BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Talks.cam//talks.cam.ac.uk//
X-WR-CALNAME:Talks.cam
BEGIN:VEVENT
SUMMARY:Regulation of proteasome function in normal and disease states - P
 rofessor Alfred Goldberg\, Harvard Medical School
DTSTART:20150515T151500Z
DTEND:20150515T161500Z
UID:TALK59479@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:Synopsis: It is generally assumed that degradation by the ubiq
 uitin-proteasome pathway is regulated solely by ubiquitination.  However\,
  we recently found several novel cellular mechanism that regulate proteaso
 me content and functional capacity.  When proteasomes are inhibited pharma
 cologically or become stalled\, they have a mechanism that prevents furthe
 r binding of ubiquitin conjugates\, and they stimulate production of new p
 roteasomes by enhancing transcription of genes for all proteasome subunits
 . We also have found that proteasome capacity to degrade ubiquitin conjuga
 tes and misfolded aggregation-prone proteins in cells is enhanced by phosp
 horylation of a 19S regulatory subunit. In certain mouse or cellular model
 s of neurodegenerative disease\, the 26S proteasome’s capacity to degrad
 e ubiquitinated proteins is impaired\, but can be activated by pharmacolog
 ical agents that promote proteasome phosphorylation and thus enhance the d
 egradation of the toxic proteins.
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
END:VEVENT
END:VCALENDAR