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SUMMARY:Controlling Protein Damage - Dr. Stefan Rüdiger\, Utrecht Univers
 ity
DTSTART:20151028T103000Z
DTEND:20151028T113000Z
UID:TALK62165@talks.cam.ac.uk
CONTACT:Jerome Charmet
DESCRIPTION:Molecular chaperones such as the Hsp90 chaperone are the first
  line of the cellular defense system against protein damage and aggregatio
 n. The chaperones are part of the proteostasis network\, the natural defen
 se system against protein damage problems. Hsp90 interacts in vivo and in 
 vitro with the Tau protein\, the molecular basis of this interaction remai
 ned enigmatic. We disclosed a structural model of the Hsp90-Tau complex\, 
 showing the Tau protein behaves as a bona fide client of the Hsp90 chapero
 ne. Hsp90 binds to a broad region in Tau that includes the aggregation-pro
 ne repeats. Our model resolves the paradox on how Hsp90 specifically selec
 ts for late folding intermediates but also intrinsically disordered protei
 ns such as Tau. Our data offer a mechanistic understanding how molecular c
 haperones can deal with aggregates in neurodegenerative diseases.
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theater
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