Evidence map›Paper›PMID 18591423›Full record

ArticleThe Journal of general physiology2008

Intracellular proton regulation of ClC-0.

Giovanni Zifarelli, Anna Rosa Murgia, Paolo Soliani, Michael Pusch

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 37 citations in OpenAlex.

  1. Insights into CLC-0's Slow-Gating from Intracellular Proton Inhibition.International journal of molecular sciences · 2024
    Article
  2. Biophysical and Pharmacological Insights to CLC Chloride Channels.Handbook of experimental pharmacology · 2024
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
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  12. Molecular mechanism of proton transport in CLC Cl-/H+ exchange transporters.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Proton block of the CLC-5 Cl-/H+ exchanger.The Journal of general physiology · 2010
    Article
  20. Article
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

4 authors at 1 institution in 1 country.

Giovanni ZifarelliIstituto di Biofisica, Consiglio Nazionale delle Ricerche, I-16149 Genova, Italy.
Anna Rosa Murgia
Paolo Soliani
Michael Pusch
Instituto di Biofisica · ES

Funding

Telethon GGP04018
6 · The paper itself

Abstract

Some CLC proteins function as passive Cl(-) ion channels whereas others are secondary active chloride/proton antiporters. Voltage-dependent gating of the model Torpedo channel ClC-0 is modulated by intracellular and extracellular pH, possibly reflecting a mechanistic relationship with the chloride/proton coupling of CLC antiporters. We used inside-out patch clamp measurements and mutagenesis to explore the dependence of the fast gating mechanism of ClC-0 on intracellular pH and to identify the putative intracellular proton acceptor(s). Among the tested residues (S123, K129, R133, K149, E166, F214L, S224, E226, V227, C229, R305, R312, C415, H472, F418, V419, P420, and Y512) only mutants of E166, F214, and F418 qualitatively changed the pH(int) dependence. No tested amino acid emerged as a valid candidate for being a pH sensor. A detailed kinetic analysis of the dependence of fast gate relaxations on pH(int) and [Cl(-)](int) provided quantitative constraints on possible mechanistic models of gating. In one particular model, a proton is generated by the dissociation of a water molecule in an intrapore chloride ion binding site. The proton is delivered to the side chain of E166 leading to the opening of the channel, while the hydroxyl ion is stabilized in the internal/central anion binding site. Deuterium isotope effects confirm that proton transfer is rate limiting for fast gate opening and that channel closure depends mostly on the concentration of OH(-) ions. The gating model is in natural agreement with the finding that only the closing rate constant, but not the opening rate constant, depends on pH(int) and [Cl(-)](int).

Indexed as

ProtonsAlgorithmsAmino Acid SubstitutionAnimalsChloride ChannelsChloridesDeuterium OxideElectric StimulationElectrophysiologyFemaleHydrogen-Ion ConcentrationIon Channel GatingKineticsModels, MolecularMutationOocytesChloride ChannelsChloridesCLC-0 chloride channel protein, Torpedo californicaDeuterium OxideProtonsRecombinant ProteinsWater

Identifiers

PMID18591423
PMCPMC2442169
OpenAlexW2031806724

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.