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dc.contributor.authorvon Ahsen, O
dc.contributor.authorRenken, C
dc.contributor.authorPerkins, G
dc.contributor.authorKluck, RM
dc.contributor.authorBossy-Wetzel, E
dc.contributor.authorNewmeyer, DD
dc.date.accessioned2020-12-21T03:11:03Z
dc.date.available2020-12-21T03:11:03Z
dc.date.issued2000-09-04
dc.identifier.citationvon Ahsen, O., Renken, C., Perkins, G., Kluck, R. M., Bossy-Wetzel, E. & Newmeyer, D. D. (2000). Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release. JOURNAL OF CELL BIOLOGY, 150 (5), pp.1027-1036. https://doi.org/10.1083/jcb.150.5.1027.
dc.identifier.issn0021-9525
dc.identifier.urihttp://hdl.handle.net/11343/257102
dc.description.abstractProapoptotic members of the Bcl-2 protein family, including Bid and Bax, can activate apoptosis by directly interacting with mitochondria to cause cytochrome c translocation from the intermembrane space into the cytoplasm, thereby triggering Apaf-1-mediated caspase activation. Under some circumstances, when caspase activation is blocked, cells can recover from cytochrome c translocation; this suggests that apoptotic mitochondria may not always suffer catastrophic damage arising from the process of cytochrome c release. We now show that recombinant Bid and Bax cause complete cytochrome c loss from isolated mitochondria in vitro, but preserve the ultrastructure and protein import function of mitochondria, which depend on inner membrane polarization. We also demonstrate that, if caspases are inhibited, mitochondrial protein import function is retained in UV-irradiated or staurosporine-treated cells, despite the complete translocation of cytochrome c. Thus, Bid and Bax act only on the outer membrane, and lesions in the inner membrane occurring during apoptosis are shown to be secondary caspase-dependent events.
dc.languageEnglish
dc.publisherROCKEFELLER UNIV PRESS
dc.titlePreservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release
dc.typeJournal Article
dc.identifier.doi10.1083/jcb.150.5.1027
melbourne.affiliation.departmentMedical Biology (W.E.H.I.)
melbourne.source.titleThe Journal of Cell Biology
melbourne.source.volume150
melbourne.source.issue5
melbourne.source.pages1027-1036
dc.rights.licenseCC BY-NC-SA
melbourne.elementsid1240426
melbourne.contributor.authorKluck, Ruth
dc.identifier.eissn1540-8140
melbourne.accessrightsOpen Access


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