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SUMMARY:Mechanisms for the Selective Degradation of Ubiquitinated Proteins
  by the 26S Proteasome - Fred Goldberg\, Harvard Medical School
DTSTART:20120622T151500Z
DTEND:20120622T170000Z
UID:TALK37979@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:The 26S Proteasome is the major site for protein degradation i
 n  eukaryotic cells and selectively digests proteins marked for degradatio
 n by attachment of a  ubiquitin chain.   Recent studies indicate multiple 
 ATP-dependent steps in this process and clarify how certain types of ubiqu
 itinated proteins become tightly bound  and how deubiquitination\, ATP hyd
 rolysis\, and proteolysis are coupled.  In this process\, the six proteaso
 mal AAA ATPase subunits  function cooperatively to drive protein unfolding
  translocation\, and opening the gate for substrate-entry into the 20S pro
 teolytic core.  Prof Goldberg will also discuss how proteasome function is
  impaired in certain neurodegenerative disease and the development of the 
 proteasome inhibitors\, now widely used as scientific reagents and in the 
 treatment of hematologic cancers. 
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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