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J. Biol. Chem., Vol. 281, Issue 47, 36187-36197, November 24, 2006

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Evaluation of the Roles of Apoptosis, Autophagy, and Mitophagy in the Loss of Plating Efficiency Induced by Bax Expression in Yeast^*

Ingrid Kiová¹, Louis-Thomas Plamondon^¶, Louise Brisson^¶, Muriel Priault, Vincent Renouf, Jacques Schaeffer^||, Nadine Camougrand², and Stéphen Manon³

From the UMR5095 CNRS/Université de Bordeaux 2, 1 Rue Camille Saint-Saëns, 33077 Bordeaux Cedex, France, the Department of Biochemistry, Faculty of Natural Sciences, Comenius University, Mlynska Dolina CH-1, 84215 Bratislava, Slovak Republic, the ^¶Département de Biochimie et de Microbiologie, Université Laval, Québec G1K 7P4, Canada, and the ^||Service Commun de Microscopie, Université de Bordeaux 2, 146 Rue Léo Saignat, 33076 Bordeaux Cedex, France

We found recently that, in yeast cells, the heterologous expression of Bax induces a loss of plating efficiency different from that induced by acute stress because it is associated with the maintenance of plasma membrane integrity (Camougrand, N., Grelaud-Coq, A., Marza, E., Priault, M., Bessoule, J. J., and Manon, S. (2003) Mol. Microbiol. 47, 495-506). Bax effects were neither dependent on the presence of the yeast metacaspase Yca1p and the apoptosis-inducing factor homolog nor associated with the appearance of typical apoptotic markers such as metacaspase activation, annexin V binding, and DNA cleavage. Yeast cells expressing Bax instead displayed autophagic features, including increased accumulation of Atg8p, activation of vacuolar alkaline phosphatase, and the presence of autophagosomes and autophagic bodies. However, the inactivation of autophagy did not prevent and actually slightly accelerated Bax-induced loss of plating efficiency. On the other hand, Bax expression induced a fragmentation of the mitochondrial network, which retained, however, some level of organization in wild-type cells. However, when expressed in cells inactivated for the gene UTH1, previously shown to be involved in mitophagy, Bax induced a complete disorganization of the mitochondrial network. Interestingly, although mitochondrially targeted green fluorescent protein was slowly degraded in the wild-type strain, it remained unaffected in the mutant. Furthermore, the slow loss of plating efficiency in the mutant strain correlated with a loss of plasma membrane integrity. These data suggest that Bax-induced loss of growth capacity is associated with maintenance of plasma membrane integrity dependent on UTH1, suggesting that selective degradation of altered mitochondria is required for a regulated loss of growth capacity.

Received for publication, August 4, 2006 , and in revised form, September 18, 2006.

^* This work was supported in part by grants from CNRS, the Université de Bordeaux 2, and the Conseil Régional d'Aquitaine (to UMR5095); by Science and Technology Assistance Agency Grant APVT-20-012404 (to I. K.); and by Association pour la Recherche contre le Cancer Grant 3812 (to S. M.). The France/Slovakia collaboration was supported by Égide ECO-NET 10187VF (to S. M.). 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.

¹ Recipient of a post-doctoral fellowship from the Fondation pour la Recherche Médicale.

² To whom correspondence may be addressed. Tel.: 33-556-99-9045; Fax: 33-556-99-9051; E-mail: n.camougrand{at}ibgc.cnrs.fr. ³ To whom correspondence may be addressed. Tel.: 33-556-99-9045; Fax: 33-556-99-9051; E-mail: stephen.manon{at}ibgc.cnrs.fr.

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