Imperial College London
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DrMarufAli

Faculty of Natural Sciences, Department of Life Sciences

Reader in Molecular and Structural Biology
 
 
 
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Contact

 

+44 (0)20 7594 5733maruf.ali Website

 
 
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Location

 

505Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Kopp:2019:10.1038/s41594-019-0324-9,
author = {Kopp, MC and Larburu, N and vinoth, D and Adams, CJ and Ali, MMU},
doi = {10.1038/s41594-019-0324-9},
journal = {Nature Structural and Molecular Biology},
pages = {1053--1062},
title = {UPR proteins IRE1 and PERK switch BiP from chaperone to ER stress sensor},
url = {http://dx.doi.org/10.1038/s41594-019-0324-9},
volume = {26},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - BiP is a major ER chaperone and suggested to act as primary sensor in the activationof the unfolded protein response (UPR). How BiP operates as a molecular chaperoneand as an ER stress sensor is unknown. Here, by reconstituting components ofhuman UPR, ER stress and BiP chaperone systems, we discover that the interactionof BiP with the luminal domains (LD) of UPR proteins, IRE1 and PERK, switch BiPfrom its chaperone cycle into an ER stress sensor cycle by preventing the binding ofits cochaperones, with loss of ATPase stimulation. Furthermore, misfolded proteindependentdissociation of BiP from IRE1 is primed by ATP but not ADP. Our dataelucidate a previously unidentified mechanistic cycle of BiP function that explains itsability to act as a Hsp70 chaperone and ER stress sensor.
AU  - Kopp,MC
AU  - Larburu,N
AU  - vinoth,D
AU  - Adams,CJ
AU  - Ali,MMU
DO  - 10.1038/s41594-019-0324-9
EP  - 1062
PY  - 2019///
SN  - 1545-9985
SP  - 1053
TI  - UPR proteins IRE1 and PERK switch BiP from chaperone to ER stress sensor
T2  - Nature Structural and Molecular Biology
UR  - http://dx.doi.org/10.1038/s41594-019-0324-9
UR  - http://hdl.handle.net/10044/1/74374
VL  - 26
ER  -
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