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Diverse regulation of protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate post-translational modification

✍ Scribed by Keith Vosseller; Kaoru Sakabe; Lance Wells; Gerald W Hart

Book ID: 104414724
Publisher: Elsevier Science
Year: 2002
Tongue: English
Weight: 156 KB
Volume: 6
Category: Article
ISSN: 1367-5931
DOI: 10.1016/s1367-5931(02)00384-8

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✦ Synopsis

N-Acetylglucosamine O-linked to serines and threonines of cytosolic and nuclear proteins (O-GlcNAc) is an abundant reversible post-translational modification found in all higher eukaryotes. Evidence for functional regulation of proteins by this dynamic saccharide is rapidly accumulating. Deletion of the gene encoding the enzyme that attaches O-GlcNAc (OGT) is lethal at the single cell level, indicating the fundamental requirement for this modification. Recent studies demonstrate a role for O-GlcNAcylation in processes as diverse as transcription in the nucleus and signaling in the cytoplasm, suggesting that O-GlcNAc has both protein and site-specific influences on biochemistry and metabolism throughout the cell.

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