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Cited by 92Mitochondrial Function and PathologyIon channel regulation and functionATP Synthase and ATPases Research

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

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Raghavan, Adithya, Sheiko, Tatiana, Graham, Brett H., Craigen, William J.·2012·Biochimica et Biophysica Acta (BBA) - Biomembranes
DOI 10.1016/j.bbamem.2011.10.019PMC PMC4273737
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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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  • Mice null for Vdac1 and Vdac3 are viable and display little overt phenotypic changes, whereas on that murine genetic background Vdac2−/− mice were embryonically lethal.

    “Interestingly, mice null for Vdac1 and Vdac3 are viable and display little overt phenotypical changes; however, on this particular murine genetic background, Vdac2−/− mice were embryonically lethal (99, 100).”

    From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [99]

    Section 6.6 states that VDAC1- and VDAC3-deficient mice can survive, whereas global VDAC2 deletion causes early embryonic death. But §6.1 reports strain-dependent partial embryonic lethality and mild growth retardation in VDAC1-null mice, and infertility in VDAC3-null males. These findings do not support describing the mice as having little overt phenotypic change; the cited passages also do not establish that the VDAC2 result was obtained on the same genetic background. Page numbers were not provided in our copy. (LLM, conf=0.87)

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References 87 · Cited by 92

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Authors
Raghavan, A., Sheiko, T., Graham, B. H., & Craigen, W. J.
Affiliations
Baylor College of Medicine (US)
Corresponding author
Craigen, William J.
ORCID
Graham, Brett H.
Venue
Biochimica et Biophysica Acta (BBA) - Biomembranes
Publisher
Elsevier BV
Published
2012-06
Volume
1818
Issue
6
Pages
1477-1485
ISSN
0005-2736 (ISSN-L)
DOI
10.1016/j.bbamem.2011.10.019
PMC
PMC4273737
OpenAlex
W2083677673
Cited by
92
References
87
Citations by year
2026: 2 · 2025: 6 · 2024: 10 · 2023: 6 · 2022: 4 · 2021: 8 · 2020: 9 · 2019: 6 · 2018: 2 · 2017: 6 · 2016: 11 · 2015: 6 · 2014: 6 · 2013: 5 · 2012: 5
FWCI
0.47
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institute of General Medical Sciences (F32GM065041)
  • National Institute of Neurological Disorders and Stroke (R01NS042319)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (K08HD044808)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords
voltage-dependent anion channel, VDAC isoforms, mitochondrial outer membrane, loss-of-function mutations, mitochondrial metabolism, metabolite transport, insect models, mammalian models
MeSH terms
Animals, Humans, Models, Genetic, Protein Isoforms, Voltage-Dependent Anion Channels, Embryonic Stem Cells

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