Ca2+-activated, phospholipid-dependent protein kinase catalyzes the phosphorylation of actin-binding proteins.
Chicken gizzard vinculin and filamin were found to be phosphorylated by Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C). These two actin-binding proteins serve as substrates for protein kinase C specifically in the free form, whereas they are little phosphorylated by protein kinase C in the presence of F-actin. In contrast, alpha-actinin from chicken gizzard is less susceptible to phosphorylation by protein kinase C, either in the presence or in the absence of F-actin. In light of these data, the possibility that Ca2+ and phospholipid-dependent phosphorylation by protein kinase C may modulate the function of actin-binding proteins has to be considered.
D000185:Actinin / Q000378:metabolism*; D000199:Actins / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002645:Chickens; D003285:Contractile Proteins / Q000378:metabolism*; D064448:Filamins; D006801:Humans; D008840:Microfilament Proteins; D009124:Muscle Proteins / Q000378:metabolism*; D010743:Phospholipids / Q000494:pharmacology; D010766:Phosphorylation; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism*; D016596:Vinculin
D000199:Actins; D003285:Contractile Proteins; D064448:Filamins; D008840:Microfilament Proteins; D009124:Muscle Proteins; D010743:Phospholipids; D000185:Actinin; D016596:Vinculin; D011494:Protein Kinases; D011493:Protein Kinase C; D002118:Calcium