Evidence map›Paper›PMID 26802629›Full record

ArticleeLife2016

Unnatural amino acid photo-crosslinking of the IKs channel complex demonstrates a KCNE1:KCNQ1 stoichiometry of up to 4:4.

Christopher I Murray, Maartje Westhoff, Jodene Eldstrom, Emely Thompson, Robert Emes, David Fedida

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

53 citing papers in PubMed, 90 citations in OpenAlex.

  1. Chemical tuning reveals a cation-π gating bridge between the voltage-sensor and pore domains in the KProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Functional Profiling ofCirculation. Genomic and precision medicine · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Ion permeation through a narrow cavity constriction in KCNQ1 channels: Mechanism and implications for pathogenic variants.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Targeting the ICirculation research · 2024
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Mechanism of external K+ sensitivity of KCNQ1 channels.The Journal of general physiology · 2023
    Article
  19. Review
  20. Modulation of the IBBA advances · 2023
    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

6 authors at 1 institution in 1 country.

Christopher I MurrayDepartment of Anesthesiology, Pharmacology and Therapeutics, University of British Columbia, Vancouver, Canada.
Maartje WesthoffDepartment of Anesthesiology, Pharmacology and Therapeutics, University of British Columbia, Vancouver, Canada.
Jodene EldstromDepartment of Anesthesiology, Pharmacology and Therapeutics, University of British Columbia, Vancouver, Canada.
Emely ThompsonDepartment of Anesthesiology, Pharmacology and Therapeutics, University of British Columbia, Vancouver, Canada.
Robert EmesDepartment of Anesthesiology, Pharmacology and Therapeutics, University of British Columbia, Vancouver, Canada.
David FedidaDepartment of Anesthesiology, Pharmacology and Therapeutics, University of British Columbia, Vancouver, Canada.
University of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cardiac repolarization is determined in part by the slow delayed rectifier current (IKs), through the tetrameric voltage-gated ion channel, KCNQ1, and its β-subunit, KCNE1. The stoichiometry between α and β-subunits has been controversial with studies reporting either a strict 2 KCNE1:4 KCNQ1 or a variable ratio up to 4:4. We used IKs fusion proteins linking KCNE1 to one (EQ), two (EQQ) or four (EQQQQ) KCNQ1 subunits, to reproduce compulsory 4:4, 2:4 or 1:4 stoichiometries. Whole cell and single-channel recordings showed EQQ and EQQQQ to have increasingly hyperpolarized activation, reduced conductance, and shorter first latency of opening compared to EQ - all abolished by the addition of KCNE1. As well, using a UV-crosslinking unnatural amino acid in KCNE1, we found EQQQQ and EQQ crosslinking rates to be progressively slowed compared to KCNQ1, which demonstrates that no intrinsic mechanism limits the association of up to four β-subunits within the IKs complex.

Indexed as

HumansKCNQ1 Potassium ChannelPotassium Channels, Voltage-GatedProtein SubunitsKCNE1 protein, humanKCNQ1 Potassium ChannelKCNQ1 protein, humanPotassium Channels, Voltage-GatedProtein SubunitsbiochemistrybiophysicshumanKCNE1KCNQ1photo-crosslinkingsingle channelstoichiometrystructural biologyunnatrual amino acid

Identifiers

PMID26802629
PMCPMC4807126
OpenAlexW2260592789

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.