Reflections on VDAC as a voltage-gated channel and a mitochondrial regulator

Carmen A. Mannella, Kathleen W. Kinnally

    Research output: Contribution to journalArticlepeer-review


    There is excellent agreement between the electrophysiological properties and the structure of the mitochondrial outer membrane protein, VDAC, ex vivo. However, the inference that the well-defined canonical "open" state of the VDAC pore is the normal physiological state of the channel in vivo is being challenged by several lines of evidence. Knowing the atomic structure of the detergent solubilized protein, a long sought after goal, will not be sufficient to understand the functioning of this channel protein. In addition, detailed information about VDAC's topology in the outer membrane of intact mitochondria, and the structural changes that it undergoes in response to different stimuli in the cell will be needed to define its physiological functions and regulation.

    Original languageEnglish (US)
    Pages (from-to)149-155
    Number of pages7
    JournalJournal of Bioenergetics and Biomembranes
    Issue number3
    StatePublished - Jun 2008


    • Channel
    • Mitochondria
    • Mitochondrial porin
    • Patch clamp
    • Planar bilayer
    • VDAC

    ASJC Scopus subject areas

    • Physiology
    • Cell Biology


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