Abstract
Permeabilization of the outer mitochondrial membrane initiates apoptotic cell death. B-cell lymphoma 2 (BCL-2) antagonist killer (BAK) and BCL-2-associated X (BAX) mediate mitochondrial poration, but how this process unfolds remains poorly defined. Two studies in this issue investigate thetransition of dormant, inactive BAK monomer to a highly dynamic membrane-associated, pore-forming oligomer.
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