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SUMMARY:Selective inhibition of phosphatases to boost protein quality cont
 rol : A possible treatment for degenerative diseases - Anne Bertolotti\, M
 RC Laboratory of Molecular Biology
DTSTART:20190605T093000Z
DTEND:20190605T103000Z
UID:TALK118987@talks.cam.ac.uk
CONTACT:Gabriella Heller
DESCRIPTION:The deposition of misfolded proteins is a defining feature of 
 many age-dependent human diseases\, including the increasingly prevalent n
 eurodegenerative diseases. Why misfolding-prone proteins accumulate in age
 d cells remains largely unclear. Cells normally strive to ensure that prot
 eins get correctly folded and have powerful and sophisticated protein qual
 ity control mechanisms to maintain protein homeostasis under adverse condi
 tions. However\, with age\, the cellular defence systems against misfolded
  proteins gradually fail\, leading to the accumulation of misfolded protei
 ns with devastating consequences for cells and organisms.\nIn principle\, 
 improving the cells’ ability to deal with misfolded proteins should repr
 esent a generic approach to reduce pathology in diverse protein misfolding
  diseases. My lab has identified powerful strategies to help cells survive
  when protein quality control fails and implemented some of these strategi
 es in mice. Exploiting the current knowledge on protein quality control sy
 stems\, we have identified a small drug-like molecule that safely boosts t
 he natural defence system against misfolded proteins. Our work demonstrate
 s that generic approaches aimed at helping cells to survive protein qualit
 y control failures can be useful to prevent protein misfolding diseases\, 
 including the devastating neurodegenerative diseases.\n \nThe small molecu
 les we have identified selectively inhibit  a regulatory subunit of a seri
 ne/threonine phosphatase controlling the termination of a proteostatic pat
 hway\, an interesting finding because phosphatases were previously thought
  to be undruggable. We have expanded on this idea and developed assays to 
 selectively inhibit regulatory subunits of phosphatases. The assays are ve
 rsatile and in principle\, generically applicable to any phosphatases. Thi
 s work has broad relevance because there are hundreds of phosphatases that
  could be inhibited using the same paradigm consisting of targeting their 
 regulatory subunits. This opens up a broad range of possibilities to manip
 ulate cellular function for therapeutic benefit.
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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