BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Talks.cam//talks.cam.ac.uk//
X-WR-CALNAME:Talks.cam
BEGIN:VEVENT
SUMMARY:Proteostasis function and disfunction: the folding machines that m
 aintain proteome health  - Judith Frydman\, Stanford University
DTSTART:20190426T100000Z
DTEND:20190426T110000Z
UID:TALK122743@talks.cam.ac.uk
CONTACT:Gabriella Heller
DESCRIPTION:Correct protein folding and quality control are essential for 
 normal cellular function. The accumulation of misfolded proteins is emergi
 ng as central to a wide range of disease states\, including many neurodege
 nerative disorders such as Huntington’s and Alzheimer’s Disease. In eu
 karyotes\, a complex network of molecular chaperones facilitate protein fo
 lding  and monitor all aspects of protein homeostasis. \nOur research inve
 stigates the mechanisms and pathways by which chaperones carry out these d
 iverse functions.  We find that distinct chaperone networks assist the fol
 ding of newly translated and the quality control of stress-denatured prote
 ins. A chaperone network linked to the protein synthesis apparatus assists
  protein biogenesis.  The emergence of this translation-linked chaperone n
 etwork likely underlies the elaborate co-translational folding process nec
 essary for the evolution of larger multidomain proteins characteristic of 
 eukaryotic cells. A stress-inducible chaperone network protects cells from
  environmental stress and assists quality control. These chaperones also c
 ommunicate with the ubiquitin-proteasome pathway to clear misfolded protei
 ns from the cell.  Protein quality control in the eukaryotic cytosol  also
  relies on the chaperone-mediated sequestration of misfolded cytosolic pro
 teins in specific quality control compartments. Our studies of chaperone f
 unction provide a framework to understand the link between protein misfold
 ing and human diseases. 
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
END:VEVENT
END:VCALENDAR