A Lethal Channel between the ATP Synthase Monomers.

Salvatore Nesci

Journal: Trends in biochemical sciences 2018;43(5):311-313

PMID: 29555114

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Abstract

The molecular structure of the transmembrane domain of ATP synthases is responsible for the inner mitochondrial membrane bending. According to the hypothesized mechanism, ATP synthase dissociation from dimers to monomers, triggered by Ca binding to F, allows the mitochondrial permeability transition pore formation at the interface between the detached monomers.

Address: Department of Veterinary Medical Sciences, University of Bologna, Via Tolara di Sopra 50, 40064 Ozzano Emilia (BO), Italy. Electronic address: [email protected].

DOI: 10.1016/j.tibs.2018.02.013

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MeSH Terms: Calcium, Humans, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Mitochondrial Permeability Transition Pore, Mitochondrial Proton-Translocating ATPases, Models, Molecular