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F‐ATP synthase and the permeability transition pore: fewer doubts, more certainties

Whether the mitochondrial permeability transition pore (PTP), also called mitochondrial megachannel (MMC), originates from the F‐ATP synthase is a matter of controversy. This hypothesis is supported both by site‐directed mutagenesis of specific residues of F‐ATP synthase affecting regulation of the...

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Published in:	FEBS letters 2019-07, Vol.593 (13), p.1542-1553
Main Authors:	Carraro, Michela, Checchetto, Vanessa, Szabó, Ildikó, Bernardi, Paolo
Format:	Article
Language:	English
Subjects:	Animals ATP synthase calcium channel cyclophilin Humans mitochondria Mitochondria - metabolism Mitochondrial Membrane Transport Proteins - metabolism Mitochondrial Proton-Translocating ATPases - chemistry Mitochondrial Proton-Translocating ATPases - genetics Mitochondrial Proton-Translocating ATPases - metabolism permeability transition Protein Engineering
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creator	Carraro, Michela Checchetto, Vanessa Szabó, Ildikó Bernardi, Paolo
description	Whether the mitochondrial permeability transition pore (PTP), also called mitochondrial megachannel (MMC), originates from the F‐ATP synthase is a matter of controversy. This hypothesis is supported both by site‐directed mutagenesis of specific residues of F‐ATP synthase affecting regulation of the PTP/MMC and by deletion of specific subunits causing dramatic changes in channel conductance. In contrast, human cells lacking an assembled F‐ATP synthase apparently display persistence of the PTP. We discuss recent data that shed new light on this controversy, supporting the conclusion that the PTP/MMC originates from a Ca2+‐dependent conformational change in F‐ATP synthase allowing its reversible transformation into a high‐conductance channel.
doi_str_mv	10.1002/1873-3468.13485
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subjects	Animals ATP synthase calcium channel cyclophilin Humans mitochondria Mitochondria - metabolism Mitochondrial Membrane Transport Proteins - metabolism Mitochondrial Proton-Translocating ATPases - chemistry Mitochondrial Proton-Translocating ATPases - genetics Mitochondrial Proton-Translocating ATPases - metabolism permeability transition Protein Engineering
title	F‐ATP synthase and the permeability transition pore: fewer doubts, more certainties
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