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Review
. 2022 Oct;1869(10):119317.
doi: 10.1016/j.bbamcr.2022.119317. Epub 2022 Jun 22.

Pro-apoptotic complexes of BAX and BAK on the outer mitochondrial membrane

Philipp Wolf  1 , Axel Schoeniger  1 , Frank Edlich  2
Affiliations
Free article
Review

Pro-apoptotic complexes of BAX and BAK on the outer mitochondrial membrane

Philipp Wolf et al. Biochim Biophys Acta Mol Cell Res. 2022 Oct.
Free article

Abstract

In multicellular organisms the regulated cell death apoptosis is critically important for both ontogeny and homeostasis. Mitochondria are indispensable for stress-induced apoptosis. The BCL-2 protein family controls mitochondrial apoptosis and initiates cell death through the pro-apoptotic activities of BAX and BAK at the outer mitochondrial membrane (OMM). Cellular survival is ensured by the retrotranslocation of mitochondrial BAX and BAK into the cytosol by anti-apoptotic BCL-2 proteins. BAX/BAK-dependent OMM permeabilization releases the mitochondrial cytochrome c (cyt c), which initiates activation of caspase-9. The caspase cascade leads to cell shrinkage, plasma membrane blebbing, chromatin condensation, and apoptotic body formation. Although it is clear that ultimately complexes of active BAX and BAK commit the cell to apoptosis, the nature of these complexes is still enigmatic. Excessive research has described a range of complexes, varying from a few molecules to several 10,000, in different systems. BAX/BAK complexes potentially form ring-like structures that could expose the inner mitochondrial membrane. It has been suggested that these pores allow the efflux of small proteins and even mitochondrial DNA. Here we summarize the current state of knowledge for mitochondrial BAX/BAK complexes and the interactions between these proteins and the membrane.

Keywords: BCL-2 proteins; BH3 profiling; Cancer; Cell death; Immunotherapy.

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