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SUMMARY:EPFL BioE Talks SERIES  "Harnessing Evolutionarily Optimized Signa
 ling Pathways for Therapeutic Benefits"
DTSTART:20210308T160000
DTEND:20210308T163000
DTSTAMP:20260405T191650Z
UID:258ad1752f77b1b693db0142d5a77ad41ee4d95aac1396d2d0be52fe
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Anne Bertolotti\, MRC Laboratory of Molecular Biology\, 
 Cambridge (UK)\nWEEKLY EPFL BIOE TALKS SERIES\n \n(note that this talk is
  number one of a double-feature seminar - see details of the second talk h
 ere)\n\nAbstract:\nDuring optimal conditions\, a majority of the cellular 
 resources is dedicated to protein synthesis. To survive under challenging 
 conditions\, cells adapt by phosphorylating the translation initiation fac
 tor\, eiF2 to reduce protein synthesis\, thereby sparing their resou
 rces to neutralize the challenges. We have exploited this pathway pharmaco
 logically and showed its benefits in diverse models of neurodegenerative d
 iseases. eIF2 phosphorylation is believed to cause a global reduction i
 n protein synthesis whilst enabling translation of few transcripts. A glob
 al reduction of protein synthesis comes with the life-threatening risk of 
 depleting essential proteins. We found that translation attenuation follow
 ing eIF2a phosphorylation is not as uniform as anticipated but preferentia
 lly targets long-lived proteins. This shows that protein stability buffers
  the cost of translational attenuation\, establishing an evolutionary prin
 ciple of cellular robustness.\n\nPhosphorylation of the translation initia
 tion factor eIF2a is a rapid and vital response to many forms of stress\, 
 including protein-misfolding stress in the endoplasmic reticulum (ER stres
 s). It is believed to cause a general reduction in protein synthesis while
  enabling translation of few transcripts. Such a reduction of protein synt
 hesis comes with the threat of depleting essential proteins\, a risk thoug
 ht to be mitigated by its transient nature. Here\, we find that translatio
 n attenuation is not uniform\, with cytosolic and mitochondrial ribosomal 
 sub- units being prominently downregulated. Translation attenuation of the
 se targets persists after translation recovery. Surprisingly\, this occurs
  without a measurable decrease in ribosomal proteins. Explaining this conu
 ndrum\, translation attenuation preferentially targets long-lived proteins
 \, a finding not only demonstrated by ribosomal proteins but also observed
  at a global level. This shows that protein stability buffers the cost of 
 translational attenuation\, establishing an evolutionary principle of cell
 ular robustness.\n\nBio:\nSince 2006: Group leader at MRC Laboratory of Mo
 lecular Biology\, Cambridge\, UK\n2014: Hooke medal\n2013: EMBO member\n20
 04: EMBO Young Investigator\n2001-2006: Associate professor\,\nEcole Norma
 le Supérieure\, Paris\, France\n1998-2000: Post-doctoral training with Pr
 of. David Ron\,\nThe Skirball Institute of Biomolecular Medicine\, NYU Med
 ical Center\, New York\, USA\nEMBO long term fellowship\nHFSP long term fe
 llowship\n1999: INSERM Position\n1993-1998: PhD training with Dr. Laszlo T
 ora and Prof. Pierre Chambon\,\nInstitut de Génétique et de Biologie Mol
 éculaire et Cellulaire\, Illkirch\, France.\n\n\n\nZoom link (with regist
 ration) for attending remotely: https://go.epfl.ch/EPFLBioETalks\n\n\nIMPO
 RTANT NOTICE: due to restrictions resulting from the ongoing Covid-19 pand
 emic\, this seminar can be followed via Zoom web-streaming only\, (followi
 ng prior one-time registration through the link above).
LOCATION:via Zoom web-streaming only\, due to Covid-19 pandemic https://go
 .epfl.ch/EPFLBioETalks https://go.epfl.ch/EPFLBioETalks
STATUS:CONFIRMED
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