Novel insights into the mitochondrial permeability transition

Massimo Bonora, José Manuel Bravo-San Pedro, Guido Kroemer, Lorenzo Galluzzi, Paolo Pinton

    Research output: Contribution to journalReview articlepeer-review

    21 Citations (Scopus)

    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.

    Original languageEnglish
    Pages (from-to)2666-2670
    Number of pages5
    JournalCell Cycle
    Volume13
    Issue number17
    DOIs
    Publication statusPublished - 1 Sept 2014

    Keywords

    • Apoptosis
    • BCL-X
    • Cyclophilin D
    • Cyclosporin A
    • Necrosis
    • Permeability transition pore complex

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