NDLI: Isoform-specific and protein kinase C-mediated regulation of CTP:phosphoethanolamine cytidylyltransferase phosphorylation.

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Isoform-specific and protein kinase C-mediated regulation of CTP:phosphoethanolamine cytidylyltransferase phosphorylation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Pereira, Leanne Bakovic, Marica Cornell, Rosemary B. Zhu, Lin Singh, Ratnesh Kumar Pavlovic, Zvezdan
Description	Author Affiliation: Pavlovic Z ( From the Department of Human Health and Nutritional Sciences, University of Guelph, Ontario N1G 2W1 and.)
Abstract	CTP:phosphoethanolamine cytidylyltransferase (Pcyt2) is the main regulatory enzyme for de novo biosynthesis of phosphatidylethanolamine by the CDP-ethanolamine pathway. There are two isoforms of Pcyt2, - and -ß; however, very little is known about their specific roles in this important metabolic pathway. We previously demonstrated increased phosphatidylethanolamine biosynthesis subsequent to elevated activity and phosphorylation of Pcyt2 and -ß in MCF-7 breast cancer cells grown under conditions of serum deficiency. Mass spectroscopy analyses of Pcyt2 provided evidence for isoform-specific as well as shared phosphorylations. Pcyt2ß was specifically phosphorylated at the end of the first cytidylyltransferase domain. Pcyt2 was phosphorylated within the -specific motif that is spliced out in Pcyt2ß and on two PKC consensus serine residues, Ser-215 and Ser-223. Single and double mutations of PKC consensus sites reduced Pcyt2 phosphorylation, activity, and phosphatidylethanolamine synthesis by 50-90%. The phosphorylation and activity of endogenous Pcyt2 were dramatically increased with phorbol esters and reduced by specific PKC inhibitors. In vitro translated Pcyt2 was phosphorylated by PKC , PKCßI, and PKCßII. Pcyt2 Ser-215 was also directly phosphorylated with PKC . Mapping of the Pcyt2 - and -ß-phosphorylated sites to the solved structure of a human Pcyt2ß showed that they clustered within and flanking the central linker region that connects the two catalytic domains and is a novel regulatory segment not present in other cytidylyltransferases. This study is the first to demonstrate differences in phosphorylation between Pcyt2 isoforms and to uncover the role of the PKC-regulated phosphorylation.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	13
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-03-28
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Protein Kinase C Metabolism RNA Nucleotidyltransferases Amino Acid Motifs Amino Acid Sequence Animals Catalytic Domain Isoenzymes Chemistry MCF-7 Cells Mice Models, Molecular Molecular Sequence Data Mutation Phorbol Esters Pharmacology Phosphopeptides Phosphorylation Drug Effects Antagonists & Inhibitors Genetics Protein Kinase Inhibitors Serum Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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