Evidence map›Paper›PMID 20962273›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Stoichiometry of the KCNQ1 - KCNE1 ion channel complex.

Koichi Nakajo, Maximilian H Ulbrich, Yoshihiro Kubo, Ehud Y Isacoff

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
9.1field-weighted citation impact, top 2% 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

110 citing papers in PubMed, 199 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026
    Review
  5. KCNQ1 and PIPCell research · 2025
    Article
  6. Article
  7. Functional Profiling ofCirculation. Genomic and precision medicine · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Targeting the ICirculation research · 2024
    Article
  15. Article
  16. Review
  17. Mechanism of external K+ sensitivity of KCNQ1 channels.The Journal of general physiology · 2023
    Article
  18. Article
  19. Article
  20. Modulation of the IBBA advances · 2023
    Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Koichi NakajoDivision of Biophysics and Neurobiology, National Institute for Physiological Sciences, Okazaki, Aichi 444-8585, Japan.
Maximilian H Ulbrich
Yoshihiro Kubo
Ehud Y Isacoff
National Institute for Physiological Sciences · JPUniversity of California, Berkeley · US

Funding

STRUCTURAL REARRANGEMENTS IN CHANNEL GATINGR01NS035549 · NINDS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ISACOFF, EHUD · 1996 to 2013
$4.1M
NINDS NIH HHS R01 NS035549NINDS NIH HHS R01 NS35549
6 · The paper itself

Abstract

The KCNQ1 voltage-gated potassium channel and its auxiliary subunit KCNE1 play a crucial role in the regulation of the heartbeat. The stoichiometry of KCNQ1 and KCNE1 complex has been debated, with some results suggesting that the four KCNQ1 subunits that form the channel associate with two KCNE1 subunits (a 42 stoichiometry), while others have suggested that the stoichiometry may not be fixed. We applied a single molecule fluorescence bleaching method to count subunits in many individual complexes and found that the stoichiometry of the KCNQ1 - KCNE1 complex is flexible, with up to four KCNE1 subunits associating with the four KCNQ1 subunits of the channel (a 44 stoichiometry). The proportion of the various stoichiometries was found to depend on the relative expression densities of KCNQ1 and KCNE1. Strikingly, both the voltage-dependence and kinetics of gating were found to depend on the relative densities of KCNQ1 and KCNE1, suggesting the heart rhythm may be regulated by the relative expression of the auxiliary subunit and the resulting stoichiometry of the channel complex.

Indexed as

AnimalsHumansIon Channel GatingKCNQ1 Potassium ChannelMiceMultiprotein ComplexesMyocardial ContractionMyocardiumOocytesPotassium Channels, Voltage-GatedRatsXenopus laevisKCNE1 protein, humanKcne1 protein, mouseKcne1 protein, ratKCNQ1 Potassium ChannelKCNQ1 protein, humanKcnq1 protein, mouseKcnq1 protein, ratMultiprotein ComplexesPotassium Channels, Voltage-Gated

Identifiers

PMID20962273
PMCPMC2973890
OpenAlexW2083128912

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.