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Prevention of apoptosis by the interaction between FIH1 and Bax

Biao Yan1, Men Kong, Yi-han Chen

  • 1Department of Biochemistry and Molecular Biology, College of Life Science and Technology, Tongji University, Shanghai, China. yanbiao1982@hotmail.com

Molecular and Cellular Biochemistry
|November 12, 2010
PubMed

Insights

Factor Inhibiting HIF-1 (FIH1) retains Bax in the cytosol, preventing its translocation to mitochondria. This interaction suppresses Bax-mediated apoptosis, revealing FIH1

Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Bax protein initiates mitochondrial-dependent apoptosis in mammalian cells.
  • The precise mechanisms regulating Bax inactivation remain incompletely understood.

Purpose of the Study:

  • To identify novel regulators of Bax-mediated apoptosis.
  • To elucidate the interaction between FIH1 and Bax.

Main Methods:

  • Mass spectrometry identified FIH1 as a potential Bax interactor.
  • Coimmunoprecipitation and GST pull-down assays confirmed direct FIH1-Bax interaction.

Main Results:

  • FIH1 overexpression suppressed Bax-mediated apoptosis.
  • FIH1 deficiency accelerated Bax-mediated apoptosis.
  • FIH1 acts as a cytosolic retention factor for Bax, inhibiting its mitochondrial translocation.

Conclusions:

  • FIH1 directly interacts with Bax and regulates its apoptotic function.
  • FIH1 plays a novel inhibitory role in Bax-mediated apoptosis by retaining Bax in the cytosol.

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