Imperial College London

Dr Kambiz N. Alavian, PhD, SFHEA, FLS, FRSB

Faculty of MedicineDepartment of Brain Sciences

Reader in Neuroscience
 
 
 
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Contact

 

+44 (0)20 7594 7006k.alavian Website

 
 
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Assistant

 

Mrs Hadeel Abdeen +44 (0)20 7594 7014

 
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Location

 

E507Burlington DanesHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Chen:2011:10.1083/jcb.201108059,
author = {Chen, Y-B and Aon, MA and Hsu, Y-T and Soane, L and Teng, X and McCaffery, JM and Cheng, W-C and Qi, B and Li, H and Alavian, KN and Dayhoff-Brannigan, M and Zou, S and Pineda, FJ and O'Rourke, B and Ko, YH and Pedersen, PL and Kaczmarek, LK and Jonas, EA and Hardwick, JM},
doi = {10.1083/jcb.201108059},
journal = {The Journal of Cell Biology},
pages = {263--276},
title = {Bcl-x(L) regulates mitochondrial energetics by stabilizing the inner membrane potential},
url = {http://dx.doi.org/10.1083/jcb.201108059},
volume = {195},
year = {2011}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Mammalian Bcl-xL protein localizes to the outer mitochondrial membrane, where it inhibits apoptosis by binding Bax and inhibiting Bax-induced outer membrane permeabilization. Contrary to expectation, we found by electron microscopy and biochemical approaches that endogenous Bcl-xL also localized to inner mitochondrial cristae. Two-photon microscopy of cultured neurons revealed large fluctuations in inner mitochondrial membrane potential when Bcl-xL was genetically deleted or pharmacologically inhibited, indicating increased total ion flux into and out of mitochondria. Computational, biochemical, and genetic evidence indicated that Bcl-xL reduces futile ion flux across the inner mitochondrial membrane to prevent a wasteful drain on cellular resources, thereby preventing an energetic crisis during stress. Given that F1FO–ATP synthase directly affects mitochondrial membrane potential and having identified the mitochondrial ATP synthase β subunit in a screen for Bcl-xL–binding partners, we tested and found that Bcl-xL failed to protect β subunit–deficient yeast. Thus, by bolstering mitochondrial energetic capacity, Bcl-xL may contribute importantly to cell survival independently of other Bcl-2 family proteins.
AU - Chen,Y-B
AU - Aon,MA
AU - Hsu,Y-T
AU - Soane,L
AU - Teng,X
AU - McCaffery,JM
AU - Cheng,W-C
AU - Qi,B
AU - Li,H
AU - Alavian,KN
AU - Dayhoff-Brannigan,M
AU - Zou,S
AU - Pineda,FJ
AU - O'Rourke,B
AU - Ko,YH
AU - Pedersen,PL
AU - Kaczmarek,LK
AU - Jonas,EA
AU - Hardwick,JM
DO - 10.1083/jcb.201108059
EP - 276
PY - 2011///
SN - 0021-9525
SP - 263
TI - Bcl-x(L) regulates mitochondrial energetics by stabilizing the inner membrane potential
T2 - The Journal of Cell Biology
UR - http://dx.doi.org/10.1083/jcb.201108059
UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000296205300010&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://rupress.org/jcb/article/195/2/263/36649/Bcl-xL-regulates-mitochondrial-energetics-by
UR - http://hdl.handle.net/10044/1/103365
VL - 195
ER -