ArticleThe Journal of general physiology2003
Electrostatic control and chloride regulation of the fast gating of ClC-0 chloride channels.
Article in The Journal of general physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- Insights into CLC-0's Slow-Gating from Intracellular Proton Inhibition.International journal of molecular sciences · 2024Article
- Dynamical model of the CLC-2 ion channel reveals conformational changes associated with selectivity-filter gating.PLoS computational biology · 2020Article
- Proton-dependent inhibition, inverted voltage activation, and slow gating of CLC-0 Chloride Channel.PloS one · 2020Article
- Structure of the human ClC-1 chloride channel.PLoS biology · 2019Article
- A tale of two CLCs: biophysical insights toward understanding ClC-5 and ClC-7 function in endosomes and lysosomes.The Journal of physiology · 2015Review
- Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter.Nature structural & molecular biology · 2014Article
- Regulatory phosphorylation induces extracellular conformational changes in a CLC anion channel.Biophysical journal · 2013Article
- A three-state multi-ion kinetic model for conduction properties of ClC-0 chloride channel.Biophysical journal · 2010Article
- Accessibility of the CLC-0 pore to charged methanethiosulfonate reagents.Biophysical journal · 2010Article
- Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms.The Journal of general physiology · 2009Article
- Intracellular proton regulation of ClC-0.The Journal of general physiology · 2008Article
- The role of a conserved lysine in chloride- and voltage-dependent ClC-0 fast gating.The Journal of general physiology · 2007Article
- Roles of K149, G352, and H401 in the channel functions of ClC-0: testing the predictions from theoretical calculations.The Journal of general physiology · 2006Article
- The fast gating mechanism in ClC-0 channels.Biophysical journal · 2005Article
- Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule.The Journal of general physiology · 2005Article
- Exterior site occupancy infers chloride-induced proton gating in a prokaryotic homolog of the ClC chloride channel.Biophysical journal · 2004Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The opening and closing of chloride (Cl-) channels in the ClC family are thought to tightly couple to ion permeation through the channel pore. In the prototype channel of the family, the ClC-0 channel from the Torpedo electric organ, the opening-closing of the pore in the millisecond time range known as "fast gating" is regulated by both external and internal Cl- ions. Although the external Cl- effect on the fast-gate opening has been extensively studied at a quantitative level, the internal Cl- regulation remains to be characterized. In this study, we examine the internal Cl- effects and the electrostatic controls of the fast-gating mechanism. While having little effect on the opening rate, raising [Cl-]i reduces the closing rate (or increases the open time) of the fast gate, with an apparent affinity of >1 M, a value very different from the one observed in the external Cl- regulation on the opening rate. Mutating charged residues in the pore also changes the fast-gating properties-the effects are more prominent on the closing rate than on the opening rate, a phenomenon similar to the effect of [Cl-]i on the fast gating. Thus, the alteration of fast-gate closing by charge mutations may come from a combination of two effects: a direct electrostatic interaction between the manipulated charge and the negatively charged glutamate gate and a repulsive force on the gate mediated by the permeant ion. Likewise, the regulations of internal Cl- on the fast gating may also be due to the competition of Cl- with the glutamate gate as well as the overall more negative potential brought to the pore by the binding of Cl-. In contrast, the opening rate of the fast gate is only minimally affected by manipulations of [Cl-]i and charges in the inner pore region. The very different nature of external and internal Cl- regulations on the fast gating thus may suggest that the opening and the closing of the fast gate are not microscopically reversible processes, but form a nonequilibrium cycle in the ClC-0 fast-gating mechanism.
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