ATP合酶
ATP合成酶γ亚单位
线粒体
线粒体通透性转换孔
蛋白质亚单位
细胞生物学
质子泵
生物
线粒体内膜
化学
生物物理学
生物化学
ATP酶
酶
基因
程序性细胞死亡
ATP水解
细胞凋亡
作者
Andrea Carrer,Ludovica Tommasin,Justina Šileikytė,Francesco Ciscato,Riccardo Filadi,Andrea Urbani,Michael Forte,Andrea Rasola,Ildikò Szabó,Michela Carraro,Paolo Bernardi
标识
DOI:10.1038/s41467-021-25161-x
摘要
Abstract F-ATP synthase is a leading candidate as the mitochondrial permeability transition pore (PTP) but the mechanism(s) leading to channel formation remain undefined. Here, to shed light on the structural requirements for PTP formation, we test cells ablated for g, OSCP and b subunits, and ρ 0 cells lacking subunits a and A6L. Δg cells (that also lack subunit e) do not show PTP channel opening in intact cells or patch-clamped mitoplasts unless atractylate is added. Δb and ΔOSCP cells display currents insensitive to cyclosporin A but inhibited by bongkrekate, suggesting that the adenine nucleotide translocator (ANT) can contribute to channel formation in the absence of an assembled F-ATP synthase. Mitoplasts from ρ 0 mitochondria display PTP currents indistinguishable from their wild-type counterparts. In this work, we show that peripheral stalk subunits are essential to turn the F-ATP synthase into the PTP and that the ANT provides mitochondria with a distinct permeability pathway.
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