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FEBS J. 2017 Mar;284(5):711-724. doi: 10.1111/febs.14008. Epub 2017 Feb 1.

The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID.

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Institute of Pharmacology, University of Bern, Switzerland.
Interfaculty Institute of Biochemistry, University of Tübingen, Germany.


The BCL-2 family members are key regulators of the intrinsic apoptotic pathway, which is defined by permeabilization of the mitochondrial outer membrane by members of the BAX-like subfamily. BOK is classified as a BAX-like protein; however, its (patho-)physiological role remains largely unclear. We therefore assessed the membrane permeabilization potential of C-terminally truncated recombinant BOK, BOK∆C . We show that BOK∆C can permeabilize liposomes mimicking the composition of mitochondrial outer membrane, but not of endoplasmic reticulum, forming large and stable pores over time. Importantly, pore formation was enhanced by the presence of cBID and refractory to the addition of antiapoptotic BCL-XL . However, isolated mitochondria from Bax-/- Bak-/- cells were resistant to BOK-induced cytochrome c release, even in the presence of cBID. Taken together, we show that BOK∆C can permeabilize liposomes, and cooperate with cBID, but its role in directly mediating mitochondrial permeabilization is unclear and may underlie a yet to be determined negative regulation.


BOK ; apoptosis; liposome; mitochondria; pore

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