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SUMMARY:CANCELLED: Selective inhibition of phosphatases to boost protein q
 uality control : A possible treatment for degenerative diseases - Dr Anne 
 Bertolotti
DTSTART:20191126T130000Z
DTEND:20191126T140000Z
UID:TALK129607@talks.cam.ac.uk
CONTACT:38852
DESCRIPTION:The deposition of misfolded proteins is a defining feature of 
 many age-dependent human diseases\,including the increasingly prevalent ne
 urodegenerative diseases. Why misfolding-prone proteins accumulate in aged
  cells remains largely unclear.Cells normally strive to ensure that protei
 ns get correctly folded and have powerful and sophisticated protein qualit
 y control mechanisms to maintain protein homeostasis under adverse conditi
 ons. However\, with age\, the cellular defence systems against misfolded p
 roteins gradually fail\, leading to the accumulation of misfolded proteins
  with devastating consequences for cells andorganisms. \n\nIn principle\, 
 improving the cells’ ability to deal with misfolded proteins should repr
 esent a generic approach to reduce pathologyin diverse protein misfolding 
 diseases. My lab has identified powerful strategies to help cells survive 
 when protein quality control fails and implemented some of these strategie
 s in mice. Exploiting the current knowledge on protein quality control sys
 tems\, we have identified a small drug-like molecule that safely boosts th
 e natural defence system against misfolded proteins. Our work demonstrates
  that generic approaches aimed at helping cells to survive protein quality
  control failures can be useful to prevent protein misfolding diseases\,in
 cluding the devastating neurodegenerative diseases. \n\nThe small molecule
 s we have identified selectively inhibit  aregulatory subunit of a serine/
 threonine phosphatase controlling thetermination of a proteostatic pathway
 \, an interesting finding because phosphatases were previously thought to 
 be undruggable. We have expanded on this idea and developed assays to sele
 ctively inhibit regulatory subunits of phosphatases. The assays are versat
 ile and in principle\, generically applicable to any phosphatases. This wo
 rk has broad relevance because there are hundreds of phosphatases that cou
 ld be inhibited using the same paradigm consisting oftargeting their regul
 atory subunits. This opens up a broad range of possibilities to manipulate
  cellular function for therapeutic benefit. 
LOCATION:Department of Biochemistry\, Sanger Building\, Thomas Lecture The
 atre
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