Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis |
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Authors: | I Marzo C Brenner N Zamzami JM Jürgensmeier SA Susin HL Vieira MC Prévost Z Xie S Matsuyama JC Reed G Kroemer |
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Affiliation: | CNRS, UPR 420, 19 rue Guy M?quet, F-94801 Villejuif, France. |
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Abstract: | The proapoptotic Bax protein induces cell death by acting on mitochondria. Bax binds to the permeability transition pore complex (PTPC), a composite proteaceous channel that is involved in the regulation of mitochondrial membrane permeability. Immunodepletion of Bax from PTPC or purification of PTPC from Bax-deficient mice yielded a PTPC that could not permeabilize membranes in response to atractyloside, a proapoptotic ligand of the adenine nucleotide translocator (ANT). Bax and ANT coimmunoprecipitated and interacted in the yeast two-hybrid system. Ectopic expression of Bax induced cell death in wild-type but not in ANT-deficient yeast. Recombinant Bax and purified ANT, but neither of them alone, efficiently formed atractyloside-responsive channels in artificial membranes. Hence, the proapoptotic molecule Bax and the constitutive mitochondrial protein ANT cooperate within the PTPC to increase mitochondrial membrane permeability and to trigger cell death. |
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