Abstract
All animals and plants dynamically attach and remove O-linked β-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.
Original language | English (US) |
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Pages (from-to) | 1017-1022 |
Number of pages | 6 |
Journal | Nature |
Volume | 446 |
Issue number | 7139 |
DOIs | |
State | Published - Apr 26 2007 |
ASJC Scopus subject areas
- General