Related Experiment Video
Updated: Jan 5, 2026

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
Published on: April 27, 2010
Molecular mechanisms regulating O-linked N-acetylglucosamine (O-GlcNAc)-processing enzymes
Dustin T King1, Alexandra Males2, Gideon J Davies2
1Department 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.
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.
Related Concept Videos
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Proteoglycans
Protein Glycosylation
Glycosylation occurs in...
Protein Folding Quality Check in the RER
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Biosynthesis of Polysaccharides

