Evidence map›Paper›PMID 21112284›Full record

ArticleBiophysical journal2010

KCNE1 remodels the voltage sensor of Kv7.1 to modulate channel function.

Dick Wu, Hua Pan, Kelli Delaloye, Jianmin Cui

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.7field-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

33 citing papers in PubMed, 51 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
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  4. NovelFrontiers in physiology · 2024
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  5. Article
  6. Mechanistic insights into robust cardiac IbioRxiv : the preprint server for biology · 2023
    Article
  7. Modulation of the IBBA advances · 2023
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  8. Article
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  10. Modulating the voltage sensor of a cardiac potassium channel shows antiarrhythmic effects.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  11. Article
  12. Article
  13. A PIPCommunications biology · 2020
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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.

Dick WuDepartment of Biomedical Engineering, and Cardiac Bioelectricity and Arrhythmia Center, Washington University, St. Louis, Missouri, USA.
Hua Pan
Kelli Delaloye
Jianmin Cui
Washington University in St. Louis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The KCNE1 auxiliary subunit coassembles with the Kv7.1 channel and modulates its properties to generate the cardiac I(Ks) current. Recent biophysical evidence suggests that KCNE1 interacts with the voltage-sensing domain (VSD) of Kv7.1. To investigate the mechanism of how KCNE1 affects the VSD to alter the voltage dependence of channel activation, we perturbed the VSD of Kv7.1 by mutagenesis and chemical modification in the absence and presence of KCNE1. Mutagenesis of S4 in Kv7.1 indicates that basic residues in the N-terminal half (S4-N) and C-terminal half (S4-C) of S4 are important for stabilizing the resting and activated states of the channel, respectively. KCNE1 disrupts electrostatic interactions involving S4-C, specifically with the lower conserved glutamate in S2 (Glu(170) or E2). Likewise, Trp scanning of S4 shows that mutations to a cluster of residues in S4-C eliminate current in the presence of KCNE1. In addition, KCNE1 affects S4-N by enhancing MTS accessibility to the top of the VSD. Consistent with the structure of Kv channels and previous studies on the KCNE1-Kv7.1 interaction, these results suggest that KCNE1 alters the interactions of S4 residues with the surrounding protein environment, possibly by changing the protein packing around S4, thereby affecting the voltage dependence of Kv7.1.

Indexed as

Ion Channel GatingAmino AcidsAmino Acid SequenceAmino Acid SubstitutionAnimalsExtracellular SpaceKCNQ1 Potassium ChannelModels, MolecularMolecular Sequence DataMutationPotassium Channels, Voltage-GatedProtein ConformationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryStatic ElectricityAmino AcidsKCNQ1 Potassium ChannelPotassium Channels, Voltage-Gated

Identifiers

PMID21112284
PMCPMC2998620
OpenAlexW2066466524

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.