ArticleBiophysical journal2014
Multiple discrete transitions underlie voltage-dependent activation in CLC Cl(-)/H(+) antiporters.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Determining the molecular basis of voltage sensitivity in membrane proteins.The Journal of general physiology · 2018Article
- Modulation of ClC-3 gating and proton/anion exchange by internal and external protons and the anion selectivity filter.The Journal of physiology · 2018Article
- Gating Charge Calculations by Computational Electrophysiology Simulations.Biophysical journal · 2017Article
- Gating the glutamate gate of CLC-2 chloride channel by pore occupancy.The Journal of general physiology · 2016Article
- Neuronal ClC-3 Splice Variants Differ in Subcellular Localizations, but Mediate Identical Transport Functions.The Journal of biological chemistry · 2015Article
- A tale of two CLCs: biophysical insights toward understanding ClC-5 and ClC-7 function in endosomes and lysosomes.The Journal of physiology · 2015Review
- Mutations associated with Dent's disease affect gating and voltage dependence of the human anion/proton exchanger ClC-5.Frontiers in physiology · 2015Article
- Behind the scenes of CLC gating: deriving the voltage dependence of membrane proteins by admittance measurements.Biophysical journal · 2014Article
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2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Most mammalian chloride channels and transporters in the CLC family display pronounced voltage-dependent gating. Surprisingly, despite the complex nature of the gating process and the large contribution to it by the transport substrates, experimental investigations of the fast gating process usually produce canonical Boltzmann activation curves that correspond to a simple two-state activation. By using nonlinear capacitance measurements of two mutations in the ClC-5 transporter, here we are able to discriminate and visualize discrete transitions along the voltage-dependent activation pathway. The strong and specific dependence of these transitions on internal and external [Cl(-)] suggest that CLC gating involves voltage-dependent conformational changes as well as coordinated movement of transported substrates.
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