A. Thayer, Robert H. Lemon, Alan S. Fairhurst

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Abstract: 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.

Original languageEnglish (US)
Pages (from-to)1090-1093
Number of pages4
JournalJournal of Neurochemistry
Volume41
Issue number4
DOIs
StatePublished - Apr 1983

Keywords

  • Brain
  • Calcium
  • Calmodulin
  • Protein phosphorylation

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