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Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel.
Department of Zoology, University of Maryland, College Park 20742.
Voltage-gated ion-channel proteins contain "voltage-sensing" domains that drive the conformational transitions between open and closed states in response to changes in transmembrane voltage. We have used site-directed mutagenesis to identify residues affecting the voltage sensitivity of a mitochondrial channel, the voltage-dependent anion-selective channel (VDAC). Although charge changes at many sites had no effect, at other sites substitutions that increased positive charge also increased the steepness of voltage dependence and substitutions that decreased positive charge decreased voltage dependence by an appropriate amount. In contrast to the plasma membrane K+ and Na+ channels, these residues are distributed over large parts of the VDAC protein. These results have been used to define the conformational transitions that accompany voltage gating of an ion channel. This gating mechanism requires the movement of large portions of the VDAC protein through the membrane.
PMID: 7685903 [PubMed - indexed for MEDLINE]
PMCID: PMC46737
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Cited by 12 PubMed Central articles
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Opening and closing the metabolite gate.
Törnroth-Horsefield S, Neutze R.
Proc Natl Acad Sci U S A. 2008 Dec 16; 105(50):19565-6. Epub 2008 Dec 10.
[Proc Natl Acad Sci U S A. 2008]
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The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating.
Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J, Toro L, Ping P, Abramson J.
Proc Natl Acad Sci U S A. 2008 Nov 18; 105(46):17742-7. Epub 2008 Nov 6.
[Proc Natl Acad Sci U S A. 2008]
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Structure of the human voltage-dependent anion channel.
Bayrhuber M, Meins T, Habeck M, Becker S, Giller K, Villinger S, Vonrhein C, Griesinger C, Zweckstetter M, Zeth K.
Proc Natl Acad Sci U S A. 2008 Oct 7; 105(40):15370-5. Epub 2008 Oct 1.
[Proc Natl Acad Sci U S A. 2008]
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