Protein O-glucosyltransferase 2 (POGLUT2)

Protein O-glucosyltransferase 2 (POGLUT2) is an ER-resident enzyme with a C-terminal KDEL retention motif, catalyzing the addition of glucose from UDP-glucose to serine residues within the consensus sequence of EGF-like repeats in substrate proteins such as Notch receptors, Fibrillin-1, Fibrillin-2, and LTBP1[1][3][4][5]. POGLUT2 also has xylosyltransferase activity, transferring xylose from UDP-xylose, but with lower efficiency. These post-translational modifications support the proper folding and secretion of target proteins, impacting pathways like Notch signaling and the structure of the extracellular matrix[3][5]. Dysregulation or mutation of POGLUT2 is associated with muscle dystrophy, cancer (via effects on cell proliferation), hepatic dysfunction, and pancreatic β-cell apoptosis[1][5]. There are no known direct-acting drugs or clinical biomarkers for POGLUT2 at this time.

Other names

KDELC1KDEL motif-containing protein 1Endoplasmic reticulum resident protein 58ERp58EP58Protein O-xylosyltransferase POGLUT2MGC5302UNQ1910/PRO4357

For inhibitors or modulators (theoretically): block O-glucosylation or O-xylosylation of EGF repeats, disrupting protein folding, secretion, and Notch/fibrillin function. No clinically approved POGLUT2-targeting drugs/mechanisms described.