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SUMMARY:RNP granules in health and disease (via Zoom) - Roy Parker\, Inves
 tigator\, Howard Hughes Medical Institute\, Executive Director\, BioFronti
 ers Institute\, Distinguished Professor and Cech-Leinwand Endowed Chair of
  Biochemistry\, University of Colorado Boulder\,  USA
DTSTART:20200922T150000Z
DTEND:20200922T160000Z
UID:TALK151111@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:Eukaryotic cells contain multiple assemblies of RNA and protei
 n referred to as RNP granules\, or RNP condensates. In the cytosol\, ubiqu
 itous RNP granules include stress granules\, which form when translation i
 nitation is limited\, and P-bodies\, which are constitutive RNP granules c
 ontaining mRNAs and the RNA decay machinery. Both stress granules and P-bo
 dies contain complex proteomes and transcriptomes and their assembly/disas
 sembly are regulated by diverse RNP remodeling complexes.  \n\nFocusing on
  stress granules\, we have provided evidence that stress granule\, and pre
 sumably other RNP condensate\, assembly occurs in part through intermolecu
 lar RNA-RNA interactions. However\, based on in vitro studies\, we demonst
 rate that RNA condensation should be expected to be a thermodynamically fa
 vored process in cells. This argues cells must contain mechanisms to limit
  RNA driven condensation. We have demonstrated that abundant RNA helicase 
 reduces RNA recruitment to RNA condensates in vitro and in cells\, as well
  as limiting stress granule formation. This defines a new function for abu
 ndant RNA helicases to limit thermodynamically favored intermolecular RNA-
 RNA interactions in cells as “RNA decondenases”\, thereby allowing pro
 per RNP function\n\nhttps://zoom.us/j/95181300678?pwd=cUNLN0IwUXZROHYwRlIw
 QVRUNlhBUT09\n\nMeeting ID: 951 8130 0678 \nPasscode: 159352 \n
LOCATION:Webinar via Zoom
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