ArticleThe Journal of general physiology2003
Probing the pore of ClC-0 by substituted cysteine accessibility method using methane thiosulfonate reagents.
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 40 papers.
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Who cites it
40 citing papers in PubMed, 62 citations in OpenAlex.
- Chloride ions in health and disease.Bioscience reports · 2024Review
- Biophysical and Pharmacological Insights to CLC Chloride Channels.Handbook of experimental pharmacology · 2024Article
- Cyclic Thiosulfonates for Thiol-Mediated Uptake: Cascade Exchangers, Transporters, Inhibitors.JACS Au · 2022Article
- A CLC-ec1 mutant reveals global conformational change and suggests a unifying mechanism for the CLC CleLife · 2020Article
- Dynamical model of the CLC-2 ion channel reveals conformational changes associated with selectivity-filter gating.PLoS computational biology · 2020Article
- Comparison of ion transport determinants between a TMEM16 chloride channel and phospholipid scramblase.The Journal of general physiology · 2019Article
- Chloride Ion Transport by theFrontiers in chemistry · 2018Article
- Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters.eLife · 2017Article
- Helix O modulates voltage dependency of CLC-1.Pflugers Archiv : European journal of physiology · 2017Article
- Modulation of the slow/common gating of CLC channels by intracellular cadmium.The Journal of general physiology · 2015Article
- A single point mutation reveals gating of the human ClC-5 Cl-/H+ antiporter.The Journal of physiology · 2013Article
- Alkaline pH block of CLC-K kidney chloride channels mediated by a pore lysine residue.Biophysical journal · 2013Article
- A designed inhibitor of a CLC antiporter blocks function through a unique binding mode.Chemistry & biology · 2012Article
- Extracellular determinants of anion discrimination of the Cl-/H+ antiporter protein CLC-5.The Journal of biological chemistry · 2011Article
- Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.The Journal of general physiology · 2010Article
- Permeant anions contribute to voltage dependence of ClC-2 chloride channel by interacting with the protopore gate.The Journal of physiology · 2010Article
- Accessibility of the CLC-0 pore to charged methanethiosulfonate reagents.Biophysical journal · 2010Article
- Voltage-dependent and -independent titration of specific residues accounts for complex gating of a ClC chloride channel by extracellular protons.The Journal of physiology · 2009Article
- Review. Proton-coupled gating in chloride channels.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2009Review
- Blocking pore-open mutants of CLC-0 by amphiphilic blockers.The Journal of general physiology · 2009Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
ClC channels are a family of protein molecules containing two ion-permeation pores. Although these transmembrane proteins are important for a variety of physiological functions, their molecular operations are only superficially understood. High-resolution X-ray crystallography techniques have recently revealed the structures of two bacterial ClC channels, but whether vertebrate ClC channel pores are similar to those of bacterial homologues is not clear. To study the pore architecture of the Torpedo ClC-0 channel, we employed the substituted-cysteine-accessibility method (SCAM) and used charged methane thiosulfonate (MTS) compounds to modify the introduced cysteine. Several conclusions were derived from this approach. First, the MTS modification pattern from Y512C to E526C in ClC-0, which corresponds to residues forming helix R in bacterial ClC channels, is indeed consistent with the suggested helical structure. Second, the ClC-0 pore is more accessible to the negatively charged than to the positively charged MTS compound, a pore property that is regulated by the intrinsic electrostatic potential in the pore. Finally, attempts to modify the introduced cysteine at positions intracellular to the selectivity filter did not result in larger MTS modification rates for the open-state channel, suggesting that the fast gate of ClC-0 cannot be located at a position intracellular to the Cl- selectivity filter. Thus, the proposal that the glutamate side chain is the fast gate of the channel is applicable to ClC-0, revealing a structural and functional conservation of ClC channels between bacterial and vertebrate species.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.