Evidence map›Paper›PMID 20051516›Full record

ArticleThe Journal of biological chemistry2010

Disruption of the K+ channel beta-subunit KCNE3 reveals an important role in intestinal and tracheal Cl- transport.

Patricia Preston, Lena Wartosch, Dorothee Günzel, Michael Fromm, Patthara Kongsuphol, Jiraporn Ousingsawat, Karl Kunzelmann, Jacques Barhanin, Richard Warth, Thomas J Jentsch

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

70 citing papers in PubMed, 105 citations in OpenAlex.

  1. Potassium Channels of the Airway Epithelium.Acta physiologica (Oxford, England) · 2026
    Review
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  5. Article
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  12. KCNE1 does not shift TMEM16A from a CaPflugers Archiv : European journal of physiology · 2023
    Article
  13. Mechanism of external K+ sensitivity of KCNQ1 channels.The Journal of general physiology · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

10 more citing papers are in PubMed but not listed here.

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

10 authors at 4 institutions in 2 countries.

Patricia PrestonLeibniz-Institut für Molekulare Pharmakologie and Max-Delbrück-Centrum für Molekulare Medizin, 13125 Berlin, Germany.
Lena Wartosch
Dorothee Günzel
Michael Fromm
Patthara Kongsuphol
Jiraporn Ousingsawat
Karl Kunzelmann
Jacques Barhanin
Richard Warth
Thomas J Jentsch
Charité - Universitätsmedizin Berlin · DELeibniz-Forschungsinstitut für Molekulare Pharmakologie · DEUniversity of Regensburg · DEUniversité Côte d'Azur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The KCNE3 beta-subunit constitutively opens outwardly rectifying KCNQ1 (Kv7.1) K(+) channels by abolishing their voltage-dependent gating. The resulting KCNQ1/KCNE3 heteromers display enhanced sensitivity to K(+) channel inhibitors like chromanol 293B. KCNE3 was also suggested to modify biophysical properties of several other K(+) channels, and a mutation in KCNE3 was proposed to underlie forms of human periodic paralysis. To investigate physiological roles of KCNE3, we now disrupted its gene in mice. kcne3(-/-) mice were viable and fertile and displayed neither periodic paralysis nor other obvious skeletal muscle abnormalities. KCNQ1/KCNE3 heteromers are present in basolateral membranes of intestinal and tracheal epithelial cells where they might facilitate transepithelial Cl(-) secretion through basolateral recycling of K(+) ions and by increasing the electrochemical driving force for apical Cl(-) exit. Indeed, cAMP-stimulated electrogenic Cl(-) secretion across tracheal and intestinal epithelia was drastically reduced in kcne3(-/-) mice. Because the abundance and subcellular localization of KCNQ1 was unchanged in kcne3(-/-) mice, the modification of biophysical properties of KCNQ1 by KCNE3 is essential for its role in intestinal and tracheal transport. Further, these results suggest KCNE3 as a potential modifier gene in cystic fibrosis.

Indexed as

AnimalsCell LineChloridesGastric MucosaHumansIntestinal MucosaIntestinesKCNQ1 Potassium ChannelMiceMice, KnockoutMuscle, SkeletalPatch-Clamp TechniquesPotassium Channels, Voltage-GatedProtein Structure, QuaternaryProtein SubunitsRotarod Performance TestChloridesKcne3 protein, mouseKCNQ1 Potassium ChannelPotassium Channels, Voltage-GatedProtein Subunits

Identifiers

PMID20051516
PMCPMC2844166
OpenAlexW2114192621

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.