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- Title
Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins.
- Authors
Hart, Gerald W; Housley, Michael P; Slawson, Chad
- 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.
- Publication
Nature, 2007, Vol 446, Issue 7139, p1017
- ISSN
1476-4687
- Publication type
Journal Article
- DOI
10.1038/nature05815