O-linked β-D-N-acetylglucosamine (O-GlcNAc) is an abundant post-translational modification (PTM) that modifies the serine or threonine residues of thousands of proteins in the nucleus, cytoplasm and mitochondria. Being a major "nutrient sensor" in cells, the O-GlcNAc pathway is sensitive to cellular metabolic states. Extensive crosstalk is observed between O-GlcNAcylation and protein phosphorylation. O-GlcNAc regulates protein functions at multiple levels, including enzymatic activity, transcriptional activity, subcellular localization, intermolecular interactions and degradation. Abnormal O-GlcNAcylation is associated with many human diseases including cancer, diabetes and neurodegenerative diseases. Though research on O-GlcNAc is still in its infantry, accumulating evidence suggest O-GlcNAcylation to be a promising therapeutic target. In this review, we briefly discuss the basic features of this PTM, the O-GlcNAc signaling pathway, its regulatory functions on different proteins, and its involvement in human diseases. We hope this review will provide insights to researchers who study human disease, as well as researchers who are interested in the fundamental roles of O-GlcNAcylation in all cells.
Keywords: Cancer; Diabetes; Neurodegenerative disease; O-GlcNAc; Post-translational modification; Protein function.
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