Toward the molecular structure of the mitochondrial channel, VDAC

Carmen A. Mannella, Michael Forte, Marco Colombini

Research output: Contribution to journalArticle

119 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)7-19
Number of pages13
JournalJournal of Bioenergetics and Biomembranes
Volume24
Issue number1
DOIs
StatePublished - Feb 1992

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Structural Models
Molecular Structure
Electron Microscopy
Protein Domains

Keywords

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

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

Toward the molecular structure of the mitochondrial channel, VDAC. / Mannella, Carmen A.; Forte, Michael; Colombini, Marco.

In: Journal of Bioenergetics and Biomembranes, Vol. 24, No. 1, 02.1992, p. 7-19.

Research output: Contribution to journalArticle

Mannella, Carmen A. ; Forte, Michael ; Colombini, Marco. / Toward the molecular structure of the mitochondrial channel, VDAC. In: Journal of Bioenergetics and Biomembranes. 1992 ; Vol. 24, No. 1. pp. 7-19.
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