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Journal of Bioenergetics and Biomembranes

, Volume 24, Issue 1, pp 7–19 | Cite as

Toward the molecular structure of the mitochondrial channel, VDAC

  • Carmen A. Mannella
  • Michael Forte
  • Marco Colombini
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Abstract

A summary is presented of the most recent information about the structure and mechanism of closure of the mitochondrial channel, VDAC. Considerable information has come from studies involving electron microscopy of two-dimensional crystals and from electrophysiological studies of wild-type channels and site-directed mutants. Available evidence points to a β-barrel as the basic structural model for VDAC. Two models for voltage- or effector- induced closure have been proposed, the first involving removal of strands from the wall of the pore, the second invoking movement of protein domains into the lumen. Experimental strategies to resolve the actual mechanism are presented.

Key words

Mitochondrial outer membrane VDAC membrane channel voltage gating electron microscopy membrane crystals site-directed mutagenesis 

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Copyright information

© Plenum Publishing Corporation 1992

Authors and Affiliations

  • Carmen A. Mannella
    • 1
    • 2
  • Michael Forte
    • 3
  • Marco Colombini
    • 4
  1. 1.Wadsworth Center for Laboratories and ResearchNew York State Department of HealthAlbany
  2. 2.Department of Biomedical Sciences, School of Public HealthState University of New York at AlbanyAlbany
  3. 3.Vollum Institute for Advanced Biomedical ResearchOregon Health Sciences UniversityPortland
  4. 4.Laboratories of Cell Biology, Department of ZoologyUniversity of MarylandCollege Park

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