The interplay between BCL-2 family proteins and mitochondrial morphology in the regulation of apoptosis.

Apoptosis is a highly regulated process where key players such as BCL-2 family members control the recruitment of the mitochondrial subroutine. This culminates in the release of cytochrome c from the organelle in the cytoplasm, where it is required for the activation of effector caspases. The complete release of cytochrome c is the result of the combined action of proapoptotic BCL-2 family members and of changes in the complex morphology and ultrastructure of the organelle, controlled by the balance between fusion and fission processes. Here we discuss recent findings pointing to a role for changes in mitochondrial morphology during apoptosis and how these might be regulated by members of the BCL-2 family.