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J. Biol. Chem., Vol. 282, Issue 34, 24938-24947, August 24, 2007

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Control of Bax Homodimerization by Its Carboxyl Terminus^*

Emine Er, Lisenn Lalier, Pierre-François Cartron, Lisa Oliver, and François M. Vallette¹

From the INSERM U601, Département de Recherches en Cancérologie de Nantes and the Université de Nantes, Faculté de Médecine, 9 Quai Moncousu F-44035 Nantes, Cedex 01 France

The regulated oligomerization of proteins is increasingly understood to be an important step in many cellular processes, including signaling, transcription, and protein degradation. The activity of Bax, which is essential for the completion of apoptosis, has been shown to be associated with its oligomerization: homodimerization that appears to facilitate mitochondrial permeabilization during apoptosis and heterodimerization with multidomain anti-apoptotic members of the Bcl-2 family inhibiting this process. Several domains have been identified to be crucial in the homo-/heterodimerization or oligomerization of Bax, especially the so-called Bax homology 3 domain. In this study we show that although the carboxyl terminus of Bax is not implicated in its mitochondrial localization, it has a role in the dimerization process and thus in its activity.

Received for publication, May 9, 2007

^* This work was supported by grants from Ligue Nationale Contre le Cancer (program équipe labelisé), INSERM, and the Agence Nationale de la Recherche (Projet MABA). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2.

¹ To whom correspondence should be addressed. Tel.: 33-240084081; Fax: 33-240084082; E-mail: francois.vallette{at}univ-nantes.fr.

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