ArticleThe Journal of physiology2002
Effect of an N-terminus deletion on voltage-dependent gating of the ClC-2 chloride channel.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed.
- Article
- Biophysical and Pharmacological Insights to CLC Chloride Channels.Handbook of experimental pharmacology · 2024Article
- Adrenal Anion Channels: New Roles in Zona Glomerulosa Physiology and in the Pathophysiology of Primary Aldosteronism.Handbook of experimental pharmacology · 2024Article
- CryoEM structures of the human CLC-2 voltage gated chloride channel reveal a ball and chain gating mechanism.bioRxiv : the preprint server for biology · 2023Article
- Cryo-EM structures of ClC-2 chloride channel reveal the blocking mechanism of its specific inhibitor AK-42.Nature communications · 2023Article
- Article
- Dynamical model of the CLC-2 ion channel reveals conformational changes associated with selectivity-filter gating.PLoS computational biology · 2020Article
- Pathogenesis of hypertension in a mouse model for human CLCN2 related hyperaldosteronism.Nature communications · 2019Article
- Pathogenesis of Familial Hyperaldosteronism Type II: New Concepts Involving Anion Channels.Current hypertension reports · 2019Review
- A gain-of-function mutation in the CLCN2 chloride channel gene causes primary aldosteronism.Nature genetics · 2018Article
- Prolonged ATScientific reports · 2017Article
- Research and progress on ClC‑2 (Review).Molecular medicine reports · 2017Review
- Cavβ2 transcription start site variants modulate calcium handling in newborn rat cardiomyocytes.Pflugers Archiv : European journal of physiology · 2015Article
- GlialCAM, a CLC-2 Cl(-) channel subunit, activates the slow gate of CLC chloride channels.Biophysical journal · 2014Article
- Chloride channelopathies of ClC-2.International journal of molecular sciences · 2013Review
- Regulation of ClC-2 gating by intracellular ATP.Pflugers Archiv : European journal of physiology · 2013Article
- Functional characterization of a ClC-2-like Cl(-) conductance in surface epithelial cells of rat rectal colon.The Journal of membrane biology · 2010Article
- P2X4 activation modulates volume-sensitive outwardly rectifying chloride channels in rat hepatoma cells.The Journal of biological chemistry · 2010Article
- Cumulative activation of voltage-dependent KVS-1 potassium channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- Removal of gating in voltage-dependent ClC-2 chloride channel by point mutations affecting the pore and C-terminus CBS-2 domain.The Journal of physiology · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ClC-2, a chloride channel widely expressed in mammalian tissues, is activated by hyperpolarisation and extracellular acidification. Deletion of amino acids 16-61 in rat ClC-2 abolishes voltage and pH dependence in two-electrode voltage-clamp experiments in amphibian oocytes. These results have been interpreted in terms of a ball-and-chain type of mechanism in which the N-terminus would behave as a ball that is removed from an inactivating site upon hyperpolarisation. We now report whole-cell patch-clamp measurements in mammalian cells showing hyperpolarization-activation of rClC-2Delta16-61 differing only in presenting faster opening and closing kinetics than rClC-2. The lack of time and voltage dependence observed previously was reproduced, however, in nystatin-perforated patch experiments. The behaviour of wild-type rClC-2 did not differ between conventional and nystatin-perforated patches. Similar results were obtained with ClC-2 from guinea-pig. One possible explanation of the results is that some diffusible component is able to lock the channel in an open state but does so only to the mutated channel. Alternative explanations involving the osmotic state of the cell and cytoskeleton structure are also considered. Low extracellular pH activates the wild-type channel but not rClC-2Delta16-61 when expressed in oocytes, a result that had been interpreted to suggest that protons affect the ball-and-chain mechanism. In our experiments no difference was seen in the effect of extracellular pH upon rClC-2 and rClC-2Delta16-61 in either recording configuration, suggesting that protons act independently from possible effects of the N-terminus on gating. Our observations of voltage-dependent gating of the N-terminal deleted ClC-2 are an argument against a ball-and-chain mechanism for this channel.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.