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.
| Original language | English (US) |
|---|---|
| Journal | Science's STKE : signal transduction knowledge environment |
| Volume | 2003 |
| Issue number | 188 |
| State | Published - 2003 |
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Coupling gating with ion permeation in ClC channels. / Chen, Tsung-Yu.
In: Science's STKE : signal transduction knowledge environment, Vol. 2003, No. 188, 2003.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Coupling gating with ion permeation in ClC channels.
AU - Chen, Tsung-Yu
PY - 2003
Y1 - 2003
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0037811498&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037811498&partnerID=8YFLogxK
M3 - Article
C2 - 12824475
AN - SCOPUS:0037811498
VL - 2003
JO - Science Signaling
JF - Science Signaling
SN - 1937-9145
IS - 188
ER -