Dolichol-phosphate mannosyltransferase subunit 2 (DPM2)

Dolichol-phosphate mannosyltransferase subunit 2 (DPM2) is a highly hydrophobic, small ER membrane protein that serves as the regulatory subunit of the dolichol-phosphate-mannose (DPM) synthase complex in humans[1][3][4]. This complex is essential for the formation of dolichol-phosphate mannose, a critical glycosyl donor for various glycosylation pathways, including N-glycosylation, O-mannosylation, and GPI-anchor synthesis[1][3][4]. DPM2 anchors and stabilizes the catalytic subunit DPM1 and is essential for maintaining proper localization and activity of the complex within the endoplasmic reticulum, thereby regulating protein and lipid glycosylation[2][4]. Loss-of-function or mutation in DPM2 results in congenital disorders of glycosylation, predominantly affecting muscular and nervous system development and resulting in clinical features such as hypotonia, developmental delay, and abnormal enzyme glycosylation profiles[4]. No known drugs target DPM2 directly, and there are no established mechanisms of action for pharmacological modulation of this protein.

Other names

Dolichol phosphate-mannose biosynthesis regulatory proteinDPM synthase subunit 2Dolichol-phosphate mannose synthase subunit 2Dolichyl-phosphate mannosyltransferase polypeptide 2, regulatory subunitMy026MGC21559MGC111193DPM synthase complex subunitCDG1U