EGF domain-specific O-linked N-acetylglucosamine transferase (EOGT)

EGF domain-specific O-linked N-acetylglucosamine transferase (EOGT) is an enzyme localized to the lumen of the endoplasmic reticulum that catalyzes the attachment of N-acetylglucosamine (GlcNAc) via O-linkage to specific serine or threonine residues within epidermal growth factor (EGF)-like domains of secreted and membrane proteins[1][4][5]. This post-translational modification, called O-GlcNAcylation, is essential for the regulation of protein stability, extracellular signaling, and cell–cell or cell–matrix interactions, particularly during development[1][3][4][5]. EOGT is distinct from the cytoplasmic O-GlcNAc transferase (OGT), acting selectively on EGF repeats in proteins of the secretory pathway, including the Notch receptor and its ligands, Dumpy, Delta, and Serrate[1][2][4][5]. Loss-of-function mutations in EOGT are causative for Adams-Oliver syndrome type 4, a disorder characterized by scalp defects and limb malformations[5]. EOGT has not been directly targeted by approved pharmacological interventions, and no established drugs modulate its activity.

Other names

EOGT1AER61C3orf64FLJ33770Extracellular O-linked N-acetylglucosamine transferaseAOS4EGF domain-specific O-GlcNAc transferaseAER61 glycosyltransferase

Not applicable (no approved drugs specifically targeting EOGT reported in current literature)