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

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

Adithya Raghavan  1 , Tatiana Sheiko, Brett H Graham, William J Craigen
Affiliations
Review

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

Adithya Raghavan et al. Biochim Biophys Acta. 2012 Jun.

Abstract

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.

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Figures

Fig. 1
Fig. 1
Gene structures of human VDAC isoforms with their reported alternate spliced variants (not drawn to scale). Predicted putative exons are shown in dashed boxes. Alternate polyadenlyation sites are marked with arrows for hVDAC2. Translated regions are filled boxes, untranslated regions are not filled. The predicted start codons of the isoforms are shown, along with the ATG mini-exon for hVDAC3 (in italics). The vertical arrows represent the multiple polyadenylation sites found in the VDAC2 gene. See text for details.
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