Ion Channels pp 169-202 | Cite as

VDAC, a Channel in the Outer Mitochondrial Membrane

  • Marco Colombini
  • Elizabeth Blachly-Dyson
  • Michael Forte
Chapter
Part of the Ion Channels book series (IC, volume 4)

Abstract

Proteins that form aqueous channels in membranes generate conduction pathways with a variety of shapes and sizes. Perhaps the largest channel-forming protein is the 2-MDa ryanodine receptor while the smallest may be gramicidin. However, the size of the conducting pathway is not correlated with the amount of protein mass needed to make up the structure, as demonstrated by the fact that some of the narrowest conducting pathways are produced by very large amounts of protein (e. g., 0.3 MDa for the Na+/ K+/Ca2+ channel family). In contrast, the focus of this review, the voltage-dependent anion channel (VDAC) of the mitochondrial outer membrane, produces one of the largest aqueous pathways from a single 30-kDa protein. VDAC also demonstrates that functional complexity does not seem to correlate well with the amount of protein used to form a channel. VDAC has a small amount of protein mass but displays complex behavior. It has two voltage-gating processes, can be controlled by metabolites and regulatory proteins, is able to form complexes with other proteins and enzymes, and responds to the protein concentration of the cytoplasm (Colombini, 1994). Thus, many functions are packed into a single, relatively small VDAC protein.

Keywords

Closed State Voltage Dependence Mitochondrial Outer Membrane Voltage Sensor Channel Closure 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Science+Business Media New York 1996

Authors and Affiliations

  • Marco Colombini
    • 1
  • Elizabeth Blachly-Dyson
    • 2
  • Michael Forte
    • 2
  1. 1.Department of ZoologyUniversity of MarylandCollege ParkUSA
  2. 2.Vollum InstituteOregon Health Sciences UniversityPortlandUSA

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