Bid-induced Conformational Change of Bax Is Responsible for Mitochondrial Cytochrome c Release during Apoptosis

doi:10.1083/jcb.144.5.891

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J. Cell Biol., Volume 144, Number 5, March 8, 1999 891-901

Bid-induced Conformational Change of Bax Is Responsible for Mitochondrial Cytochrome c Release during Apoptosis

Solange Desagher, Astrid Osen-Sand, Anthony Nichols, Robert Eskes, Sylvie Montessuit, Sandra Lauper, Kinsey Maundrell, Bruno Antonsson, and Jean-Claude Martinou

Serono Pharmaceutical Research Institute, Ares-Serono International S.A., CH-1228 Plan-les-Ouates, Geneva, Switzerland

Here we report that in staurosporine-induced apoptosis of HeLa cells, Bid, a BH3 domain containing protein, translocates fromthe cytosol to mitochondria. This event is associated with a changein conformation of Bax which leads to the unmasking of its NH₂-terminaldomain and is accompanied by the release of cytochrome c frommitochondria. A similar finding is reported for cerebellar granulecells undergoing apoptosis induced by serum and potassium deprivation.The Bax-conformational change is prevented by Bcl-2 and Bcl-x_Lbut not by caspase inhibitors. Using isolated mitochondria andvarious BH3 mutants of Bid, we demonstrate that direct bindingof Bid to Bax is a prerequisite for Bax structural change andcytochrome c release. Bcl-x_L can inhibit the effect of Bid byinteracting directly with Bax. Moreover, using mitochondria fromBax-deficient tumor cell lines, we show that Bid- induced releaseof cytochrome c is negligible when Bid is added alone, but dramaticallyincreased when Bid and Bax are added together. Taken together,our results suggest that, during certain types of apoptosis, Bidtranslocates to mitochondria and binds to Bax, leading to a changein conformation of Bax and to cytochrome c release frommitochondria.

Key words: apoptosis; Bax; Bid; cytochrome c; mitochondria

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