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.
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February 2017
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Cover Image
The surface of the catalytic subunit of protein phosphatase PP1 (central 3D-structure) has many binding sites for regulatory proteins that are embedded in regulatory networks (coloured circles linked by lines). Please see pp. 89–99 for more information. Image provided by Mathieu Bollen.
Review Article|
February 15 2017
Stress-induced O-GlcNAcylation: an adaptive process of injured cells
Marissa R. Martinez;
Marissa R. Martinez
1Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205-2185, U.S.A.
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Thiago Braido Dias;
Thiago Braido Dias
*
1Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205-2185, U.S.A.
2Department of Pharmacology, Ribeirao Preto Medical School, University of Sao Paulo, Av Bandeirantes 3900, Ribeirao Preto, 14049-900 SP, Brazil
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Peter S. Natov;
1Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205-2185, U.S.A.
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Natasha E. Zachara
1Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205-2185, U.S.A.
Correspondence: Natasha E. Zachara (nzachara@jhmi.edu)
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Publisher: Portland Press Ltd
Received:
October 25 2016
Revision Received:
November 30 2016
Accepted:
December 14 2016
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society
2017
Biochem Soc Trans (2017) 45 (1): 237–249.
Article history
Received:
October 25 2016
Revision Received:
November 30 2016
Accepted:
December 14 2016
Citation
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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