Evidence map›Paper›PMID 14581587›Full record

ArticleThe Journal of general physiology2003

Electrostatic control and chloride regulation of the fast gating of ClC-0 chloride channels.

Tsung-Yu Chen, Mei-Fang Chen, Chia-Wei Lin

Open access · bronzeAbstract read
In one paragraph

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 40 citations in OpenAlex.

  1. Insights into CLC-0's Slow-Gating from Intracellular Proton Inhibition.International journal of molecular sciences · 2024
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  11. Intracellular proton regulation of ClC-0.The Journal of general physiology · 2008
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Tsung-Yu ChenCenter for Neuroscience University of California-Davis, 1544 Newton Court, Davis, CA 95616, USA. tycchen@ucdavis.edu
Mei-Fang Chen
Chia-Wei Lin
University of California, Davis · US

Funding

Molecular Physiology of CLC Chloride ChannelsR01GM065447 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI CHEN, TSUNG-YU · 2003 to 2018
$3.9M
Gating Mechanisms of CLC Chloride ChannelsR56GM065447 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, TSUNG-YU · 2008 to 2008
$375k
NIGMS NIH HHS GM65447NIGMS NIH HHS R01 GM065447NIGMS NIH HHS R56 GM065447
6 · The paper itself

Abstract

The opening and closing of chloride (Cl-) channels in the ClC family are thought to tightly couple to ion permeation through the channel pore. In the prototype channel of the family, the ClC-0 channel from the Torpedo electric organ, the opening-closing of the pore in the millisecond time range known as "fast gating" is regulated by both external and internal Cl- ions. Although the external Cl- effect on the fast-gate opening has been extensively studied at a quantitative level, the internal Cl- regulation remains to be characterized. In this study, we examine the internal Cl- effects and the electrostatic controls of the fast-gating mechanism. While having little effect on the opening rate, raising [Cl-]i reduces the closing rate (or increases the open time) of the fast gate, with an apparent affinity of >1 M, a value very different from the one observed in the external Cl- regulation on the opening rate. Mutating charged residues in the pore also changes the fast-gating properties-the effects are more prominent on the closing rate than on the opening rate, a phenomenon similar to the effect of [Cl-]i on the fast gating. Thus, the alteration of fast-gate closing by charge mutations may come from a combination of two effects: a direct electrostatic interaction between the manipulated charge and the negatively charged glutamate gate and a repulsive force on the gate mediated by the permeant ion. Likewise, the regulations of internal Cl- on the fast gating may also be due to the competition of Cl- with the glutamate gate as well as the overall more negative potential brought to the pore by the binding of Cl-. In contrast, the opening rate of the fast gate is only minimally affected by manipulations of [Cl-]i and charges in the inner pore region. The very different nature of external and internal Cl- regulations on the fast gating thus may suggest that the opening and the closing of the fast gate are not microscopically reversible processes, but form a nonequilibrium cycle in the ClC-0 fast-gating mechanism.

Indexed as

AnimalsChloride ChannelsChloridesFemaleIon Channel GatingMutagenesis, Site-DirectedStatic ElectricityXenopusChloride ChannelsChloridesCLC-0 chloride channel protein, Torpedo californica

Identifiers

PMID14581587
PMCPMC2229583
OpenAlexW2095642680

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.