Imperial College London

ProfessorGuyRutter

Faculty of MedicineDepartment of Medicine

Visiting Professor
 
 
 
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Contact

 

+44 (0)20 7594 3340g.rutter Website

 
 
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Location

 

ICTEM buildingHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Parks:2021:10.1002/1873-3468.14101,
author = {Parks, SZ and Gao, T and Awuapura, NJ and Ayathamattam, J and Chabosseau, PL and Kalvakolanu, D and Valdivia, HH and Rutter, GA and Leclerc, I and Nakatogawa, H},
doi = {10.1002/1873-3468.14101},
journal = {FEBS Letters},
pages = {1782--1796},
title = {The Ca2+-binding protein sorcin stimulates transcriptional activity of the unfolded protein response mediator ATF6},
url = {http://dx.doi.org/10.1002/1873-3468.14101},
volume = {595},
year = {2021}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Sorcin is a calcium-binding protein involved in maintaining endoplasmic reticulum (ER) Ca2+ stores. We have previously shown that overexpressing sorcin under the rat insulin promoter was protective against high-fat diet-induced pancreatic beta-cell dysfunction in vivo. Activating transcription factor 6 (ATF6) is a key mediator of the unfolded protein response (UPR) that provides cellular protection during the progression of ER stress. Here, using nonexcitable HEK293 cells, we show that sorcin overexpression increased ATF6 signalling, whereas sorcin knock out caused a reduction in ATF6 transcriptional activity and increased ER stress. Altogether, our data suggest that sorcin downregulation during lipotoxic stress may prevent full ATF6 activation and a normal UPR during the progression of obesity and insulin resistance.
AU - Parks,SZ
AU - Gao,T
AU - Awuapura,NJ
AU - Ayathamattam,J
AU - Chabosseau,PL
AU - Kalvakolanu,D
AU - Valdivia,HH
AU - Rutter,GA
AU - Leclerc,I
AU - Nakatogawa,H
DO - 10.1002/1873-3468.14101
EP - 1796
PY - 2021///
SN - 0014-5793
SP - 1782
TI - The Ca2+-binding protein sorcin stimulates transcriptional activity of the unfolded protein response mediator ATF6
T2 - FEBS Letters
UR - http://dx.doi.org/10.1002/1873-3468.14101
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000653160600001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14101
UR - http://hdl.handle.net/10044/1/89478
VL - 595
ER -