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SUMMARY:Recent aspects of chaperone functions in health and disease - A BI
 OLOGICAL RIG SEMINAR - Prof. Ulrich Hartl - Max-Planck-Institute of Bioche
 mistry
DTSTART:20250408T140000Z
DTEND:20250408T150000Z
UID:TALK229738@talks.cam.ac.uk
CONTACT:Echo Wu Williamson
DESCRIPTION:Recent aspects of molecular chaperone function in health and d
 isease\nF. Ulrich Hartl\nDepartment of Cellular Biochemistry\, Max Planck 
 Institute of Biochemistry\, Martinsried\, Germany\nWhile protein folding w
 as originally assumed to occur spontaneously\, we now appreciate that in t
 he crowded environment of cells\, newly-synthesized polypeptides depend on
  molecular chaperones to reach their folded states efficiently and at a bi
 ologically relevant time scale. Assistance of protein folding is provided 
 by members of different chaperone classes acting to facilitate the interco
 nversion of folding intermediates\, preventing misfolding and off-pathway 
 aggregation\, often in an ATP-dependent mechanism. A well-studied example 
 are the cylindrical chaperonins (GroEL/ES in bacteria\, Hsp60 in mitochond
 ria\, TRiC in the eukaryotic cytosol)\, which form nano-cages for single p
 rotein molecules to fold unimpaired by aggregation. As an added benefit\, 
 encapsulation results in entropic confinement of dynamic folding intermedi
 ates\, thereby markedly accelerating folding for some proteins over the sp
 ontaneous folding rate. \n\nOnce folded\, many proteins continue to requir
 e chaperone surveillance to retain their functional states\, especially un
 der conditions of cell stress. Failure of the chaperone machinery to maint
 ain proteostasis\, i.e. the conformational integrity and balance of the ce
 llular proteome\, facilitates the manifestation of diseases in which prote
 ins misfold and form toxic aggregates. These disorders include\, among oth
 ers\, Alzheimer’s\, Parkinson’s\, and Huntington’s disease. \n\nI wi
 ll provide an overview of chaperone mechanisms and then discuss recent wor
 k providing new insights into the role of chaperones in protein folding an
 d proteostasis maintenance\, with a focus on observations in intact cells.
 \n\n
LOCATION:Department of Chemistry\, Cambridge\, Pfizer LT
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