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International Journal of Cell BiologyVolume 2013 2013, Article ID 705294, 10 pages

Review Article

INSERM, U848, Institut Gustave Roussy, Pavillon de Recherche 1, 39 Rue Camille Desmoulins, 94805 Villejuif, France

Université Paris Sud-Paris XI, 94805 Villejuif, France

Institut Gustave Roussy, 94805 Villejuif, France

Université Paris Descartes-Paris V, Sorbonne Paris Cité, 75006 Paris, France

Metabolomics Platform, Institut Gustave Roussy, 94805 Villejuif, France

Pôle de Biologie, Hôpital Européen Georges Pompidou, AP-HP, 75015 Paris, France

Equipe 11 Labelisée par la Ligue Nationale Contre le Cancer, Centre de Recherche des Cordeliers, 75006 Paris, France

Received 30 November 2012; Revised 9 January 2013; Accepted 23 January 2013

Academic Editor: Marc Diederich

Copyright © 2013 Judith Michels et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The BCL-2 homolog BCL-XL, one of the two protein products of BCL2L1, has originally been characterized for its prominent prosurvival functions. Similar to BCL-2, BCL-XL binds to its multidomain proapoptotic counterparts BAX and BAK, hence preventing the formation of lethal pores in the mitochondrial outer membrane, as well as to multiple BH3-only proteins, thus interrupting apical proapoptotic signals. In addition, BCL-XL has been suggested to exert cytoprotective functions by sequestering a cytosolic pool of the pro-apoptotic transcription factor p53 and by binding to the voltage-dependent anion channel 1 VDAC1, thereby inhibiting the so-called mitochondrial permeability transition MPT. Thus, BCL-XL appears to play a prominent role in the regulation of multiple distinct types of cell death, including apoptosis and regulated necrosis. More recently, great attention has been given to the cell death-unrelated functions of BCL-2-like proteins. In particular, BCL-XL has been shown to modulate a number of pathophysiological processes, including—but not limited to—mitochondrial ATP synthesis, protein acetylation, autophagy and mitosis. In this short review article, we will discuss the functions of BCL-XL at the interface between cell death and metabolism.

Author: Judith Michels, Oliver Kepp, Laura Senovilla, Delphine Lissa, Maria Castedo, Guido Kroemer, and Lorenzo Galluzzi



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