Stress-induced O-GlcNAcylation: an adaptive process of injured cells

Biochem Soc Trans. 2017 Feb 8;45(1):237-249. doi: 10.1042/BST20160153.


In the 30 years, since the discovery of nucleocytoplasmic glycosylation, O-GlcNAc has been implicated in regulating cellular processes as diverse as protein folding, localization, degradation, activity, post-translational modifications, and interactions. The cell co-ordinates these molecular events, on thousands of cellular proteins, in concert with environmental and physiological cues to fine-tune epigenetics, transcription, translation, signal transduction, cell cycle, and metabolism. The cellular stress response is no exception: diverse forms of injury result in dynamic changes to the O-GlcNAc subproteome that promote survival. In this review, we discuss the biosynthesis of O-GlcNAc, the mechanisms by which O-GlcNAc promotes cytoprotection, and the clinical significance of these data.

Keywords: OGT; chaperone; glycoprotein; heat shock response; mgea5; signal transduction.

Publication types

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

MeSH terms

  • Acetylglucosamine / metabolism*
  • Adaptation, Physiological / physiology*
  • Animals
  • Cell Survival
  • Glycosylation
  • Humans
  • Models, Biological
  • Protein Processing, Post-Translational*
  • Signal Transduction / physiology*
  • Stress, Physiological / physiology*


  • Acetylglucosamine