Calmodulin-dependent glycogen synthase kinase.

M E Payne; T R Soderling

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PubMed · 6251041

Calmodulin-dependent glycogen synthase kinase.

M E Payne·T R Soderling

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Abstract

A cAMP-independent glycogen synthase kinase has been purified from rabbit liver. This kinase is completely dependent on the presence of calmodulin and Ca2+ for activity. Half-maximal activation required about 0.1 microM calmodulin. Complete inhibition was obtained in the presence of ethylene glycol bis(beta-aminoethyl ether)N,N,N',N'-tetraacetic acid or trifluoperazine. This calmodulin-dependent synthase kinase does not phosphorylate phosphorylase, myosin light chain, casein, or histone. It rapidly incorporates 0.4 to 0.5 mol of 32P/mol of synthase subunit into the NH2-terminal domain, resulting in partial inactivation of glycogen synthase. These results indicate the existence of a calmodulin-dependent kinase which may be specific for glycogen synthase.

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Animals Calcium-Binding Proteins Calcium-Calmodulin-Dependent Protein Kinases Calmodulin Glycogen Synthase Kinases Kinetics Liver Protein Kinases Rabbits Substrate Specificity Trifluoperazine Journal Article Research Support, U.S. Gov't, P.H.S.

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M E Payne, T R Soderling. 1980-09-10. Calmodulin-dependent glycogen synthase kinase.. https://pubmed.ncbi.nlm.nih.gov/6251041/

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