O-linked β-N-acetylglucosamine (O-GlcNAc) is a post-translational modification (i.e., O-GlcNAcylation) on serine/threonine residues of proteins. Distinct from the traditional glycosylation (i.e., N-glycosylation, O-glycosylation, and GPI-anchored glycosylation), O-GlcNAcylation is a unique intracellular monosaccharide modification without being further elongated into complex sugar structures. O-GlcNAcylation is catalyzed by a pair of enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). OGT transfers the GlcNAc moiety from UDP-GlcNAc to specific serine/threonine residues of target proteins while OGA removes it. As a highly dynamic modification, O-GlcNAcylation plays important roles in almost all biochemical processes examined (including transcription, translation, cell cycle, metabolism and signaling). Aberrant O-GlcNAcylation underlies the etiology and development of a number of chronic diseases (including cancer, diabetes, and neurodegenerative disease). Targeting protein O-GlcNAcylation holds great promise for biomedical applications (e.g., as therapeutic targets and biomarkers).
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