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There is something about BOK we just don't get yet.

Manuel D Haschka1, Andreas Villunger1,2

  • 1Division of Developmental Immunology, BIOCENTER, Medical University of Innsbruck, Innsbruck, Austria.

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The proapoptotic BCL-2 family member BOK forms pores in liposomes, enhanced by cBID but not BCL-XL. BOK binds mitochondria but cannot release cytochrome c, even with cBID.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The BCL-2 protein family regulates apoptosis.
  • BOK is a proapoptotic member of the BCL-2 family.
  • Pore formation by BCL-2 proteins is a key mechanism in apoptosis.

Purpose of the Study:

  • To investigate the pore-forming ability of BOK.
  • To determine the effects of cBID and BCL-XL on BOK-mediated pore formation.
  • To assess BOK's ability to induce mitochondrial outer membrane permeabilization.

Main Methods:

  • Liposome-based pore formation assays.
  • Mitochondrial binding studies.
  • Cytochrome c release assays.

Main Results:

  • BOK forms large, stable pores in artificial liposomes.
  • Pore formation is enhanced by the proapoptotic protein cBID.
  • The antiapoptotic protein BCL-XL does not affect BOK-mediated pore formation.
  • BOK binds to isolated mitochondria but does not induce cytochrome c release.

Conclusions:

  • BOK possesses intrinsic pore-forming capabilities.
  • BOK's function is modulated by other BCL-2 family members.
  • BOK-induced mitochondrial outer membrane permeabilization is inefficient, even with cBID assistance.