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

Marissa R. Martinez, Thiago Braido Dias, Peter S. Natov, Natasha E. Zachara

Research output: Contribution to journalReview articlepeer-review

41 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)237-249
Number of pages13
JournalBiochemical Society transactions
Issue number1
StatePublished - Feb 8 2017

ASJC Scopus subject areas

  • Biochemistry


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