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The O-GlcNAc Modification.

Source

Essentials of Glycobiology [Internet]. 3rd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2015-2017.Chapter 19.
2017.

Author information

1
Distinguished Professor of Medicine and Cellular & Molecular Medicine, Co-Director, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, California, USA
2
Professor of Surgery, Director, National Center for Functional Glycomics, Harvard Medical School, Cambridge, Massachusetts, USA
3
Distinguished Professor of Cellular & Molecular Medicine, Co-Director, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, California, USA
4
Horace W. Goldsmith Foundation Chair and Professor of Cell Biology, Albert Einstein College of Medicine, New York, New York, USA
5
Professor and Chairman of Biological Chemistry, Johns Hopkins University, Baltimore, Maryland, USA
6
Professor of Mycology, ETH Zürich, Zürich, Switzerland
7
Regents Professor and Director, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA
8
Professor, Laboratory of Immunoglycobiology, WPI Immunology Frontier Research Center, Osaka University, Osaka, Japan
9
Professor of Glycoproteomics and Glycomics, Macquarie University and Institute for Glycomics, Griffith University, Sydney, Australia
10
Professor and Eminent Scholar, University of Georgia, Athens, Georgia, USA
11
Professor, Departments of Pharmacology and Neuroscience, Johns Hopkins University, Baltimore, Maryland, USA
12
Director, Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany

Excerpt

This chapter presents an overview of the dynamic modification of serine or threonine hydroxyl moieties on nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-linked N-acetylglucosamine, termed O-β-GlcNAc or simply O-GlcNAc. This seemingly simple carbohydrate modification plays key roles in cellular physiology and disease progression. Underpinning these observations are the thousands of O-GlcNAc-modified proteins that regulate cellular pathways such as epigenetics, gene expression, translation, protein degradation, signal transduction, mitochondrial bioenergetics, the cell cycle, and protein localization.

Copyright 2015-2017 by The Consortium of Glycobiology Editors, La Jolla, California. All rights reserved.

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