Molecular and topological reorganizations in mitochondrial architecture interplay during Bax-mediated steps of apoptosis.

ABSTRACT: During apoptosis, Bcl-2 proteins such as Bax and Bak mediate the release of pro-apoptotic proteins from the mitochondria by clustering on the outer mitochondrial membrane and thereby permeabilizing it. However, it remains unclear how outer membrane openings form. Here, we combined different correlative microscopy and electron cryo-tomography approaches to visualize the effects of Bax activity on mitochondria in human cells. Our data show that Bax clusters localize near outer membrane ruptures of highly variable size. Bax clusters contain structural elements suggesting a higher order organization of their components. Furthermore, unfolding of inner membrane cristae is coupled to changes in the supramolecular assembly of ATP synthases, particularly pronounced at membrane segments exposed to

SUBMITTER: Ader NR 

PROVIDER: S-EPMC6361589 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature