Bonora Massimo, Bravo-San Pedro José Manuel, Kroemer Guido, Galluzzi Lorenzo, Pinton Paolo
a Section of Pathology , Oncology and Experimental Biology ; Laboratory for Technologies of Advanced Therapies (LTTA); Department of Morphology , Surgery and Experimental Medicine ; University of Ferrara ; Ferrara , Italy.
Cell Cycle. 2014;13(17):2666-70. doi: 10.4161/15384101.2014.949082.
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.
阿拉维安及其同事最近提供了进一步的证据，支持线粒体F1FO ATP合酶的c亚基构成了长期以来寻找的负责所谓“线粒体通透性转换”（MPT）的超分子复合物的成孔单元这一观点。这些发现除了为MPT背后的分子机制提供了新的线索外，还证实了包括细胞色素c和F1FO ATP合酶在内的细胞死亡机制的几个组成部分介导关键代谢活动的观点。
