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Sci. STKE, 24 June 2003
Vol. 2003, Issue 188, p. pe23
[DOI: 10.1126/stke.2003.188.pe23]

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Coupling Gating with Ion Permeation in ClC Channels

Tsung-Yu Chen*

Center for Neuroscience and Department of Neurology, University of California, Davis, CA, 95616

Abstract: In ClC chloride (Cl) channels, unlike cation-selective ion channels, ion permeation is intimately coupled to fast gating. Recent research comparing the crystallographic structure of a bacterial ClC channel with functional studies of a Torpedo ClC channel suggests that gating depends on the negatively charged carboxyl group on a glutamate residue, which blocks the channel pore. In this model, the permeating Cl competes with the carboxyl group for an anion-binding site in the channel pore. This model of Cl competition with a glutamate gate helps explain the effect of intracellular Cl on channel gating; the mechanism underlying the effects of extracellular Cl, however, remains to be determined, as does the nature of the Cl channel slow gate.

*Contact information. E-mail: tycchen{at}ucdavis.edu

Citation: T.-Y. Chen, Coupling Gating with Ion Permeation in ClC Channels. Sci. STKE 2003, pe23 (2003).

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
CLC-0 and CFTR: Chloride Channels Evolved From Transporters.
T.-Y. Chen and T.-C. Hwang (2008)
Physiol Rev 88, 351-387
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The voltage-dependent ClC-2 chloride channel has a dual gating mechanism.
L. Zuniga, M. I. Niemeyer, D. Varela, M. Catalan, L. P. Cid, and F. V. Sepulveda (2004)
J. Physiol. 555, 671-682
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A conserved pore-lining glutamate as a voltage- and chloride-dependent gate in the ClC-2 chloride channel.
M. I. Niemeyer, L P. Cid, L. Zuniga, M. Catalan, and F. V Sepulveda (2003)
J. Physiol. 553, 873-879
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