Regulation of mitochondrial membrane permeabilization by BCL-2 family proteins and caspases.

No abstract is available for this paper.

• Publication year

  2004

• Venue

  Current Opinion in Cell Biology

• Publication date

  2004-12-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/J.CEB.2004.09.009PMID 15530776
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Cell death: critical control points.

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• During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria.

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• Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain.

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• VDAC2 Inhibits BAK Activation and Mitochondrial Apoptosis

  2003influential reference
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• Ku70 suppresses the apoptotic translocation of Bax to mitochondria

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• Cytochrome C-mediated apoptosis.

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• A JNK-dependent pathway is required for TNFalpha-induced apoptosis.

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• Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak‐mediated permeabilization

  2003influential reference
• ReviewMitochondria : Releasing Power for Life and Unleashing the Machineries of Death

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• Requirement for Caspase-2 in Stress-Induced Apoptosis Before Mitochondrial Permeabilization

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• Cytochrome c release from mitochondria proceeds by a two-step process

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• Caspase-2 Induces Apoptosis by Releasing Proapoptotic Proteins from Mitochondria*

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• Bax-mediated Ca2+ Mobilization Promotes Cytochromec Release during Apoptosis*

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• Caspase-2 Acts Upstream of Mitochondria to Promote Cytochromec Release during Etoposide-induced Apoptosis*

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• Mitochondrial endonuclease G is important for apoptosis in C. elegans

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  2001influential reference
• Apoptosis‐associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl‐2

  2001influential reference
• BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak.

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• Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death

  2001influential reference
• The pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites

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• Reduced Loading of Intracellular Ca2+ Stores and Downregulation of Capacitative Ca2+Influx in Bcl-2–Overexpressing Cells

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  2000cited by this paper
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  2000cited by this paper
• Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria.

  2000cited by this paper
• tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c.

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  1999cited by this paper
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  1999cited by this paper
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  1998cited by this paper
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  1998cited by this paper
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  1998cited by this paper
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