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SUMMARY:Taming a protein destruction machine - Nicolas Thoma\, Friedrich M
 iescher Institute for Biomedical Reearch\, Basel\, Switzerland
DTSTART:20150129T161500Z
DTEND:20150129T180000Z
UID:TALK54690@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:The evolutionarily conserved CUL4 E3 ubiquitin ligases\, in co
 ncert with their DDB1 adaptor\, regulate a diverse set of cellular process
 es including development\, transcription\, replication and DNA repair. Wit
 hin the CRL4DDB2 ligase\, DDB2 recruits the ligase to damaged DNA. CRL4 sp
 ecificity is conferred upon by a set of more than a dozen substrate recept
 ors\, designated DCAFs (DDB1 CUL4 Associated Factors). While DDB2 is speci
 fic for finding UV-induced DNA lesions in the genome\, the remainder of th
 e ligase receptors serve in pathways unrelated to DNA damage recognition. 
 Using the CRL4DDB2 ligase as a model system\, we studied targeting and reg
 ulation of this bi-functional nano-machine\, investigating common architec
 tural and functional traits amongst the modular CRL4 ligases. We recently 
 also investigated how the Cop9 signalosome controls CRL function\, and how
  small molecules such as the drug thalidomide impact ligase activity.
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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