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CATEGORIES:Biophysical Seminars
SUMMARY:Proteostasis function and disfunction: the folding
  machines that maintain proteome health  - Judith 
 Frydman\, Stanford University
DTSTART;TZID=Europe/London:20190426T110000
DTEND;TZID=Europe/London:20190426T120000
UID:TALK122743AThttp://talks.cam.ac.uk
URL:http://talks.cam.ac.uk/talk/index/122743
DESCRIPTION:Correct protein folding and quality control are es
 sential for normal cellular function. The accumula
 tion of misfolded proteins is emerging as central 
 to a wide range of disease states\, including many
  neurodegenerative disorders such as Huntington’s 
 and Alzheimer’s Disease. In eukaryotes\, a complex
  network of molecular chaperones facilitate protei
 n folding  and monitor all aspects of protein home
 ostasis. \nOur research investigates the mechanism
 s and pathways by which chaperones carry out these
  diverse functions.  We find that distinct chapero
 ne networks assist the folding of newly translated
  and the quality control of stress-denatured prote
 ins. A chaperone network linked to the protein syn
 thesis apparatus assists protein biogenesis.  The 
 emergence of this translation-linked chaperone net
 work likely underlies the elaborate co-translation
 al folding process necessary for the evolution of 
 larger multidomain proteins characteristic of euka
 ryotic cells. A stress-inducible chaperone network
  protects cells from environmental stress and assi
 sts quality control. These chaperones also communi
 cate with the ubiquitin-proteasome pathway to clea
 r misfolded proteins from the cell.  Protein quali
 ty control in the eukaryotic cytosol  also relies 
 on the chaperone-mediated sequestration of misfold
 ed cytosolic proteins in specific quality control 
 compartments. Our studies of chaperone function pr
 ovide a framework to understand the link between p
 rotein misfolding and human diseases. 
LOCATION:Department of Chemistry\, Cambridge\, Unilever lec
 ture theatre
CONTACT:Gabriella Heller
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