Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc
Top Cited Papers
- 23 March 2001
- journal article
- review article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 291 (5512) , 2376-2378
- https://doi.org/10.1126/science.1058714
Abstract
The dynamic glycosylation of serine or threonine residues on nuclear and cytosolic proteins by O-linked β- 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.Keywords
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