Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Top Cited Papers
- 25 April 2007
- journal article
- review article
- Published by Springer Nature in Nature
- Vol. 446 (7139) , 1017-1022
- https://doi.org/10.1038/nature05815
Abstract
All animals and plants dynamically attach and remove O-linked beta-N-acetylglucosamine (O-GlcNAc) at serine and threonine residues on myriad nuclear and cytoplasmic proteins. O-GlcNAc cycling, which is tightly regulated by the concerted actions of two highly conserved enzymes, serves as a nutrient and stress sensor. On some proteins, O-GlcNAc competes directly with phosphate for serine/threonine residues. Glycosylation with O-GlcNAc modulates signalling, and influences protein expression, degradation and trafficking. Emerging data indicate that O-GlcNAc glycosylation has a role in the aetiology of diabetes and neurodegeneration.Keywords
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