>> Chemical biology of O-GlcNAc: Enzyme Mechanisms to Chemical Probes 

 

Venue: Room A204-206, Chemistry Building A
Date: May 23, 2014 (Friday)
Time: 15:30-16:30
Organizer: College of Chemistry and Molecular Engineering

 

O-linked N-acetylglucosamine (O-GlcNAc) is an abundant form of protein O-glycosylation found in the nucleus and cytoplasm of multicellular eukaryotes. This post-translational modification is found on hundreds of proteins yet is regulated by only two enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). O-GlcNAc levels in cells respond to changes in glucose availability and in some cases can influence protein phosphorylation. Accordingly, O-GlcNAc has been implicated in various essential biological processes. Inappropriate regulation of O-GlcNAc has been proposed to play roles in diseases ranging from cancer to Alzheimer's. Here the lecturer will discuss his research focused on understanding the substrate specificities and catalytic mechanisms of OGT and OGA, as well as the exploitation of these insights to design probes of these enzymes that are active in cells and tissues. He will also discuss how these tools have enabled his team to interrogate the functional roles of O-GlcNAc in various biological models including transgenic Alzheimer mice.

 

 

Written by: Jiang Zhihui
Edited by: Arthars
Source: PKU Lecture Hall

 

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