Calmodulin-dependent glycogen synthase kinase.
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.
D000818:Animals; D002135:Calcium-Binding Proteins / Q000494:pharmacology*; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002147:Calmodulin / Q000494:pharmacology*; D038341:Glycogen Synthase Kinases; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D011817:Rabbits; D013379:Substrate Specificity; D014268:Trifluoperazine / Q000494:pharmacology
D002135:Calcium-Binding Proteins; D002147:Calmodulin; D014268:Trifluoperazine; D011494:Protein Kinases; D038341:Glycogen Synthase Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases