ArticleThe Journal of general physiology2005
Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule.
Article in The Journal of general physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 58 citations in OpenAlex.
- 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
- Chloride Ion Transport by theFrontiers in chemistry · 2018Article
- Helix O modulates voltage dependency of CLC-1.Pflugers Archiv : European journal of physiology · 2017Article
- Computationally Efficient Multiscale Reactive Molecular Dynamics to Describe Amino Acid Deprotonation in Proteins.Journal of chemical theory and computation · 2016Article
- A tale of two CLCs: biophysical insights toward understanding ClC-5 and ClC-7 function in endosomes and lysosomes.The Journal of physiology · 2015Review
- 13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.Journal of biomolecular NMR · 2015Article
- Water access points and hydration pathways in CLC H+/Cl- transporters.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A single point mutation reveals gating of the human ClC-5 Cl-/H+ antiporter.The Journal of physiology · 2013Article
- Cysteine scanning of CFTR's first transmembrane segment reveals its plausible roles in gating and permeation.Biophysical journal · 2013Article
- A designed inhibitor of a CLC antiporter blocks function through a unique binding mode.Chemistry & biology · 2012Article
- CLC anion channel regulatory phosphorylation and conserved signal transduction domains.Biophysical journal · 2012Article
- Molecular mechanism of proton transport in CLC Cl-/H+ exchange transporters.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Extracellular determinants of anion discrimination of the Cl-/H+ antiporter protein CLC-5.The Journal of biological chemistry · 2011Article
- Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle.Science (New York, N.Y.) · 2010Article
- Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.The Journal of general physiology · 2010Article
- Antiport mechanism for Cl(-)/H(+) in ClC-ec1 from normal-mode analysis.Biophysical journal · 2010Article
- Accessibility of the CLC-0 pore to charged methanethiosulfonate reagents.Biophysical journal · 2010Article
- Chloride channels: often enigmatic, rarely predictable.Annual review of physiology · 2010Review
- Channel-like slippage modes in the human anion/proton exchanger ClC-4.The Journal of general physiology · 2009Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ClC chloride channels, which are ubiquitously expressed in mammals, have a unique double-barreled structure, in which each monomer forms its own pore. Identification of pore-lining elements is important for understanding the conduction properties and unusual gating mechanisms of these channels. Structures of prokaryotic ClC transporters do not show an open pore, and so may not accurately represent the open state of the eukaryotic ClC channels. In this study we used cysteine-scanning mutagenesis and modification (SCAM) to screen >50 residues in the intracellular vestibule of ClC-0. We identified 14 positions sensitive to the negatively charged thiol-modifying reagents sodium (2-sulfonatoethyl)methanethiosulfonate (MTSES) or sodium 4-acetamido-4'-maleimidylstilbene-2'2-disulfonic acid (AMS) and show that 11 of these alter pore properties when modified. In addition, two MTSES-sensitive residues, on different helices and in close proximity in the prokaryotic structures, can form a disulfide bond in ClC-0. When mapped onto prokaryotic structures, MTSES/AMS-sensitive residues cluster around bound chloride ions, and the correlation is even stronger in the ClC-0 homology model developed by Corry et al. (2004). These results support the hypothesis that both secondary and tertiary structures in the intracellular vestibule are conserved among ClC family members, even in regions of very low sequence similarity.
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