title: Functions of BCL-X L at the Interface between Cell Death and Metabolism.
abstract: 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.
authors.affiliation: 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.
authors.forename: Judith
authors.initials: J
authors.lastname: Michels
authors.forename: Oliver
authors.initials: O
authors.lastname: Kepp
authors.forename: Laura
authors.initials: L
authors.lastname: Senovilla
authors.forename: Delphine
authors.initials: D
authors.lastname: Lissa
authors.forename: Maria
authors.initials: M
authors.lastname: Castedo
authors.forename: Guido
authors.initials: G
authors.lastname: Kroemer
authors.forename: Lorenzo
authors.initials: L
authors.lastname: Galluzzi