Abstract
Mitochondrial permeabilization is a key event in apoptosis, which defines the point of no return in the cell's commitment to death. BAX and BAK are proteins of the BCL-2 family that control this process to release cytochrome c and other apoptototic factors into the cytosol thus activating the caspase cascade and leading to cell death. Despite intense research, we still lack adequate understanding of the protein structures and their dynamic regulation that mediate mitochondrial membrane permeabilization in apoptosis. I will discuss our latest discoveries using advanced microscopy methods to provide a holistic view of the macromolecular assembly of the key effectors BAX and BAK that uncovers key aspects of the dynamic architecture of the apoptotic pore.
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