A Lethal Channel between the ATP Synthase Monomers

Salvatore Nesci

doi:10.1016/j.tibs.2018.02.013

A Lethal Channel between the ATP Synthase Monomers

Trends Biochem Sci. 2018 May;43(5):311-313. doi: 10.1016/j.tibs.2018.02.013. Epub 2018 Mar 16.

Author

Salvatore Nesci¹

Affiliation

¹ Department of Veterinary Medical Sciences, University of Bologna, Via Tolara di Sopra 50, 40064 Ozzano Emilia (BO), Italy. Electronic address: salvatore.nesci@unibo.it.

PMID: 29555114
DOI: 10.1016/j.tibs.2018.02.013

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 Ca²⁺ binding to F₁, allows the mitochondrial permeability transition pore formation at the interface between the detached monomers.

Keywords: ATP synthase; cristae; mitochondria; mitochondrial permeability transition pore.

Publication types

Review

MeSH terms

Calcium / metabolism*
Humans
Mitochondrial Membrane Transport Proteins / metabolism*
Mitochondrial Membranes / metabolism*
Mitochondrial Permeability Transition Pore
Mitochondrial Proton-Translocating ATPases / metabolism*
Models, Molecular

Substances

Mitochondrial Membrane Transport Proteins
Mitochondrial Permeability Transition Pore
Mitochondrial Proton-Translocating ATPases
Calcium