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

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

Author information

1
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205-2185, U.S.A.
2
Department of Pharmacology, Ribeirao Preto Medical School, University of Sao Paulo, Av Bandeirantes 3900, Ribeirao Preto, 14049-900 SP, Brazil.
3
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205-2185, U.S.A. nzachara@jhmi.edu.

Abstract

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

PMID:
28202678
DOI:
10.1042/BST20160153
[Indexed for MEDLINE]

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