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

FEBS Letters

article

Michela Carraro¹  Vanessa Checchetto²  Ildikó Szabó²  Paolo Bernardi¹ 

[1] Department of Biomedical Sciences, University of Padova;Department of Biology, University of Padova

关键词: ATP synthase;    calcium;    channel;    cyclophilin;    mitochondria;    permeability transition;   

DOI  :  10.1002/1873-3468.13485

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 FATP 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 FATP synthase allowing its reversible transformation into a high-conductance channel.

【 授权许可】

Unknown