Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc.
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.[1]References
- Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Wells, L., Vosseller, K., Hart, G.W. Science (2001) [Pubmed]
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