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SUMMARY:Establishing a structure-function relationship between biomolecula
 r condensates and protein degradation - Janet Kumita\, Department of Pharm
 acology\, University of Cambridge
DTSTART:20230329T093000Z
DTEND:20230329T103000Z
UID:TALK198781@talks.cam.ac.uk
CONTACT:Alyssa Miller
DESCRIPTION:Our bodies contain some 100\,000 proteins that enable or regul
 ate essentially every biochemical process on which our lives depend. To ma
 intain healthy proteostasis\, cells have evolved intricate quality control
  networks that identify aberrant and damaged components and destroy them. 
 For this to occur\, cells need to spatially organise their components to p
 romote specific reactions and processes. The rapid formation and dissoluti
 on of membraneless\, biomolecular condensates (BCs) is key to many biologi
 cal roles\, including autophagy\, the cell’s waste disposal machinery. B
 Cs contain an array of different biomolecules and\, depending on their bio
 logical function\, they can be very fluid in nature or they can have a mor
 e gel-like composition\; therefore the dynamics and physical attributes of
  BCs appear to be closely linked with their biological roles. But how does
  the cell control the phase boundaries within live cells and how do they k
 now when to form droplets in the right place at the right time? Here we ar
 e exploring the design of novel proteins comprising molecular adhesive pep
 tides to drive liquid-liquid-phase separation (LLPS) and consensus tetratr
 icopeptide repeat units (CTPR) to endow the droplets with functional capab
 ilities in order to create well defined BCs. We want to characterise the p
 hysico-chemical properties of these LLPS-CTPR designs in vitro and relate 
 these attributes to their ability to induce autophagosome formation and su
 bsequent protein degradation in cells. We hope to establish a structure-fu
 nction relationship that will enable rational design of artificial phase-s
 eparating molecules that can drive the removal of disease-causing proteins
  from the cell.
LOCATION:Department of Chemistry\, Unilever Lecture Theatre
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