Protein O-glucosyltransferase 1 (POGLUT1)

Protein O-glucosyltransferase 1 (POGLUT1) is an enzyme localized in the endoplasmic reticulum that catalyzes the transfer of glucose (and, to a lesser extent, xylose) to serine residues within specific consensus sequences of EGF-like repeats in multiple substrate proteins, especially Notch receptors[1][2][3][4][5][7]. Through this posttranslational modification, POGLUT1 is essential for proper Notch receptor folding and function, thereby enabling activation of the Notch signaling pathway, which is crucial for cellular differentiation, proliferation, and apoptosis throughout development and adult life[3][7]. Mutations or dysregulation of POGLUT1 are implicated in genetic disorders such as limb-girdle muscular dystrophy type 21 (LGMDR21) and Dowling-Degos disease, highlighting its pivotal role in both muscular and dermatologic tissue biology[3][6]. POGLUT1 belongs to the CAP10-like family of glycosyltransferases and shares structural and functional homology with its Drosophila homolog, Rumi[5][6].

Other names

C3orf9CLP46KTELC1KDELCL1MDSRPMDS010UNQ490/PRO1006hCLP46hRumiMGC329959630046K23RikRumiCAP10-like 46 kDa proteinKTEL motif-containing protein 1Myelodysplastic syndromes relative proteinProtein O-xylosyltransferase POGLUT1KDELC family like 1LGMD2ZLGMDR21

Enzyme inhibition (theoretical, for any future inhibitors targeting Notch signaling regulation via POGLUT1 modulation)