In this section
@article{Carrara:2015:10.7554/eLife.03522,
author = {Carrara, M and Prischi, F and Nowak, PR and Kopp, MC and Ali, MMU},
doi = {10.7554/eLife.03522},
journal = {eLife},
pages = {1--16},
title = {Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein C(H)1 to initiate ER stress signaling},
url = {http://dx.doi.org/10.7554/eLife.03522},
volume = {4},
year = {2015}
}
TY - JOUR
AB - The unfolded protein response (UPR) is an essential cell signaling system that detects the accumulation of misfolded proteins within the endoplasmic reticulum (ER) and initiates a cellular response in order to maintain homeostasis. How cells detect the accumulation of misfolded proteins remains unclear. In this study, we identify a noncanonical interaction between the ATPase domain of the ER chaperone BiP and the luminal domains of the UPR sensors Ire1 and Perk that dissociates when authentic ER unfolded protein CH1 binds to the canonical substrate binding domain of BiP. Unlike the interaction between chaperone and substrates, we found that the interaction between BiP and UPR sensors was unaffected by nucleotides. Thus, we discover that BiP is dual functional UPR sensor, sensing unfolded proteins by canonical binding to substrates and transducing this event to noncanonical, signaling interaction to Ire1 and Perk. Our observations implicate BiP as the key component for detecting ER stress and suggest an allosteric mechanism for UPR induction.
AU - Carrara,M
AU - Prischi,F
AU - Nowak,PR
AU - Kopp,MC
AU - Ali,MMU
DO - 10.7554/eLife.03522
EP - 16
PY - 2015///
SN - 2050-084X
SP - 1
TI - Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein C(H)1 to initiate ER stress signaling
T2 - eLife
UR - http://dx.doi.org/10.7554/eLife.03522
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000349821100001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://elifesciences.org/articles/03522
UR - http://hdl.handle.net/10044/1/21845
VL - 4
ER -
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