Bax mitochondrial relocation is linked to its phosphorylation and its interaction with Bcl-xL

Authors:

David Garenne1,2, Thibaud T. Renault1,3, Stéphen Manon1

doi: 10.15698/mic2016.12.547
Volume 3, pp. 597 to 605, published 05/12/2016.

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Affiliations:

1 Institut de Biochimie et de Génétique Cellulaires, UMR5095, CNRS & Université de Bordeaux, CS61390, 146 Rue Léo Saignat, 33077 Bordeaux, France.

2 Present address: INRA, UMR1332, 71 Avenue Edouard Bourlaud, 33882 Villenave d’Ornon, France.

3 Present address: Department of Regulation in Infection Biology, Charitéplatz 1, 10117 Berlin, Germany.

Keywords: 

Bax, Bcl-xL, mitochondria, phosphorylation, cytochrome c release, apoptosis, yeast (S.cerevisiae).

Corresponding Author(s):

Stéphen Manon, manon@ibgc.cnrs.fr

Conflict of interest statement:

The authors declare no conflict of interest.

Please cite this article as:

David Garenne, Thibaud T. Renault, Stéphen Manon (2016). Bax mitochondrial relocation is linked to its phosphorylation and its interaction with Bcl-xL. Microbial Cell 3(12): 597-605. doi: 10.15698/mic2016.12.547

© 2016 Garenne et al. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.

Abstract:

The heterologous expression of Bax, and other Bcl-2 family members, in the yeast Saccharomyces cerevisiae, has proved to be a valuable reporter system to investigate the molecular mechanisms underlying their interaction with mitochondria. By combining the co-expression of Bax and Bcl-xL mutants with analyzes of their localization and interaction in mitochondria and post-mitochondrial supernatants, we showed that the ability of Bax and Bcl-xL to interact is dependent both on Bax phosphorylation – mimicked by a substitution S184D – and by Bax and Bcl-xL localization. This, and previous data, provide the molecular basis for a model of dynamic equilibrium for Bax localization and activation, regulated both by phosphorylation and Bcl-xL.