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DTSTART:20200329T030000
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DTSTART:20191027T020000
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DTSTAMP:20260405T014601Z
UID:5da42e48a036c358028609@ist.ac.at
DTSTART:20191106T113000
DTEND:20191106T123000
DESCRIPTION:Speaker: Elif Karagöz\nhosted by Martin Loose\nAbstract: To ad
 just the folding capacity of the endoplasmic reticulum (ER)\, cells rely o
 n the unfolded protein response (UPR)\, a signaling network that relays th
 e ER folding status to the nucleus via ER-resident sensors. IRE1 is the mo
 st conserved sensor and is found from yeast to human. How IRE1 senses ER-s
 tress remained elusive. Early models suggested that the ER-resident chaper
 one BiP to be the sole regulator of IRE1 activity. We recently showed that
  IRE1s sensor domain recognizes unfolded polypeptides accumulating in the 
 ER as direct ligands. Using nuclear magnetic resonance (NMR) spectroscopy 
 experiments\, we found that unfolded proteins bind to the MHC-like fold in
  the human IRE1 lumenal domain (LD) and induce a conformational change in 
 a distant helix that promotes its oligomerization. Instead\, the NMR appro
 aches revealed that the ER-resident chaperone BiP binds to a distinct site
  at the periphery of IRE1 LD dimers and modulates its oligomerization. Our
  results support the model that unfolded protein binding activates IRE1 di
 rectly and a non-canonical chaperone binding buffers IRE1 activity.
LOCATION:Mondi Seminar Room 2\, Central Building\, ISTA
ORGANIZER:rsix@ist.ac.at
SUMMARY:Elif Karagöz: Structural insights into stress sensing mechanisms i
 n the endoplasmic reticulum
URL:https://talks-calendar.ista.ac.at/events/2379
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