Protein O-GlcNAcylation is an abundant, dynamic and reversible type of protein post-translational modification in animals that has been implicated in signalling processes linked to innate immunity, stress response, growth factor response, transcription, translation and proteosomal degradation. Only two enzymes, O-GlcNAc (O-linked N-acetylglucosamine) transferase and O-GlcNAcase, catalyse the reversible addition of the O-GlcNAc residue to over 1000 target proteins in the human cell. Recent advances in our understanding of the structures and mechanisms of these enzymes have resulted in the development of potent and selective inhibitors. The present review gives an overview of these inhibitors and how they have been used on cell lines, primary cells and animals to modulate O-GlcNAc levels and study the effects on signal transduction.
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Review Article|
October 24 2013
Chemical tools to probe cellular O-GlcNAc signalling
Adam Ostrowski;
Adam Ostrowski
*Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, DD1 5EH, U.K.
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Daan M. F. van Aalten
Daan M. F. van Aalten
1
*Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, DD1 5EH, U.K.
†MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, DD1 5EH, U.K.
1To whom correspondence should be addressed (email d.m.f.vanaalten@dundee.ac.uk).
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Publisher: Portland Press Ltd
Received:
August 12 2013
Accepted:
September 05 2013
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2013 Biochemical Society
2013
Biochem J (2013) 456 (1): 1–12.
Article history
Received:
August 12 2013
Accepted:
September 05 2013
Citation
Adam Ostrowski, Daan M. F. van Aalten; Chemical tools to probe cellular O-GlcNAc signalling. Biochem J 15 November 2013; 456 (1): 1–12. doi: https://doi.org/10.1042/BJ20131081
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