VDAC, the early days
Open accessAbstract
VDAC is now universally accepted as the channel in the mitochondrial outer membrane responsible for metabolite flux in and out of mitochondria. Its discovery occurred over two independent lines of investigation in the 1970s and 80s. This retrospective article describes the history of VDAC's discovery and how these lines merged in a collaboration by the authors. The article was written to give the reader a sense of the role played by laboratory environment, personalities, and serendipity in the discovery of the molecular basis for the unusual permeability properties of the mitochondrial outer membrane. This article is part of a Special Issue entitled: VDAC structure, function, and regulation of mitochondrial metabolism.
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VDAC is the most abundant protein of the mitochondrial outer membrane and is widely accepted as the principal route and control of metabolic flux between the cytosol and mitochondria.
“Voltage-dependent anion channel is the most abundant protein of the mitochondrial outer membrane and is widely accepted as the principal route and control of metabolic flux between the cytosol and mitochondria (95).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [95]
The Abstract identifies VDAC as the accepted channel for metabolite flux across the mitochondrial outer membrane. Section 3 reports that VDAC accounts for more than half the protein mass in the plant mitochondrial outer membranes studied, but does not establish that it is the most abundant protein in all mitochondrial outer membranes. Section 4 describes VDAC’s role in regulating mitochondrial metabolism as an unresolved question, so the claim that its control of metabolic flux is widely accepted goes beyond the source. (LLM, conf=0.84)
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Cites
Hodgkin, A. L., & Huxley, A. F. (1952) · The Journal of Physiology · doi:10.1113/jphysiol.1952.sp004764 · Cited by 23,191 · see citing works
The Fluid Mosaic Model of the Structure of Cell Membranes
Singer, S. J., & Nicolson, G. L. (1972) · Science · doi:10.1126/science.175.4023.720 · Cited by 9,158 · see citing works
Single-channel currents recorded from membrane of denervated frog muscle fibres
Neher, E., & Sakmann, B. J. (1976) · Nature · doi:10.1038/260799a0 · Cited by 2,577 · see citing works
Formation of Bimolecular Membranes from Lipid Monolayers and a Study of Their Electrical Properties
Montal, M., & Müeller, P. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.12.3561 · Cited by 1,811 · see citing works
Reconstitution of Cell Membrane Structure in vitro and its Transformation into an Excitable System
Müeller, P., Rudin, D. O., Tien, H. T., & Wescott, W. C. (1962) · Nature · doi:10.1038/194979a0 · Cited by 1,407 · see citing works
Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation
Kagawa, Y., & Racker, E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61930-1 · Cited by 1,360 · see citing works
A contribution to the theory of permeability of thin films
Danielli, J. F., & Davson, H. (1935) · Journal of Cellular and Comparative Physiology · doi:10.1002/jcp.1030050409 · Cited by 968 · see citing works
ON BIMOLECULAR LAYERS OF LIPOIDS ON THE CHROMOCYTES OF THE BLOOD
Gorter, E., & Grendel, F. (1925) · Journal of Experimental Medicine · doi:10.1084/jem.41.4.439 · Cited by 791 · see citing works
Schein, S. J., Colombini, M., & Finkelstein, A. (1976) · The Journal of Membrane Biology · doi:10.1007/bf01869662 · Cited by 509 · see citing works
Self-citationA candidate for the permeability pathway of the outer mitochondrial membrane
Colombini, M. (1979) · Nature · doi:10.1038/279643a0 · Cited by 468 · see citing works
Self-citationEnzyme Topology of Intracellular Membranes
DePierre, J. W., & Ernster, L. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.001221 · Cited by 386 · see citing works
Werkheiser, W. C., & Bartley, W. (1957) · Biochemical Journal · doi:10.1042/bj0660079 · Cited by 295 · see citing works
The external NADH dehydrogenases of intact plant mitochondria
Douce, R., Mannella, C. A., & Bonner, W. D. (1973) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(73)90255-7 · Cited by 228 · see citing works
Self-citationMitochondrial outer membrane contains a protein producing nonspecific diffusion channels.
Zalman, L. S., Nikaido, H., & Kagawa, Y. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85942-2 · Cited by 220 · see citing works
Mitchell, P. D., & Moyle, J. (1965) · Nature · doi:10.1038/2081205a0 · Cited by 206 · see citing works
Mannella, C. A. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.94.3.680 · Cited by 161 · see citing works
Self-citationThe nonelectrolyte permeability of planar lipid bilayer membranes.
Orbach, E., & Finkelstein, A. V. (1980) · The Journal of General Physiology · doi:10.1085/jgp.75.4.427 · Cited by 149 · see citing works
Phospholipase-Induced Crystallization of Channels in Mitochondrial Outer Membranes
Mannella, C. A. (1984) · Science · doi:10.1126/science.6322311 · Cited by 89 · see citing works
Self-citationParsons, D. F., Bonner, W. D., & Verboon, J. G. (1965) · Canadian Journal of Botany · doi:10.1139/b65-072 · Cited by 81 · see citing works
Biochemical characteristics of the outer membranes of plant mitochondria
Mannella, C. A., & Bonner, W. D. (1975) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(75)90105-4 · Cited by 75 · see citing works
Self-citationVDAC Channels Differentiate between Natural Metabolites and Synthetic Molecules
Rostovtseva, T. K., Komarov, A. G., Bezrukov, S. M., & Colombini, M. (2002) · The Journal of Membrane Biology · doi:10.1007/s00232-001-0159-1 · Cited by 67 · see citing works
Self-citationIon Transport Through Excitability-Inducing Material (EIM) Channels in Lipid Bilayer Membranes
Latorre, R., Ehrenstein, G., & Lecar, H. (1972) · The Journal of General Physiology · doi:10.1085/jgp.60.1.72 · Cited by 66 · see citing works
X-ray diffraction from oriented outer mitochondrial membranes
Mannella, C. A., & Bonner, W. D. (1975) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(75)90106-6 · Cited by 54 · see citing works
Self-citationMannella, C. A., & Colombini, M. (1984) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(84)90293-1 · Cited by 47 · see citing works
Self-citationNa+-gradient-stimulated AIB transport in membrane vesicles from Ehrlich ascites cells
Colombini, M., & Johnstone, R. M. (1974) · The Journal of Membrane Biology · doi:10.1007/bf01870120 · Cited by 46 · see citing works
Self-citationAltered Calcium Conductance in Pawns, Behavioural Mutants of Paramecium Aurelia
Schein, S. J., Bennett, M. V. L., & Katz, G. M. (1976) · Journal of Experimental Biology · doi:10.1242/jeb.65.3.699 · Cited by 32 · see citing works
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Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies
Midzak, A., & Papadopoulos, V. (2016) · Frontiers in Endocrinology · doi:10.3389/fendo.2016.00106 · Cited by 114 · see citing works
“Voltage-dependent anion channel is the most abundant protein of the mitochondrial outer membrane and is widely accepted as the principal route and control of metabolic flux between the cytosol and mitochondria (95).”
BackgroundLi, Q.-Q., Zhang, L., Wan, H.-Y., Liu, M., Li, X., & Tang, H. (2015) · Oncotarget · doi:10.18632/oncotarget.5318 · Cited by 46 · see citing works
- Authors
- Colombini, M., & Mannella, C. A.
- Affiliations
- University of Maryland, College Park (US)
- Wadsworth Center (US)
- Corresponding author
- Colombini, Marco
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 2012-06
- Volume
- 1818
- Issue
- 6
- Pages
- 1438-1443
- ISSN
- 0005-2736 (ISSN-L)
- PMC
- PMC3296906
- OpenAlex
- W2230130244
- Cited by
- 46
- References
- 26
- Citations by year
- 2026: 3 · 2024: 3 · 2023: 3 · 2022: 1 · 2021: 3 · 2020: 3 · 2018: 3 · 2017: 4 · 2016: 6 · 2015: 6 · 2014: 8 · 2013: 2 · 2012: 1
- FWCI
- 1.43
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation
- Medical Research Council Canada
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Social Sciences › Arts and Humanities › History and Philosophy of Science › History of Science and Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- voltage-dependent anion channel, mitochondrial outer membrane, mitochondrial permeability transition, metabolite flux, history of discovery, mitochondrial metabolism, serendipity in research, research collaboration
- MeSH terms
- Animals, Humans, Terminology as Topic, History, 20th Century, Voltage-Dependent Anion Channels, Electrophysiological Phenomena
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