Diverse regulation of protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate post-translational modification

Curr Opin Chem Biol. 2002 Dec;6(6):851-7. doi: 10.1016/s1367-5931(02)00384-8.

Abstract

N-Acetylglucosamine O-linked to serines and threonines of cytosolic and nuclear proteins (O-GlcNAc) is an abundant reversible post-translational modification found in all higher eukaryotes. Evidence for functional regulation of proteins by this dynamic saccharide is rapidly accumulating. Deletion of the gene encoding the enzyme that attaches O-GlcNAc (OGT) is lethal at the single cell level, indicating the fundamental requirement for this modification. Recent studies demonstrate a role for O-GlcNAcylation in processes as diverse as transcription in the nucleus and signaling in the cytoplasm, suggesting that O-GlcNAc has both protein and site-specific influences on biochemistry and metabolism throughout the cell.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Acetylglucosamine / metabolism*
  • Animals
  • Cell Nucleus / metabolism*
  • Cytoplasm / metabolism*
  • Glucose / metabolism
  • Humans
  • N-Acetylglucosaminyltransferases / metabolism
  • Nuclear Proteins / metabolism*
  • Phosphorylation
  • Protein Processing, Post-Translational*
  • Signal Transduction

Substances

  • Nuclear Proteins
  • N-Acetylglucosaminyltransferases
  • Glucose
  • Acetylglucosamine