Ca2+, calmodulin-dependent phosphorylation of glycogen synthase by a brain protein kinase.
A Ca2+, calmodulin-dependent protein kinase from brain with a Mr of 640 000 is capable of phosphorylating glycogen synthase from skeletal muscle. The reaction was inhibited by the addition of 1 mM EGTA and 50 microM trifluoperazine, but not by protein kinase inhibitor and heparin. The amount of phosphate incorporated into glycogen synthase was 1.4 mol/mol subunit. The phosphorylation sites of glycogen synthase were cyanogen bromide-treated peptides CB-1 and CB-2 and only the seryl residue was phosphorylated.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology*; D002135:Calcium-Binding Proteins / Q000494:pharmacology*; D002147:Calmodulin / Q000494:pharmacology*; D002417:Cattle; D006006:Glycogen Synthase / Q000302:isolation & purification; D007700:Kinetics; D008970:Molecular Weight; D010764:Phosphorylase Kinase / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*
D002135:Calcium-Binding Proteins; D002147:Calmodulin; D006006:Glycogen Synthase; D011494:Protein Kinases; D010764:Phosphorylase Kinase; D002118:Calcium