Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins

Nature. 2007 Apr 26;446(7139):1017-22. doi: 10.1038/nature05815.


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 types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Acetylglucosamine / analogs & derivatives
  • Acetylglucosamine / chemistry*
  • Acetylglucosamine / metabolism*
  • Alzheimer Disease / metabolism
  • Animals
  • Cytoplasm / chemistry
  • Cytoplasm / metabolism*
  • Enzymes / metabolism
  • Humans
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / metabolism*
  • Phosphates / metabolism


  • Enzymes
  • Nuclear Proteins
  • Phosphates
  • Acetylglucosamine