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Related Experiment Videos

Bid, but not Bax, regulates VDAC channels.

Tatiana K Rostovtseva1, Bruno Antonsson, Motoshi Suzuki

  • 1Laboratory of Physical and Structural Biology, NICHD, National Institutes of Health, Bethesda, Maryland 20892, USA. rostovts@helix.nih.gov

The Journal of Biological Chemistry
|January 20, 2004
PubMed
Summary

The pro-apoptotic protein Bax does not appear to trigger cytochrome c release by interacting with the voltage-dependent anion channel (VDAC). However, cleaved Bid protein does affect VDAC function, potentially disrupting mitochondrial metabolite exchange.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Biology

Background:

  • Cytochrome c release from mitochondria is a key event in apoptosis.
  • The voltage-dependent anion channel (VDAC) is implicated in mitochondrial outer membrane permeabilization.
  • Conflicting mechanisms exist regarding VDAC's role in cytochrome c release.

Purpose of the Study:

  • To investigate the interaction between the pro-apoptotic protein Bax and VDAC.
  • To determine if Bax mediates cytochrome c release through VDAC.
  • To examine the effect of other pro-apoptotic proteins, like Bid, on VDAC function.

Main Methods:

  • Reconstitution of mammalian VDAC channels into planar phospholipid membranes.
  • Electrophysiological recordings of VDAC channel properties.

Related Experiment Videos

  • Addition of monomeric and oligomeric Bax to reconstituted VDAC.
  • Treatment of reconstituted VDAC with caspase-8 cleaved Bid.

    • Main Results:

    • Bax, in monomeric or oligomeric forms, did not alter VDAC channel properties.
    • No electrophysiologically detectable interaction was observed between Bax and VDAC.
    • Caspace-8 cleaved Bid induced VDAC channel closure, affecting voltage gating.

    Conclusions:

    • Bax does not induce cytochrome c release by directly acting on VDAC.
    • Bid may contribute to mitochondrial dysfunction by altering VDAC gating and metabolite transport.
    • VDAC's role in apoptosis may be modulated by different pro-apoptotic proteins through distinct mechanisms.