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SUMMARY:Pharmacology Seminar Series: Professor David Ron\, How is Endoplas
 mic Reticulum Stress Recognised? - Professor David Ron
DTSTART:20260213T130000Z
DTEND:20260213T140000Z
UID:TALK242101@talks.cam.ac.uk
CONTACT:116482
DESCRIPTION:Friday 13 February\, 13:00 - 14:00\n\nSpeaker: Professor David
  Ron\n\nTalk Title: How is Endoplasmic Reticulum Stress Recognised?\n\nBio
 graphy: David studies the adaptation of eukaryotic cells to the burden of 
 unfolded proteins in their endoplasmic reticulum (ER). The context for thi
 s research is the observation that cells have mechanisms to ensure proper 
 folding of proteins\, but failures to maintain the proteome lead to toxic 
 effects known as ‘proteotoxicity’. The latter affects poorly renewable
  tissues of long-lived organisms\, exerting its deleterious consequences o
 ver extended periods of time. The accumulative erosive effects of proteoto
 xicity are believed to contribute to numerous diseases of ageing.\n\nTo me
 et this challenge\, eukaryotes have evolved signalling pathways that detec
 t the level of mismatch between burden and capacity (resulting in ER stres
 s) and elicit rectifying responses. Collectively this constitutes an unfol
 ded protein response (UPR) and is the focus of our lab.\n\nTheir long-term
  goal is to contribute to a detailed molecular understanding of protein fo
 lding homeostasis in the ER and to exploit this insight to develop tools f
 or manipulating the UPR and possible therapies for inevitable failures of 
 homeostasis. In this vein\, our most important accomplishments of recent y
 ears are the elucidation of the biochemical basis of UPR activation and th
 e discovery of a stress-responsive enzymatic mechanism that matches ER cha
 perone activity to unfolded protein burden post-translationally.
LOCATION:Seminar Room (Level 2)\, Dept of Pharmacology 
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