Dynamic interplay between O-GlcNAc and O-phosphate: the sweet side of protein regulation

Curr Opin Struct Biol. 2003 Oct;13(5):631-6. doi: 10.1016/j.sbi.2003.08.003.

Abstract

Beta-O-linked N-acetylglucosamine (O-GlcNAc) is an abundant modification of cytosolic and nuclear proteins that occurs in metazoans. O-GlcNAc is dynamically processed by a unique set of enzymes that actively add and remove the modification. Functionally, O-GlcNAc appears to regulate protein stability, subcellular localization and protein-protein interactions. The modification often acts in a reciprocal manner to O-phosphate modifications of proteins and together they can synergistically control the activity of many cellular processes. Recently, O-GlcNAc has been demonstrated to play a significant role in diseases such as diabetes, cancer and neurodegeneration. For example, the increased levels of O-GlcNAc that occur in diabetes are associated with decreased insulin responsiveness in adipocytes.

Publication types

  • Review

MeSH terms

  • Acetylglucosamine / chemistry
  • Acetylglucosamine / metabolism*
  • Animals
  • Homeostasis / physiology
  • Humans
  • Neoplasms / metabolism*
  • Phosphates / chemistry
  • Phosphates / metabolism*
  • Protein Biosynthesis*
  • Proteins / chemistry
  • Signal Transduction / physiology*
  • Transcription, Genetic / physiology*

Substances

  • Phosphates
  • Proteins
  • Acetylglucosamine