Affordable Access

deepdyve-link
Publisher Website

Molecular mechanisms regulating O-linked N-acetylglucosamine (O-GlcNAc)-processing enzymes.

Authors
  • King, Dustin T1
  • Males, Alexandra2
  • Davies, Gideon J2
  • Vocadlo, David J3
  • 1 Department of Chemistry, Simon Fraser University, Burnaby, British Columbia, V5A 1S6, Canada; Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, V5A 1S6, Canada. , (Canada)
  • 2 Department of Chemistry, University of York, York, YO10 5DD, England.
  • 3 Department of Chemistry, Simon Fraser University, Burnaby, British Columbia, V5A 1S6, Canada; Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, V5A 1S6, Canada. Electronic address: [email protected] , (Canada)
Type
Published Article
Journal
Current opinion in chemical biology
Publication Date
Dec 01, 2019
Volume
53
Pages
131–144
Identifiers
DOI: 10.1016/j.cbpa.2019.09.001
PMID: 31654859
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

The post-translational modification of proteins by O-linked N-acetylglucosamine (O-GlcNAc) dynamically programmes cellular physiology to maintain homoeostasis and tailor biochemical pathways to meet context-dependent cellular needs. Despite diverse roles of played by O-GlcNAc, only two enzymes act antagonistically to govern its cycling; O-GlcNAc transferase installs the monosaccharide on target proteins, and O-GlcNAc hydrolase removes it. The recent literature has exposed a network of mechanisms regulating these two enzymes to choreograph global, and target-specific, O-GlcNAc cycling in response to cellular stress and nutrient availability. Herein, we amalgamate these emerging mechanisms from a structural and molecular perspective to explore how the cell exerts fine control to regulate O-GlcNAcylation of diverse proteins in a selective fashion. Copyright © 2019 Elsevier Ltd. All rights reserved.

Report this publication

Statistics

Seen <100 times