Voltage-dependant anion channels: novel insights into isoform function through genetic models

Biochim Biophys Acta. 2012 Jun;1818(6):1477-85. doi: 10.1016/j.bbamem.2011.10.019. Epub 2011 Oct 25.


Voltage-dependant Anion Channels, also known as mitochondrial porins, are pore-forming proteins located in the mitochondrial outer membrane (MOM) that, in addition to forming complexes with other proteins that localize to the MOM, also function as the main conduit for transporting metabolites between the cytoplasm and mitochondria. VDACs are encoded by a multi-member gene family, and the number of isoforms and specific functions of VDACs varies between species. Translating the well-described in vitro characteristics of the VDAC isoforms into in vivo functions has been a challenge, with the generation of animal models of VDAC deficiency providing much of the available information about isoform-specific roles in biology. Here, we review the approaches used to create these insect and mammalian animal models, and the conclusions reached by studying the consequences of loss of function mutations on the genetic, physiologic, and biochemical properties of the resulting models. This article is part of a Special Issue entitled: VDAC structure, function, and regulation of mitochondrial metabolism.

Publication types

  • Review

MeSH terms

  • Animals
  • Embryonic Stem Cells / metabolism
  • Humans
  • Models, Genetic*
  • Protein Isoforms / chemistry
  • Protein Isoforms / metabolism
  • Voltage-Dependent Anion Channels / chemistry
  • Voltage-Dependent Anion Channels / deficiency
  • Voltage-Dependent Anion Channels / metabolism*


  • Protein Isoforms
  • Voltage-Dependent Anion Channels