Elucidating the effect of O-GlcNAc modification on protein stability

Principal Investigator: 
University: 
Simon Fraser University
Faculty: 
Faculty of Science
Department: 
Department of Chemistry
Award Type: 

The glycosylation of proteins with O-GlcNAc is a ubiquitous post-translational modification found throughout the metazoans. Deregulation of O-GlcNAcylation is implicated in several human diseases including type II diabetes, Alzheimer’s disease, and cancer.

However, the basic biochemical roles of O-GlcNAcylation remain largely unanswered. Several recent studies have demonstrated a clear link between O-GlcNAc and cellular thermotolerance.

It is likely that a basic function of the O-GlcNAc modification prevents the unfolding or aggregation of target proteins. Dr. King will investigate its role in protein stability through series of biochemical and biophysical experiments to probe the effect of O-GlcNAc on protein unfolding, folding, and aggregation. The results of this research will provide important insights into the basic molecular mechanisms governing O-GlcNAc deregulation in human disease. 

Research Pillar: 
Host Institution: 
Simon Fraser University
Research Location: 
Simon Fraser University
Supervisor: 
David Vocadlo
Year: 
2017