Dephosphorylation of glycogen synthase from human polymorphonuclear leukocytes.
Leukocyte glycogen synthase (UDPglucose:glycogen 4-alpha-d-glucosyltransferase, EC 2.4.1.11) was phosphorylated to about one P1/synthase subunit by either the cAMP-dependent protein kinase or the cAMP-dependent synthase kinase. The relationship between dephosphorylation and the increase in the ratio of independence was investigated by analysis of the release of 32P-labelled phosphopeptides from the trypsin-sensitive and the trypsin-insensitive regions. The trypsin-insensitive region was predominantly dephosphorylated and a close correlation between dephosphorylation of a phosphopeptide in the trypsin-insensitive region and activation of glycogen synthase is reported for the enzyme phosphorylated in both ways.
D017871:Calcium-Calmodulin-Dependent Protein Kinases; D000242:Cyclic AMP / Q000378:metabolism; D006006:Glycogen Synthase / Q000097:blood*; D006801:Humans; D046911:Macromolecular Substances; D009504:Neutrophils / Q000201:enzymology*; D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism
D046911:Macromolecular Substances; D010710:Phosphates; D000242:Cyclic AMP; D006006:Glycogen Synthase; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases