IMR Press / FBE / Volume 3 / Issue 2 / DOI: 10.2741/E255

Frontiers in Bioscience-Elite (FBE) is published by IMR Press from Volume 13 Issue 2 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.


The respiratory-dependent assembly of ANT1 regulates cytochrome c release 

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1 INSERM U688, Universite Victor Segalen-Bordeaux 2, 146 rue Leo-Saignat, F-33076 Bordeaux Cedex, France
2 University of Versailles/St Quentin, PRES UniverSud Paris, CNRS UMR 8159, Bat Buffon, 45 avenue des Etats-Unis, F-78035 Versailles, France
3 Centre de genomique fonctionnelle, Universite Victor Segalen-Bordeaux 2, 146 rue Leo-Saignat, F-33076 Bordeaux Cedex, France
4 Univ Paris-Sud, INSERM UMR-S 769, PRES UniverSud Paris, Châtenay-Malabry, 92290, France

*Author to whom correspondence should be addressed,


Front. Biosci. (Elite Ed) 2011, 3(2), 395–409;
Published: 1 January 2011

The adenine nucleotide translocator (ANT) is a control point of several fundamental cell processes, as diverse as cell energy supply, mitochondrial DNA maintenance, and apoptosis. This paper describes six individual structures of the carrier, distinguished according to ANT1 oligomeric and conformational states, as well as associations with other proteins. Transitions between these structures depend on energy demand and thus contribute to a metabolic reserve of oxidative phosphorylation (OXPHOS) activity. Moreover, at low respiratory chain activity, we demonstrate that, unlike a mitochondrial Ca2+ upload, Bax, a pro-apoptotic Bcl-2-family protein, is able to trigger a massive release of cytochrome c from one of these ANT1 structures. These new insights emphasize the close relationship between structural rearrangements of ANT and molecular apoptotic events at distinct cell energy levels. OXPHOS functioning has to therefore be considered a crucial control point for the events leading to these contrasting pathways.

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