Protein kinase C and cAMP-dependent protein kinase induce opposite effects on actin polymerizability.
Protein kinase C phosphorylated muscle and non-muscle monomeric actin more efficiently than filamentous actin in vitro. By sedimentation assay, the ratio of phosphorylated to unphosphorylated actin was much higher in sedimentable actin than in the non-sedimentable form, suggesting that phosphorylated actin was more readily incorporated into F-actin than unphosphorylated actin. In contrast, actin phosphorylated by cAMP-dependent protein kinase was found to have weaker polymerizability than the unphosphorylated form. The phosphopeptide mapping pattern of actin phosphorylated by protein kinase C was different from that of actin phosphorylated by cAMP-dependent protein kinase. Thus, both the protein kinases phosphorylate actin differently and induce opposite effects on actin polymerizability.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D004586:Electrophoresis / Q000379:methods; D009132:Muscles / Q000378:metabolism; D010766:Phosphorylation; D011108:Polymers; D011493:Protein Kinase C / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D011817:Rabbits; D051381:Rats
D000199:Actins; D011108:Polymers; D011494:Protein Kinases; D011493:Protein Kinase C