Cited by 667Protein Structure and DynamicsLipid Membrane Structure and BehaviorIon channel regulation and function

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Solution Structure of the Integral Human Membrane Protein VDAC-1 in Detergent Micelles

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Hiller, Sebastian, Garces, Robert G., Malia, Thomas J., Orekhov, Vladislav Y., Colombini, Marco, Wagner, Gerhard·2008·Science

DOI 10.1126/science.1161302PMC PMC2579273

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Abstract

The voltage-dependent anion channel (VDAC) mediates trafficking of small molecules and ions across the eukaryotic outer mitochondrial membrane. VDAC also interacts with antiapoptotic proteins from the Bcl-2 family, and this interaction inhibits release of apoptogenic proteins from the mitochondrion. We present the nuclear magnetic resonance (NMR) solution structure of recombinant human VDAC-1 reconstituted in detergent micelles. It forms a 19-stranded β barrel with the first and last strand parallel. The hydrophobic outside perimeter of the barrel is covered by detergent molecules in a beltlike fashion. In the presence of cholesterol, recombinant VDAC-1 can form voltage-gated channels in phospholipid bilayers similar to those of the native protein. NMR measurements revealed the binding sites of VDAC-1 for the Bcl-2 protein Bcl-x L , for reduced β–nicotinamide adenine dinucleotide, and for cholesterol. Bcl-x L interacts with the VDAC barrel laterally at strands 17 and 18.

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NMR with Proteins and Nucleic Acids
Wüthrich, K. (1986) · Europhysics news · doi:10.1051/epn/19861701011 · Cited by 8,028
Cell Death
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598
Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
Olsen, J. V., Blagoev, B., Gnad, F., Maček, B., Kumar, C., Mortensen, P., & Mann, M. (2006) · Cell · doi:10.1016/j.cell.2006.09.026 · Cited by 3,562
Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178
Mitochondria as the central control point of apoptosis
Desagher, S., & Martinou, J. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01803-1 · Cited by 1,935
Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis?
Heiden, M. G. V., & Thompson, C. B. (1999) · Nature Cell Biology · doi:10.1038/70237 · Cited by 660
Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria
Schein, S. J., Colombini, M., & Finkelstein, A. (1976) · The Journal of Membrane Biology · doi:10.1007/bf01869662 · Cited by 509
Self-citation
VDAC: The channel at the interface between mitochondria and the cytosol
Colombini, M. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000009862.17396.8d · Cited by 500
Self-citation
A candidate for the permeability pathway of the outer mitochondrial membrane
Colombini, M. (1979) · Nature · doi:10.1038/279643a0 · Cited by 468
Self-citation

Show all 34 references

Research works printed but not linked: 1

This work was supported by NIH roadmap grant GM075879. Purchase operation and maintenance of instruments used were supported by NIH grants GM066360 GM47467 and EB002026. S.H. was supported by the Swiss National Science Foundation. V.Y.O. was supported by the Wenner-Gren Foundation Stockholm. Initial research on this project was supported by the Ludwig Foundation for Cancer Research. We thank V. Gelev from FBReagents.com Cambridge Massachusetts for custom synthesis of the 2 H-LDAO; S. Samanta for help with the electrophysiological measurements; and D. Frueh A. Koglin Z.-Y. J. Sun K. Oxenoid and S. Jenni for technical help and valuable discussions. The atomic coordinates of VDAC-1 in LDAO micelles have been deposited at the Protein Data Bank with code 2k4t.

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Authors: Hiller, S., Garces, R. G., Malia, T. J., Orekhov, V. Y., Colombini, M., & Wagner, G.
Affiliations: Harvard University (US)
Corresponding author: Garces, Robert G.
Malia, Thomas J.
Wagner, Gerhard
ORCID: Hiller, Sebastian
Orekhov, Vladislav Y.
Colombini, Marco
Wagner, Gerhard
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2008-08-29
Volume: 321
Issue: 5893
Pages: 1206-1210
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1161302
PMC: PMC2579273
OpenAlex: W1986199954
Cited by: 667
References: 34
Citations by year: 2026: 13 · 2025: 16 · 2024: 23 · 2023: 21 · 2022: 21 · 2021: 45 · 2020: 35 · 2019: 29 · 2018: 39 · 2017: 38 · 2016: 51 · 2015: 37 · 2014: 53 · 2013: 40 · 2012: 49
FWCI: 21.42
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Science (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (P41GM066360, R01GM075879, GM 075879, GM-066360, GM47467, P01GM047467)
National Institute of Biomedical Imaging and Bioengineering (EB 002026, P41EB002026)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
Keywords: VDAC1, voltage-dependent anion channel, mitochondrial outer membrane, beta-barrel membrane proteins, detergent micelles, Bcl-xL, Bcl-2 family proteins, apoptosis, cholesterol binding, NAD+ binding, voltage-gated ion channels, protein solution structure
MeSH terms: Amino Acid Sequence, Binding Sites, Cholesterol, Detergents, Dimethylamines, Humans, Lipid Bilayers, Micelles, Molecular Sequence Data, NAD, Protein Conformation, Recombinant Proteins, Ion Channel Gating, Protein Structure, Secondary, Protein Folding, Nuclear Magnetic Resonance, Biomolecular, Voltage-Dependent Anion Channel 1, bcl-X Protein, Static Electricity, Hydrophobic and Hydrophilic Interactions

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Solution Structure of the Integral Human Membrane Protein VDAC-1 in Detergent Micelles

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