    2.7.7.14 | phosphoprotein |
splice variant Pcyt2beta is specifically phosphorylated at the end of the first cytidylyltransferase domain. Splice variant Pcyt2alpha is phosphorylated within the alpha-specific motif that is spliced out in Pcyt2beta and on two protein kinase C consensus serine residues, Ser215 and Ser223. Single and double mutations of protein kinase C consensus sites reduce Pcyt2alpha phosphorylation, activity, and phosphatidylethanolamine synthesis by 50-90%. The phosphorylation and activity of endogenous Pcyt2 are dramatically increased with phorbol esters and reduced by specific protein kinase C inhibitors. In vitro translated Pcyt2 is phosphorylated by protein kinase Calpha, protein kinase CbetaI, and protein kinase CbetaII. The phosphorylated sites cluster within and flanking the central linker region that connects the two catalytic domains and is a regulatory segment not present in other cytidylyltransferases |
738642 |
