Bax Forms an Oligomer via Separate, Yet Interdependent, Surfaces*

No abstract is available for this paper.

• Publication year

  2010

• Venue

  Journal of Biological Chemistry

• Publication date

  2010-04-09

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1074/jbc.M110.113456PMID 20382739PMCID PMC2878526
• 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.

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• To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions.

  2008cited by this paper
• Bcl-XL Inhibits Membrane Permeabilization by Competing with Bax

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• Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax.

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• Bcl‐2 changes conformation to inhibit Bax oligomerization

  2006cited by this paper
• Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies

  2006cited by this paper
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  2006cited by this paper
• Auto-activation of the Apoptosis Protein Bax Increases Mitochondrial Membrane Permeability and Is Inhibited by Bcl-2*

  2006cited by this paper
• Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.

  2005cited by this paper
• The multidomain proapoptotic molecules Bax and Bak are directly activated by heat.

  2005cited by this paper
• Distinct Domains Control the Addressing and the Insertion of Bax into Mitochondria*

  2005cited by this paper
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  2005cited by this paper
• The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA.

  2004cited by this paper
• Bcl-2 Homodimerization Involves Two Distinct Binding Surfaces, a Topographic Arrangement That Provides an Effective Mechanism for Bcl-2 to Capture Activated Bax*

  2004cited by this paper
• Conformational control of Bax localization and apoptotic activity by Pro168

  2004cited by this paper
• Interaction with a Membrane Surface Triggers a Reversible Conformational Change in Bax Normally Associated with Induction of Apoptosis*

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• BCL-2 Selectively Interacts with the BID-induced Open Conformer of BAK, Inhibiting BAK Auto-oligomerization*

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• VDAC2 Inhibits BAK Activation and Mitochondrial Apoptosis

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• The structure of a Bcl-xL/Bim fragment complex: implications for Bim function.

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• Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics.

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• Bax Is Present as a High Molecular Weight Oligomer/Complex in the Mitochondrial Membrane of Apoptotic Cells*

  2001cited by this paper
• Damage‐induced Bax N‐terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate

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• Membrane Topography and Topogenesis of Prenylated Rab Acceptor (PRA1)*

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  2000cited by this paper
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  1999cited by this paper
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  1993cited by this paper
• Removal of detergents from membrane proteins.

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