Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 6, Issue 6, Pages 851-857Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/S1367-5931(02)00384-8
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Funding
- NCI NIH HHS [CA43486, CA83261] Funding Source: Medline
- NIDDK NIH HHS [DK61671] Funding Source: Medline
- NIGMS NIH HHS [GM20528] Funding Source: Medline
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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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