ArticleThe Journal of general physiology2006
Proton sensing of CLC-0 mutant E166D.
Article in The Journal of general physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 53 citations in OpenAlex.
- Insights into CLC-0's Slow-Gating from Intracellular Proton Inhibition.International journal of molecular sciences · 2024Article
- Functional and clinical studies reveal pathophysiological complexity of CLCN4-related neurodevelopmental condition.Molecular psychiatry · 2023Article
- Molecular determinants underlying volume-regulated anion channel subunit-dependent oxidation sensitivity.The Journal of physiology · 2022Article
- Electro-steric opening of the CLC-2 chloride channel gate.Scientific reports · 2021Article
- Dynamical model of the CLC-2 ion channel reveals conformational changes associated with selectivity-filter gating.PLoS computational biology · 2020Article
- Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC ClProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Two Cl Ions and a Glu Compete for a Helix Cage in the CLC Proton/ClBiophysical journal · 2017Article
- Probing the conformation of a conserved glutamic acid within the ClThe Journal of general physiology · 2017Article
- Regulatory Conformational Coupling between CLC Anion Channel Membrane and Cytoplasmic Domains.Biophysical journal · 2016Article
- Gating the glutamate gate of CLC-2 chloride channel by pore occupancy.The Journal of general physiology · 2016Article
- In the beginning: a personal reminiscence on the origin and legacy of ClC-0, the 'Torpedo Cl(-) channel'.The Journal of physiology · 2015Review
- Structure and gating of CLC channels and exchangers.The Journal of physiology · 2015Review
- A tale of two CLCs: biophysical insights toward understanding ClC-5 and ClC-7 function in endosomes and lysosomes.The Journal of physiology · 2015Review
- GlialCAM, a CLC-2 Cl(-) channel subunit, activates the slow gate of CLC chloride channels.Biophysical journal · 2014Article
- Common gating of both CLC transporter subunits underlies voltage-dependent activation of the 2Cl-/1H+ exchanger ClC-7/Ostm1.The Journal of biological chemistry · 2013Article
- Alkaline pH block of CLC-K kidney chloride channels mediated by a pore lysine residue.Biophysical journal · 2013Article
- Sequential interaction of chloride and proton ions with the fast gate steer the voltage-dependent gating in ClC-2 chloride channels.The Journal of physiology · 2012Article
- On the mechanism of gating charge movement of ClC-5, a human Cl(-)/H(+) antiporter.Biophysical journal · 2012Article
- Intracellular proton access in a Cl(-)/H(+) antiporter.PLoS biology · 2012Article
- Anion- and proton-dependent gating of ClC-4 anion/proton transporter under uncoupling conditions.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
CLC Cl- channels are homodimers in which each subunit has a proper pore and a (fast) gate. An additional slow gate acts on both pores. A conserved glutamate (E166 in CLC-0) is a major determinant of gating in CLC-0 and is crucially involved in Cl-/H+ antiport of CLC-ec1, a CLC of known structure. We constructed tandem dimers with one wild-type (WT) and one mutant subunit (E166A or E166D) to show that these mutations of E166 specifically alter the fast gate of the pore to which they belong without effect on the fast gate of the neighboring pore. In addition both mutations activate the common slow gate. E166A pores have a large, voltage-independent open probability of the fast gate (popen), whereas popen of E166D pores is dramatically reduced. Similar to WT, popen of E166D was increased by lowering pHint. At negative voltages, E166D presents a persistent inward current that is blocked by p-chlorophenoxy-acetic acid (CPA) and increased at low pHext. The pHext dependence of the persistent current is analogous to a similar steady inward current in WT CLC-0. Surprisingly, however, the underlying unitary conductance of the persistent current in E166D is about an order of magnitude smaller than that of the transient deactivating inward Cl- current. Collectively, our data support the possibility that the mutated CLC-0 channel E166D can assume two distinct open states. Voltage-independent protonation of D166 from the outside favors a low conductance state, whereas protonation from the inside favors the high conductance state.
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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.