Phosphorylation of the calmodulin-dependent protein phosphatase by protein kinase C.
The calmodulin-dependent protein phosphatase was shown to be phosphorylated by the Ca2+, phospholipid-dependent protein kinase (protein kinase C). Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the 61 kDa catalytic subunit was phosphorylated. Phosphorylation by protein kinase C was stimulated up to 15-fold by addition of phosphatidyl-L-serine and between 0.5 to 1.0 mole of phosphate was incorporated per mole of phosphatase. It is possible that protein kinase C is involved in the regulation of the calmodulin-dependent protein phosphatase via this novel phosphorylation of the enzyme.
D000818:Animals; D001921:Brain / Q000201:enzymology; D002147:Calmodulin / Q000494:pharmacology*; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007700:Kinetics; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*
D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D010761:Phosphorus Radioisotopes; D011493:Protein Kinase C; D010749:Phosphoprotein Phosphatases