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Related Experiment Videos

Mitochondrial membrane permeabilisation by Bax/Bak.

Mauro Degli Esposti1, Caroline Dive

  • 1Cancer Research UK Cellular and Molecular Pharmacology Group, School of Biological Sciences, University of Manchester, G38 Stopford Building, Oxford Road, Manchester M134 9PT, UK.

Biochemical and Biophysical Research Communications
|May 6, 2003
PubMed
Summary

The pro-apoptotic proteins Bax and Bak are essential for releasing cytochrome c from mitochondria. Their precise mechanisms for outer mitochondrial membrane permeabilization are still being investigated, with lipid interactions playing a key role.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Bax and Bak, key Bcl-2 family proteins, are required for releasing apoptogens like cytochrome c from mitochondria.
  • BH-3 only proteins, such as Bid, interact with Bcl-2 proteins to induce cell death.
  • The exact mechanism by which Bax and Bak permeabilize the outer mitochondrial membrane (OMM) remains unclear.

Purpose of the Study:

  • To evaluate current models of Bax and Bak function in OMM permeabilization.
  • To explore the potential differences in how Bax and Bak promote OMM permeabilization.
  • To consider the role of lipid-protein interactions in Bax and Bak activity.

Main Methods:

  • Analysis of studies on Bax/Bak-deficient mouse cells.
  • Review of existing models for Bax and Bak function.

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  • Consideration of emerging data on lipid-protein interactions.

    • Main Results:

    • Bax and Bak are necessary for cytochrome c release from mitochondria.
    • BH-3 only proteins mediate interactions at the mitochondrial surface.
    • The precise mechanisms of OMM permeabilization by Bax and Bak are not fully elucidated.
    • Emerging evidence suggests crucial roles for lipid-protein interactions.

    Conclusions:

    • Bax and Bak may function distinctly in promoting OMM permeabilization.
    • Further research is needed to clarify the roles of Bax, Bak, and lipid-protein interactions in apoptosis.