Poly (ADP-ribose) synthetase is phosphorylated by protein kinase C in vitro.
Poly (ADP-ribose) synthetase from bovine thymus was phosphorylated effectively by protein kinase C in vitro. The phosphorylation was dependent on the activators of this kinase, Ca2+ and phospholipid. The apparent Km for the synthetase was about 8 microM, which was lower than that for histone H1. Though the synthetase was a weak substrate for Ca2+/calmodulin-dependent protein kinase II, other protein kinases, cyclic AMP-dependent and cofactor-independent protein kinases did not phosphorylate the synthetase. Phosphorylation of the synthetase by protein kinase C resulted in appreciable inhibition of the synthetase activity.
D000818:Animals; D001921:Brain / Q000201:enzymology; D002417:Cattle; D004789:Enzyme Activation; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D010766:Phosphorylation; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity; D013950:Thymus Gland / Q000201:enzymology*; D014981:Xenopus
D011065:Poly(ADP-ribose) Polymerases; D011493:Protein Kinase C