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SUMMARY:&quot\;Molecular mechanisms of O-GlcNAc signalling&quot\; - Profes
 sor Daan van Aalten\, FRSE\, Associate Dean\, Division of Molecular Microb
 iology\, College of Life Sciences\, University of Dundee
DTSTART:20120518T120000Z
DTEND:20120518T130000Z
UID:TALK37426@talks.cam.ac.uk
CONTACT:Jonathan Goddard
DESCRIPTION:Many proteins in the eukaryotic cell are modified by O-linked 
 N-acetylglucosamine (O-GlcNAc) on serines and threonines. O-GlcNAcylation 
 has been shown to be important for regulation of the cell cycle\, DNA tran
 scription and translation\, insulin sensitivity and protein degradation. M
 isregulation of O-GlcNAcylation is associated with diabetes and Alzheimer'
 s disease. Two enzymes are involved in the dynamic cycling of this posttra
 nslational modification\, the O-GlcNAc transferase (OGT) and O-GlcNAcase (
 OGA). It has been demonstrated that this posttranslational modification oc
 curs on some serines/threonines that are also known phosphorylation sites 
 for a number of key kinases\, giving rise to the "yin-yang" theory\, that 
 proposes that O-GlcNAcylation is a means of regulating protein phosphoryla
 tion. Work in my group is aimed at studing this mechanism. We are studying
  the structures of OGA and OGT to gain\ninsight into substrate recognition
 \, and we have developed highly potent and selective inhibitors to study O
 -GlcNAcylation in live cells. Using these tools were are currently studyin
 g the role of O-GlcNAc in signalling pathways involved in diabetes\, cance
 r and Alzheimer's disease.
LOCATION:Pfizer Lecture Theatre\, Department of Chemistry
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