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SUMMARY:Establishing a structure-function relationship between biomolecula
 r condensates and protein degradation - Dr Janet Kumita\; Dept of Pharmaco
 logy\, University of Cambridge 
DTSTART:20230613T123000Z
DTEND:20230613T133000Z
UID:TALK200797@talks.cam.ac.uk
CONTACT:Bobbie Claxton
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. \n\nJanet Kumita completed her undergraduate degree in Bio
 chemistry at the University of Waterloo  and her PhD in Chemistry at the U
 niversity of Toronto. In 2003\, she was awarded an NSERC Postdoctoral Fell
 owship and joined Prof. Sir Christopher Dobson’s group in the Department
  of Chemistry at the University of Cambridge\, investigating how extracell
 ular molecular chaperones modulate the amyloid formation of proteins assoc
 iated with neurodegenerative diseases and systemic amyloidosis. Janet spen
 t 17 years working closely with the Dobson group\, but in 2020 she moved t
 o the Department of Pharmacology to work with Prof. Laura Itzhaki. In Janu
 ary 2022\, Janet was awarded a MRC Career Development Award and became a G
 roup Leader in the Department of Pharmacology. Her research looks at decip
 hering the underlying mechanisms of protein self-assembly in order to find
  therapeutic strategies to combat neurodegenerative disorders.
LOCATION:Queen Edith's Room\, Babraham Research Campus
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