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.
Stress-induced O-GlcNAcylation: an adaptive process of injured cells
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Marissa R. Martinez, Thiago Braido Dias, Peter S. Natov, Natasha E. Zachara; Stress-induced O-GlcNAcylation: an adaptive process of injured cells. Biochem Soc Trans 8 February 2017; 45 (1): 237–249. doi: https://doi.org/10.1042/BST20160153
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