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
收藏
页码：1542 / 1553
页数：12
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