Novel insights into the mitochondrial permeability transition

被引：19

作者：

Bonora, Massimo ^{[1
]}

Pedro, Jose Manuel Bravo-San ^{[2
,3
,4
]}

Kroemer, Guido ^{[2
,3
,5
,6
,7
]}

Galluzzi, Lorenzo ^{[2
,4
,5
]}

Pinton, Paolo ^{[1
]}

机构：

[1] Univ Ferrara, Dept Morphol Surg & Expt Med, Sect Pathol Oncol & Expt Biol, Lab Technol Adv Therapies LTTA, I-44100 Ferrara, Italy

[2] Ctr Rech Cordeliers, Equipe Labelisee Ligue Natl Canc 11, Paris, France

[3] INSERM, U1138, Paris, France

[4] Gustave Roussy Comprehens Canc Ctr, Villejuif, France

[5] Univ Paris 05, Sorbonne Paris Cite, Paris, France

[6] Gustave Roussy Comprehens Canc Ctr, Villejuif, France

[7] Hop Europeen Georges Pompidou, AP HP, Paris, France

来源：

CELL CYCLE | 2014年 / 13卷 / 17期

基金：

欧洲研究理事会;

关键词：

apoptosis; BCL-X-L; cyclophilin D; cyclosporin A; necrosis; permeability transition pore complex; ATP SYNTHASE; CYCLOPHILIN-D; CYTOCHROME-C; CELL-DEATH; APOPTOTIC FUNCTIONS; SUBUNIT C; PORE; PHOSPHORYLATION; TRANSLOCATOR; MEMBRANE;

D O I：

10.4161/15384101.2014.949082

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Alavian and colleagues recently provided further evidence in support of the notion that the c subunit of the mitochondrial F1FO ATP synthase constitutes the long-sought pore-forming unit of the supramolecular complex responsible for the so-called 'mitochondrial permeability transition' (MPT). Besides shedding new light on the molecular mechanisms that underlie the MPT, these findings corroborate the notion that several components of the cell death machinery, including cytochrome c and the F1FO ATP synthase, mediate critical metabolic activities.

引用

收藏

页码：2666 / 2670

页数：5

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