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

被引：42

作者：

Carraro, Michela ^{[1
]}

Checchetto, Vanessa ^{[2
]}

Szabo, Ildiko ^{[2
]}

Bernardi, Paolo ^{[1
]}

机构：

[1] Univ Padua, Dept Biomed Sci, Via Ugo Bassi 58-B, I-35131 Padua, Italy

[2] Univ Padua, Dept Biol, Padua, Italy

来源：

FEBS LETTERS | 2019年 / 593卷 / 13期

关键词：

ATP synthase; calcium; channel; cyclophilin; mitochondria; permeability transition; INNER MITOCHONDRIAL-MEMBRANE; COMPRISE VDAC MOLECULES; DEPENDENT ANION CHANNEL; CYCLOSPORINE-A; CYCLOPHILIN-D; SUBUNIT-C; BENZODIAZEPINE-RECEPTOR; PHOSPHATE CARRIER; OXIDATIVE-PHOSPHORYLATION; CA-2+-DEPENDENT PORE;

D O I：

10.1002/1873-3468.13485

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 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.

引用

页码：1542 / 1553

页数：12

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