Protein O-GlcNAcylation: emerging mechanisms and functions

Nat Rev Mol Cell Biol. 2017 Jul;18(7):452-465. doi: 10.1038/nrm.2017.22. Epub 2017 May 10.


O-GlcNAcylation - the attachment of O-linked N-acetylglucosamine (O-GlcNAc) moieties to cytoplasmic, nuclear and mitochondrial proteins - is a post-translational modification that regulates fundamental cellular processes in metazoans. A single pair of enzymes - O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) - controls the dynamic cycling of this protein modification in a nutrient- and stress-responsive manner. Recent years have seen remarkable advances in our understanding of O-GlcNAcylation at levels that range from structural and molecular biology to cell signalling and gene regulation to physiology and disease. New mechanisms and functions of O-GlcNAcylation that are emerging from these recent developments enable us to begin constructing a unified conceptual framework through which the significance of this modification in cellular and organismal physiology can be understood.

Publication types

  • Review
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism
  • Animals
  • Humans
  • N-Acetylglucosaminyltransferases / metabolism
  • Protein Processing, Post-Translational / genetics
  • Protein Processing, Post-Translational / physiology*
  • Proteins / chemistry
  • Proteins / metabolism*
  • Signal Transduction / genetics
  • Signal Transduction / physiology


  • Proteins
  • N-Acetylglucosaminyltransferases
  • O-GlcNAc transferase
  • Acetylglucosamine