Bax targets mitochondria by distinct mechanisms before or during apoptotic cell death: a requirement for VDAC2 or Bak for efficient Bax apoptotic function
Identifieur interne : 003B79 ( Main/Exploration ); précédent : 003B78; suivant : 003B80Bax targets mitochondria by distinct mechanisms before or during apoptotic cell death: a requirement for VDAC2 or Bak for efficient Bax apoptotic function
Auteurs : S B Ma [Australie] ; T N Nguyen [Australie] ; I. Tan [Australie] ; R. Ninnis [Australie] ; S. Iyer [Australie] ; D A Stroud [Australie] ; M. Menard [Australie, France] ; R M Kluck [Australie] ; M T Ryan [Australie] ; G. Dewson [Australie]Source :
- Cell Death and Differentiation [ 1350-9047 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- Animals, Apoptosis, Cells, Cultured, Mice, 129 Strain, Mice, Inbred C57BL, Mice, Knockout, Mitochondria (metabolism), Protein Multimerization, Protein Transport, Voltage-Dependent Anion Channel 2 (metabolism), bcl-2 Homologous Antagonist-Killer Protein (metabolism), bcl-2-Associated X Protein (physiology).
- MESH :
- chemical , metabolism : Voltage-Dependent Anion Channel 2, bcl-2 Homologous Antagonist-Killer Protein.
- metabolism : Mitochondria.
- chemical , physiology : bcl-2-Associated X Protein.
- Animals, Apoptosis, Cells, Cultured, Mice, 129 Strain, Mice, Inbred C57BL, Mice, Knockout, Protein Multimerization, Protein Transport.
Abstract
In non-apoptotic cells, Bak constitutively resides in the mitochondrial outer membrane. In contrast, Bax is in a dynamic equilibrium between the cytosol and mitochondria, and is commonly predominant in the cytosol. In response to an apoptotic stimulus, Bax and Bak change conformation, leading to Bax accumulation at mitochondria and Bak/Bax oligomerization to form a pore in the mitochondrial outer membrane that is responsible for cell death. Using blue native-PAGE to investigate how Bax oligomerizes in the mitochondrial outer membrane, we observed that, like Bak, a proportion of Bax that constitutively resides at mitochondria associates with voltage-dependent anion channel (VDAC)2 prior to an apoptotic stimulus. During apoptosis, Bax dissociates from VDAC2 and homo-oligomerizes to form high molecular weight oligomers. In cells that lack VDAC2, constitutive mitochondrial localization of Bax and Bak was impaired, suggesting that VDAC2 has a role in Bax and Bak import to, or stability at, the mitochondrial outer membrane. However, following an apoptotic stimulus, Bak and Bax retained the ability to accumulate at VDAC2-deficient mitochondria and to mediate cell death. Silencing of Bak in VDAC2-deficient cells indicated that Bax required either VDAC2 or Bak in order to translocate to and oligomerize at the mitochondrial outer membrane to efficiently mediate apoptosis. In contrast, efficient Bak homo-oligomerization at the mitochondrial outer membrane and its pro-apoptotic function required neither VDAC2 nor Bax. Even a C-terminal mutant of Bax (S184L) that localizes to mitochondria did not constitutively target mitochondria deficient in VDAC2, but was recruited to mitochondria following an apoptotic stimulus dependent on Bak or upon over-expression of Bcl-xL. Together, our data suggest that Bax localizes to the mitochondrial outer membrane
Url:
DOI: 10.1038/cdd.2014.119
PubMed: 25146925
PubMed Central: 4227151
Affiliations:
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Tan</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Walter and Eliza Hall Institute of Medical Research, 1 G Royal Parade, Parkville</institution>, Melbourne, Victoria,<country>Australia</country></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Ninnis, R" sort="Ninnis, R" uniqKey="Ninnis R" first="R" last="Ninnis">R. Ninnis</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Walter and Eliza Hall Institute of Medical Research, 1 G Royal Parade, Parkville</institution>, Melbourne, Victoria,<country>Australia</country></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation><nlm:aff id="aff3"><institution>Department of Medical Biology, University of Melbourne</institution>, Parkville,<country>Victoria</country></nlm:aff><wicri:noCountry code="nlm country">Victoria</wicri:noCountry></affiliation></author><author><name sortKey="Iyer, S" sort="Iyer, S" uniqKey="Iyer S" first="S" last="Iyer">S. Iyer</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Walter and Eliza Hall Institute of Medical Research, 1 G Royal Parade, Parkville</institution>, Melbourne, Victoria,<country>Australia</country></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation><nlm:aff id="aff3"><institution>Department of Medical Biology, University of Melbourne</institution>, Parkville,<country>Victoria</country></nlm:aff><wicri:noCountry code="nlm country">Victoria</wicri:noCountry></affiliation></author><author><name sortKey="Stroud, D A" sort="Stroud, D A" uniqKey="Stroud D" first="D A" last="Stroud">D A Stroud</name><affiliation wicri:level="1"><nlm:aff id="aff2"><institution>Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University</institution>, Melbourne,<country>Australia</country></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Menard, M" sort="Menard, M" uniqKey="Menard M" first="M" last="Menard">M. Menard</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Walter and Eliza Hall Institute of Medical Research, 1 G Royal Parade, Parkville</institution>, Melbourne, Victoria,<country>Australia</country></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="aff4"><institution>Centre de Cancérologie de Lyon, Université de Lyon</institution>, Lyon,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Kluck, R M" sort="Kluck, R M" uniqKey="Kluck R" first="R M" last="Kluck">R M Kluck</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Walter and Eliza Hall Institute of Medical Research, 1 G Royal Parade, Parkville</institution>, Melbourne, Victoria,<country>Australia</country></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation><nlm:aff id="aff3"><institution>Department of Medical Biology, University of Melbourne</institution>, Parkville,<country>Victoria</country></nlm:aff><wicri:noCountry code="nlm country">Victoria</wicri:noCountry></affiliation></author><author><name sortKey="Ryan, M T" sort="Ryan, M T" uniqKey="Ryan M" first="M T" last="Ryan">M T Ryan</name><affiliation wicri:level="1"><nlm:aff id="aff2"><institution>Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University</institution>, Melbourne,<country>Australia</country></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Dewson, G" sort="Dewson, G" uniqKey="Dewson G" first="G" last="Dewson">G. Dewson</name><affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Walter and Eliza Hall Institute of Medical Research, 1 G Royal Parade, Parkville</institution>, Melbourne, Victoria,<country>Australia</country></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation><nlm:aff id="aff3"><institution>Department of Medical Biology, University of Melbourne</institution>, Parkville,<country>Victoria</country></nlm:aff><wicri:noCountry code="nlm country">Victoria</wicri:noCountry></affiliation></author></analytic><series><title level="j">Cell Death and Differentiation</title><idno type="ISSN">1350-9047</idno><idno type="eISSN">1476-5403</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Apoptosis</term><term>Cells, Cultured</term><term>Mice, 129 Strain</term><term>Mice, Inbred C57BL</term><term>Mice, Knockout</term><term>Mitochondria (metabolism)</term><term>Protein Multimerization</term><term>Protein Transport</term><term>Voltage-Dependent Anion Channel 2 (metabolism)</term><term>bcl-2 Homologous Antagonist-Killer Protein (metabolism)</term><term>bcl-2-Associated X Protein (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Apoptose</term><term>Canal anionique-2 voltage-dépendant (métabolisme)</term><term>Cellules cultivées</term><term>Mitochondries (métabolisme)</term><term>Multimérisation de protéines</term><term>Protéine Bak (métabolisme)</term><term>Protéine Bax (physiologie)</term><term>Souris de lignée C57BL</term><term>Souris de souche-129</term><term>Souris knockout</term><term>Transport de protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Voltage-Dependent Anion Channel 2</term><term>bcl-2 Homologous Antagonist-Killer Protein</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Canal anionique-2 voltage-dépendant</term><term>Mitochondries</term><term>Protéine Bak</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéine Bax</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>bcl-2-Associated X Protein</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Apoptosis</term><term>Cells, Cultured</term><term>Mice, 129 Strain</term><term>Mice, Inbred C57BL</term><term>Mice, Knockout</term><term>Protein Multimerization</term><term>Protein Transport</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Apoptose</term><term>Cellules cultivées</term><term>Multimérisation de protéines</term><term>Souris de lignée C57BL</term><term>Souris de souche-129</term><term>Souris knockout</term><term>Transport de protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>In non-apoptotic cells, Bak constitutively resides in the mitochondrial outer membrane. In contrast, Bax is in a dynamic equilibrium between the cytosol and mitochondria, and is commonly predominant in the cytosol. In response to an apoptotic stimulus, Bax and Bak change conformation, leading to Bax accumulation at mitochondria and Bak/Bax oligomerization to form a pore in the mitochondrial outer membrane that is responsible for cell death. Using blue native-PAGE to investigate how Bax oligomerizes in the mitochondrial outer membrane, we observed that, like Bak, a proportion of Bax that constitutively resides at mitochondria associates with voltage-dependent anion channel (VDAC)2 prior to an apoptotic stimulus. During apoptosis, Bax dissociates from VDAC2 and homo-oligomerizes to form high molecular weight oligomers. In cells that lack VDAC2, constitutive mitochondrial localization of Bax and Bak was impaired, suggesting that VDAC2 has a role in Bax and Bak import to, or stability at, the mitochondrial outer membrane. However, following an apoptotic stimulus, Bak and Bax retained the ability to accumulate at VDAC2-deficient mitochondria and to mediate cell death. Silencing of Bak in VDAC2-deficient cells indicated that Bax required either VDAC2 or Bak in order to translocate to and oligomerize at the mitochondrial outer membrane to efficiently mediate apoptosis. In contrast, efficient Bak homo-oligomerization at the mitochondrial outer membrane and its pro-apoptotic function required neither VDAC2 nor Bax. Even a C-terminal mutant of Bax (S184L) that localizes to mitochondria did not constitutively target mitochondria deficient in VDAC2, but was recruited to mitochondria following an apoptotic stimulus dependent on Bak or upon over-expression of Bcl-x<sub>L</sub>. Together, our data suggest that Bax localizes to the mitochondrial outer membrane <italic>via</italic> alternate mechanisms, either constitutively <italic>via</italic> an interaction with VDAC2 or after activation <italic>via</italic> interaction with Bcl-2 family proteins.</p></div></front></TEI><affiliations><list><country><li>Australie</li><li>France</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Ma, S B" sort="Ma, S B" uniqKey="Ma S" first="S B" last="Ma">S B Ma</name></noRegion><name sortKey="Dewson, G" sort="Dewson, G" uniqKey="Dewson G" first="G" last="Dewson">G. Dewson</name><name sortKey="Iyer, S" sort="Iyer, S" uniqKey="Iyer S" first="S" last="Iyer">S. Iyer</name><name sortKey="Kluck, R M" sort="Kluck, R M" uniqKey="Kluck R" first="R M" last="Kluck">R M Kluck</name><name sortKey="Menard, M" sort="Menard, M" uniqKey="Menard M" first="M" last="Menard">M. Menard</name><name sortKey="Nguyen, T N" sort="Nguyen, T N" uniqKey="Nguyen T" first="T N" last="Nguyen">T N Nguyen</name><name sortKey="Ninnis, R" sort="Ninnis, R" uniqKey="Ninnis R" first="R" last="Ninnis">R. Ninnis</name><name sortKey="Ryan, M T" sort="Ryan, M T" uniqKey="Ryan M" first="M T" last="Ryan">M T Ryan</name><name sortKey="Stroud, D A" sort="Stroud, D A" uniqKey="Stroud D" first="D A" last="Stroud">D A Stroud</name><name sortKey="Tan, I" sort="Tan, I" uniqKey="Tan I" first="I" last="Tan">I. Tan</name></country><country name="France"><noRegion><name sortKey="Menard, M" sort="Menard, M" uniqKey="Menard M" first="M" last="Menard">M. Menard</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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