Bax and Adenine Nucleotide Translocator Cooperate in the Mitochondrial Control of Apoptosis
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...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1998-09, Vol.281 (5385), p.2027-2031 |
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| creator | Marzo, Isabel Brenner, Catherine Zamzami, Naoufal Jürgensmeier, Juliane M. Susin, Santos A. Helena L. A. Vieira Prévost, Marie-Christine Xie, Zhihua Matsuyama, Shigemi Reed, John C. Kroemer, Guido |
| description | 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. |
| doi_str_mv | 10.1126/science.281.5385.2027 |
| format | Article |
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A. Vieira ; Prévost, Marie-Christine ; Xie, Zhihua ; Matsuyama, Shigemi ; Reed, John C. ; Kroemer, Guido</creator><creatorcontrib>Marzo, Isabel ; Brenner, Catherine ; Zamzami, Naoufal ; Jürgensmeier, Juliane M. ; Susin, Santos A. ; Helena L. A. Vieira ; Prévost, Marie-Christine ; Xie, Zhihua ; Matsuyama, Shigemi ; Reed, John C. ; Kroemer, Guido</creatorcontrib><description>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.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.281.5385.2027</identifier><identifier>PMID: 9748162</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Ageing, cell death ; Animals ; Apoptosis ; Atractyloside - metabolism ; Atractyloside - pharmacology ; bcl-2-Associated X Protein ; Binding Sites ; Biological and medical sciences ; Bongkrekic Acid - metabolism ; Bongkrekic Acid - pharmacology ; Brain ; Cell physiology ; Cellular biology ; Change Agents ; Coding ; Cyclosporine - pharmacology ; Dimerization ; Fundamental and applied biological sciences. Psychology ; HT29 Cells ; Humans ; Insect colonies ; Insect genetics ; Insect proteins ; Intracellular Membranes - physiology ; Liposomes ; Mice ; Mice, Inbred C57BL ; Mitochondria ; Mitochondria - physiology ; Mitochondrial ADP, ATP Translocases - chemistry ; Mitochondrial ADP, ATP Translocases - metabolism ; Mitochondrial membranes ; Molecular and cellular biology ; Molecules ; P branes ; Permeability ; Proteins ; Proto-Oncogene Proteins - chemistry ; Proto-Oncogene Proteins - genetics ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins - pharmacology ; Proto-Oncogene Proteins c-bcl-2 - pharmacology ; Rats ; Rats, Wistar ; Recombinant Proteins - pharmacology ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - genetics ; Transfection ; Yeast ; Yeasts</subject><ispartof>Science (American Association for the Advancement of Science), 1998-09, Vol.281 (5385), p.2027-2031</ispartof><rights>Copyright 1998 American Association for the Advancement of Science</rights><rights>1998 INIST-CNRS</rights><rights>Copyright American Association for the Advancement of Science Sep 25, 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c541t-a7343d96a75f2fe54197434f03261c5202f264d4e41fff683509fd717ad3968d3</citedby><cites>FETCH-LOGICAL-c541t-a7343d96a75f2fe54197434f03261c5202f264d4e41fff683509fd717ad3968d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2895738$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2895738$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>315,782,786,805,2886,2887,27931,27932,58024,58257</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2418070$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9748162$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marzo, Isabel</creatorcontrib><creatorcontrib>Brenner, Catherine</creatorcontrib><creatorcontrib>Zamzami, Naoufal</creatorcontrib><creatorcontrib>Jürgensmeier, Juliane M.</creatorcontrib><creatorcontrib>Susin, Santos A.</creatorcontrib><creatorcontrib>Helena L. A. Vieira</creatorcontrib><creatorcontrib>Prévost, Marie-Christine</creatorcontrib><creatorcontrib>Xie, Zhihua</creatorcontrib><creatorcontrib>Matsuyama, Shigemi</creatorcontrib><creatorcontrib>Reed, John C.</creatorcontrib><creatorcontrib>Kroemer, Guido</creatorcontrib><title>Bax and Adenine Nucleotide Translocator Cooperate in the Mitochondrial Control of Apoptosis</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>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.</description><subject>Ageing, cell death</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Atractyloside - metabolism</subject><subject>Atractyloside - pharmacology</subject><subject>bcl-2-Associated X Protein</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Bongkrekic Acid - metabolism</subject><subject>Bongkrekic Acid - pharmacology</subject><subject>Brain</subject><subject>Cell physiology</subject><subject>Cellular biology</subject><subject>Change Agents</subject><subject>Coding</subject><subject>Cyclosporine - pharmacology</subject><subject>Dimerization</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>HT29 Cells</topic><topic>Humans</topic><topic>Insect colonies</topic><topic>Insect genetics</topic><topic>Insect proteins</topic><topic>Intracellular Membranes - physiology</topic><topic>Liposomes</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mitochondria</topic><topic>Mitochondria - physiology</topic><topic>Mitochondrial ADP, ATP Translocases - chemistry</topic><topic>Mitochondrial ADP, ATP Translocases - metabolism</topic><topic>Mitochondrial membranes</topic><topic>Molecular and cellular biology</topic><topic>Molecules</topic><topic>P branes</topic><topic>Permeability</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins - chemistry</topic><topic>Proto-Oncogene Proteins - genetics</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Proto-Oncogene Proteins - pharmacology</topic><topic>Proto-Oncogene Proteins c-bcl-2 - pharmacology</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Transfection</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marzo, Isabel</creatorcontrib><creatorcontrib>Brenner, Catherine</creatorcontrib><creatorcontrib>Zamzami, Naoufal</creatorcontrib><creatorcontrib>Jürgensmeier, Juliane M.</creatorcontrib><creatorcontrib>Susin, Santos A.</creatorcontrib><creatorcontrib>Helena L. 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A. Vieira</au><au>Prévost, Marie-Christine</au><au>Xie, Zhihua</au><au>Matsuyama, Shigemi</au><au>Reed, John C.</au><au>Kroemer, Guido</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bax and Adenine Nucleotide Translocator Cooperate in the Mitochondrial Control of Apoptosis</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1998-09-25</date><risdate>1998</risdate><volume>281</volume><issue>5385</issue><spage>2027</spage><epage>2031</epage><pages>2027-2031</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><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.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>9748162</pmid><doi>10.1126/science.281.5385.2027</doi><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1998-09, Vol.281 (5385), p.2027-2031 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743649156 |
| source | MEDLINE; Science Magazine; JSTOR Archive Collection A-Z Listing |
| subjects | Ageing, cell death Animals Apoptosis Atractyloside - metabolism Atractyloside - pharmacology bcl-2-Associated X Protein Binding Sites Biological and medical sciences Bongkrekic Acid - metabolism Bongkrekic Acid - pharmacology Brain Cell physiology Cellular biology Change Agents Coding Cyclosporine - pharmacology Dimerization Fundamental and applied biological sciences. Psychology HT29 Cells Humans Insect colonies Insect genetics Insect proteins Intracellular Membranes - physiology Liposomes Mice Mice, Inbred C57BL Mitochondria Mitochondria - physiology Mitochondrial ADP, ATP Translocases - chemistry Mitochondrial ADP, ATP Translocases - metabolism Mitochondrial membranes Molecular and cellular biology Molecules P branes Permeability Proteins Proto-Oncogene Proteins - chemistry Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins - pharmacology Proto-Oncogene Proteins c-bcl-2 - pharmacology Rats Rats, Wistar Recombinant Proteins - pharmacology Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - genetics Transfection Yeast Yeasts |
| title | Bax and Adenine Nucleotide Translocator Cooperate in the Mitochondrial Control of Apoptosis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-04T10%3A19%3A57IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Bax%20and%20Adenine%20Nucleotide%20Translocator%20Cooperate%20in%20the%20Mitochondrial%20Control%20of%20Apoptosis&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Marzo,%20Isabel&rft.date=1998-09-25&rft.volume=281&rft.issue=5385&rft.spage=2027&rft.epage=2031&rft.pages=2027-2031&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.281.5385.2027&rft_dat=%3Cjstor_proqu%3E2895738%3C/jstor_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213569853&rft_id=info:pmid/9748162&rft_jstor_id=2895738&rfr_iscdi=true |