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

Dustin T King, Alexandra Males, Gideon J Davies, David J Vocadlo

Journal: Current opinion in chemical biology 2020;53():131-144

PMID: 31654859

Full Text on Elsevier Science View on PubMed

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.

Address: 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.; Department of Chemistry, University of York, York, YO10 5DD, England.; 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].

DOI: 10.1016/j.cbpa.2019.09.001

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MeSH Terms: Acetylglucosamine, Humans, Hydrolases, N-Acetylglucosaminyltransferases, Protein Processing, Post-Translational, Substrate Specificity, Transcriptional Activation