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SUMMARY:Chaperone networks coping with protein aggregates and amyloids - B
 ernd Bukau\, Center for Molecular Biology of Heidelberg University (ZMBH)
DTSTART:20181123T150000Z
DTEND:20181123T160000Z
UID:TALK113509@talks.cam.ac.uk
CONTACT:John Skidmore
DESCRIPTION:Misfolded proteins are sticky and tend to form intracellular a
 ggregates underpinning age-related deterioration and diseases including ca
 ncer and neurodegeneration. Normally\, multi-tiered cellular quality contr
 ol systems monitor and repair protein damage\, limiting aggregation. Sever
 e stress however overloads these systems allowing aggregates to accumulate
 . This activates a cellular machinery which mediates the organized aggrega
 tion of misfolded proteins as well as the subsequent solubilisation and re
 folding of aggregated proteins. This machinery plays a pivotal role in cel
 l survival under protein folding stress and in counteracting disease and a
 ge-associated cell toxicities.\nSmall heat shock proteins (sHsp) constitut
 e an evolutionary conserved yet diverse family of chaperones acting as fir
 st line of defense against proteotoxic stress. They promote the storage of
  misfolded proteins in native-like conformation facilitating disaggregatio
 n by ATP dependent chaperone systems. In plants\, fungi and bacteria the c
 entral disaggregation machinery is a powerful bi-chaperone system comprise
 d by the AAA+ disaggregase Hsp100 (Hsp104\, ClpB) and the cooperating Hsp7
 0 chaperone system. Metazoan cells lack Hsp100 disaggregases\, but have ev
 olved a potent Hsp70-based disaggregation machinery which relies on synerg
 istic action of Hsp70 and its co-chaperones. This activity has broad speci
 ficity and can even disassemble amyloid fibrils. This seminar provides ins
 ights into the working mode of the eukaryotic disaggregases in dealing wit
 h aggregates and amyloids.
LOCATION:The Sackler Lecture Theatre (Level 7) Wellcome Trust/MRC Building
 \, CIMR\, Addenbrooke's Site
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