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ATP 合酶复合物与线粒体通透性转换孔:吸引力的两极。

ATP synthase complex and the mitochondrial permeability transition pore: poles of attraction.

机构信息

Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary.

出版信息

EMBO Rep. 2017 Jul;18(7):1041-1042. doi: 10.15252/embr.201744412. Epub 2017 Jun 19.

Abstract

The identity of the mitochondrial permeability transition (mPT) pore, a megachannel embedded in the inner membrane opened by Ca, is fiercely debated. Unraveling the components structuring this pore is critical for combating diseases as diverse as neurodegeneration, cancer, autoimmunity, and myopathies in which this phenomenon is implicated. Current consensus is that the pore is formed within, or in‐between FF ATP synthase dimers, but not through their c‐subunit ring. Two recent studies in this issue of throw more light on these aspects, one by Giorgio 1 showing that the β subunit of the ATP synthase harbors a Ca‐binding site responsible for triggering mPT, and the other by Bonora 2 demonstrating that permeability transition requires dissociation of FF ATP synthase dimers, albeit in a manner involving the c‐subunit ring.

摘要

线粒体通透性转变(mPT)孔的身份是一个嵌入在内膜中的巨型通道,由 Ca 打开,这个问题一直存在激烈的争论。阐明构成这个孔的组件对于治疗各种疾病至关重要,这些疾病包括神经退行性疾病、癌症、自身免疫性疾病和肌病,这些疾病都与 mPT 现象有关。目前的共识是,该孔是在 FF ATP 合酶二聚体内部或之间形成的,但不是通过它们的 c 亚基环。本期的两项最新研究进一步阐明了这些方面,其中 Giorgio 1 的研究表明,ATP 合酶的 β 亚基具有一个 Ca 结合位点,负责触发 mPT,而 Bonora 2 的研究则表明,通透性转变需要 FF ATP 合酶二聚体的解离,尽管这种解离方式涉及 c 亚基环。

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