PCYT2 synthesizes CDP-glycerol in mammals and reduced PCYT2 enhances the expression of functionally glycosylated α-dystroglycan

Abstract α-Dystroglycan (α-DG) is a highly glycosylated cell-surface protein. Defective O-mannosyl glycan on α-DG associated with muscular dystrophies and cancer. In the biosynthetic pathway of glycan, fukutin (FKTN) fukutin-related protein (FKRP) transfer ribitol phosphate (RboP). Previously, we reported that FKTN FKRP can also glycerol (GroP) from CDP-glycerol (CDP-Gro) showed inhibitory effects CDP-Gro functional synthesis by preventing elongation in vitro. However, whether mammalian cells have or synthetic machinery has not been elucidated. Therefore, function mammals largely unknown. Here, reveal cultured human mouse tissues contain using liquid chromatography tandem–mass spectrometry (LC–MS/MS). By performing enzyme activity assay candidate recombinant proteins, found ethanolamine-phosphate cytidylyltransferase (PCYT2), key de novo phosphatidylethanolamine biosynthesis, glycerol-3-phosphate (Gro3P) CTP. addition, knockdown PCYT2 dramatically reduced cellular CDP-Gro. These results indicate synthase mammals. Furthermore, expression functionally increased reducing expression. Our suggest an important role for regulation