The adenine nucleotide translocator in apoptosis

• Published in: Biochimie Vol. 84; no. 2; pp. 167 - 176
• Main Authors: Belzacq, Anne-Sophie, Vieira, Helena L.A., Kroemer, Guido, Brenner, Catherine
• Format: Journal Article
• Language: English
• Published: France Elsevier Masson SAS 01.02.2002; Elsevier
• Subjects: Adenosine Triphosphate - metabolism; ADP/ATP exchange; Animals; Apoptosis - physiology; Bcl-2; bcl-2-Associated X Protein; Cell Membrane Permeability - physiology; Chemical Sciences; Humans; Liposome; Mitochondria - physiology; Mitochondrial ADP, ATP Translocases - physiology; Mitochondrion; Oncogene; Permeability transition; Proto-Oncogene Proteins - metabolism; Proto-Oncogene Proteins c-bcl-2 - physiology; Bcl-2; m-val-CsA; UCP; ADP/ATP exchange; ANT; t-BHP; PTPC; ΔΨm; pI; vMIA; Vpr; Atra; AIF; OM; MM; PBR; Catr; IM; Oncogene; Liposome; MU; MUP; Mitochondrion; CsA; MMP; Permeability transition; Anc; ROS; VDAC; BA
• ISSN: 0300-9084; 1638-6183
• DOI: 10.1016/S0300-9084(02)01366-4

Alteration of mitochondrial membrane permeability is a central mechanism leading invariably to cell death, which results, at least in part, from the opening of the permeability transition pore complex (PTPC). Indeed, extended PTPC opening is sufficient to trigger an increase in mitochondrial membrane permeability and apoptosis. Among the various PTPC components, the adenine nucleotide translocator (ANT) appears to act as a bi-functional protein which, on the one hand, contributes to a crucial step of aerobic energy metabolism, the ADP/ATP translocation, and on the other hand, can be converted into a pro-apoptotic pore under the control of onco- and anti-oncoproteins from the Bax/Bcl-2 family. In this review, we will discuss recent advances in the cooperation between ANT and Bax/Bcl-2 family members, the multiplicity of agents affecting ANT pore function and the putative role of ANT isoforms in apoptosis control.