Evidence map›Paper›PMID 24638271›Full record

ArticlePflugers Archiv : European journal of physiology2014

ClC-1 and ClC-2 form hetero-dimeric channels with novel protopore functions.

Gabriel Stölting, Martin Fischer, Christoph Fahlke

Abstract read
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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Structural basis of pH-dependent activation in a CLC transporter.Nature structural & molecular biology · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Glial Chloride Channels in the Function of the Nervous System Across Species.Advances in experimental medicine and biology · 2021
    Article
  7. Review
  8. Research and progress on ClC‑2 (Review).Molecular medicine reports · 2017
    Review
  9. Helix O modulates voltage dependency of CLC-1.Pflugers Archiv : European journal of physiology · 2017
    Article
  10. Review
  11. The ClC-K2 Chloride Channel Is Critical for Salt Handling in the Distal Nephron.Journal of the American Society of Nephrology : JASN · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
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 2 institutions in 1 country.

Gabriel StöltingInstitute of Complex Systems-Zelluläre Biophysik (ICS-4), Forschungszentrum Jülich, 52425, Jülich, Germany, g.stoelting@fz-juelich.de.
Martin Fischer
Christoph Fahlke
Forschungszentrum Jülich · DEMedizinische Hochschule Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CLC-type chloride channels exhibit a unique double-barreled architecture with two independently functioning ion conduction pathways, the so-called protopores. There exist gating processes that open and close individual protopores as well as common processes that jointly mediate slow opening and closing of both protopores. Different isoforms exhibit distinct voltage dependences and kinetics of gating. Whereas opening of the individual and common gate of homo-dimeric ClC-1 is promoted by membrane depolarization, ClC-2 is closed at positive potentials and opens only at negative voltages. To characterize the functional interaction of protopores we engineered a concatameric construct linking the coding regions of ClC-1 and ClC-2 in an open reading frame, expressed it in mammalian cells and measured anion currents through whole-cell and single channel patch clamping. In the hetero-dimeric assembly, each protopore displayed two kinetically distinct gating processes. Fast gating of the ClC-1 protopore closely resembled fast protopore gating of homo-dimeric channels. The voltage dependence of ClC-2 fast gating was shifted to more positive potentials by the adjacent ClC-1 protopore, resulting in open ClC-2 protopores at positive voltages. We observed two slow gating processes individually acting on ClC-1 and ClC-2 protopores, with distinct time and voltage dependences. Single channel recordings demonstrated that hetero-dimerization additionally modified the unitary conductance of ClC-2 protopores. Our findings suggest that inter-subunit interactions do not only affect common gating, but also ion permeation and gating of individual protopores in hetero-dimeric ClC channels.

Indexed as

Chloride ChannelsCLC-2 Chloride ChannelsHEK293 CellsHumansIon Channel GatingProtein BindingProtein MultimerizationProtein Structure, TertiaryChloride ChannelsCLC-1 channelCLC-2 Chloride Channels

Identifiers

PMID24638271
OpenAlexW2007449077

What OpenQuestion holds

Textmetadata
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.