Review
doi: 10.1126/science.1058714.
Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc
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- PMID: 11269319
- DOI: 10.1126/science.1058714
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Review
Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc
Science.
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Abstract
The dynamic glycosylation of serine or threonine residues on nuclear and cytosolic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) is abundant in all multicellular eukaryotes. On several proteins, O-GlcNAc and O-phosphate alternatively occupy the same or adjacent sites, leading to the hypothesis that one function of this saccharide is to transiently block phosphorylation. The diversity of proteins modified by O-GlcNAc implies its importance in many basic cellular and disease processes. Here we systematically examine the current data implicating O-GlcNAc as a regulatory modification important to signal transduction cascades.
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