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

Carmen A. Mannella, Kathleen W. Kinnally

Research output: Contribution to journalArticle

Abstract

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
Volume40
Issue number3
DOIs
StatePublished - Jun 2008

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Detergents
Mitochondria
Membrane Proteins
Proteins
Membranes

Keywords

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

ASJC Scopus subject areas

  • Cell Biology
  • Physiology

Cite this

Reflections on VDAC as a voltage-gated channel and a mitochondrial regulator. / Mannella, Carmen A.; Kinnally, Kathleen W.

In: Journal of Bioenergetics and Biomembranes, Vol. 40, No. 3, 06.2008, p. 149-155.

Research output: Contribution to journalArticle

Mannella, Carmen A. ; Kinnally, Kathleen W. / Reflections on VDAC as a voltage-gated channel and a mitochondrial regulator. In: Journal of Bioenergetics and Biomembranes. 2008 ; Vol. 40, No. 3. pp. 149-155.
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