Mitochondrial permeability transition involves dissociation of F₁F_O ATP synthase dimers and C-ring conformation.

ABSTRACT: The impact of the mitochondrial permeability transition (MPT) on cellular physiology is well characterized. In contrast, the composition and mode of action of the permeability transition pore complex (PTPC), the supramolecular entity that initiates MPT, remain to be elucidated. Specifically, the precise contribution of the mitochondrial F₁F_O ATP synthase (or subunits thereof) to MPT is a matter of debate. We demonstrate that F₁F_O ATP synthase dimers dissociate as the PTPC opens upon MPT induction. Stabilizing F₁F_O ATP synthase dimers by genetic approaches inhibits PTPC opening and MPT Specific mutations in the F₁F_O ATP synthase c subunit that alter C-ring conformation sensitize cells to MPT induction, w

SUBMITTER: Bonora M 

PROVIDER: S-EPMC5494524 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature