| Literature DB >> 25486353 |
Massimo Bonora1, José Manuel Bravo-San Pedro, Guido Kroemer, Lorenzo Galluzzi, Paolo Pinton.
Abstract
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.Entities:
Keywords: AIFM1, apoptosis-inducing factor mitochondrion-associated, 1; ATP5G, ATP synthase, H+ transporting, mitochondrial FO complex, subunit C; BCL-XL; CYPD cyclophilin D; CYTC holocytochrome c; CsA, cyclosporin A; IMM, inner mitochondrial membrane; MCU, mitochondrial calcium uniporter; MPT, mitochondrial permeability transition; PPIF, peptidylprolyl isomerase F; PTPC, permeability transition pore complex; RCD, regulated cell death; SMV, submitochondrial vesicle.; apoptosis; cyclophilin D; cyclosporin A; necrosis; permeability transition pore complex; Δψm; mitochondrial transmembrane potential
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Year: 2014 PMID： 25486353 PMCID： PMC4612113 DOI： 10.4161/15384101.2014.949082
Source DB: PubMed Journal: Cell Cycle ISSN： 1551-4005 Impact factor: 4.534