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Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis

Jiang, Xian ; Jiang, Hui ; Shen, Zhirong ; Wang, Xiaodong

Proceedings of the National Academy of Sciences of the United States of America, 14 October 2014, Vol.111(41), pp.14782-7 [Tạp chí có phản biện]

E-ISSN: 1091-6490 ; PMID: 25275009 Version:1 ; DOI: 10.1073/pnas.1417253111

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  • Nhan đề:
    Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis
  • Tác giả: Jiang, Xian ; Jiang, Hui ; Shen, Zhirong ; Wang, Xiaodong
  • Chủ đề: Smac ; Caspase ; Membrane Potential ; Permeability ; Apoptosis ; Cytochromes C -- Metabolism ; Metalloendopeptidases -- Metabolism ; Mitochondria -- Enzymology ; Bcl-2 Homologous Antagonist-Killer Protein -- Metabolism ; Bcl-2-Associated X Protein -- Metabolism
  • Là 1 phần của: Proceedings of the National Academy of Sciences of the United States of America, 14 October 2014, Vol.111(41), pp.14782-7
  • Mô tả: Intrinsic apoptotic stimuli initiate mammalian cells' apoptotic program by first activating the proteins that have only Bcl-2 homology domain 3 (BH3), such as Bcl-2 interacting mediator of cell death (Bim) and truncated BH3 interacting death domain agonist (tBid), which in turn trigger conformational changes in BCL2-associated X (Bax) and BCL2-antagonist/killer (Bak) proteins that enable oligomer formation on the mitochondria, causing cytochrome c and other apoptogenic proteins in the intermembrane space to leak out. Leaked cytochrome c then initiates apoptotic caspase activation through a well-defined biochemical pathway. However, how oligomerized Bax and Bak cause cytochrome c release from mitochondria remains unknown. We report here the establishment of cell lines in which Bim or tBid can be inducibly expressed to initiate apoptosis in a controlled, quantitative manner. We used these cell lines to examine apoptotic events after Bax and Bak oligomerization but before cytochrome c release. The mitochondrial metalloprotease OMA1 was activated in this system in a Bax- and Bak-dependent fashion. Activated OMA1 cleaved the dynamin-like GTPase, optical nerve atrophy 1, an event that is critical for remodeling of mitochondrial cristae. Knockdown or knockout of OMA1 in these cells attenuated cytochrome c release. Thus it is clear that oligomerized Bax and Bak trigger apoptosis by causing both the permeabilization of the mitochondrial outer membrane and activation OMA1.
  • Ngôn ngữ: English
  • Số nhận dạng: E-ISSN: 1091-6490 ; PMID: 25275009 Version:1 ; DOI: 10.1073/pnas.1417253111

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