Evidence map›Paper›PMID 12324418›Full record

ArticleBiophysical journal2002

KCNE5 induces time- and voltage-dependent modulation of the KCNQ1 current.

Kamilla Angelo, Thomas Jespersen, Morten Grunnet, Morten Schak Nielsen, Dan A Klaerke, Søren-Peter Olesen

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

52 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Kv7 Channels and Excitability Disorders.Handbook of experimental pharmacology · 2021
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. KCNE1 and KCNE3 modulate KCNQ1 channels by affecting different gating transitions.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Review
  18. KCNE3 acts by promoting voltage sensor activation in KCNQ1.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Review
  20. 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

6 authors at 1 institution in 1 country.

Kamilla AngeloDepartment of Medical Physiology, University of Copenhagen, The Panum Institute, Denmark. angelo@mfi.ku.dk
Thomas Jespersen
Morten Grunnet
Morten Schak Nielsen
Dan A Klaerke
Søren-Peter Olesen
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The function of the KCNE5 (KCNE1-like) protein has not previously been described. Here we show that KCNE5 induces both a time- and voltage-dependent modulation of the KCNQ1 current. Interaction of the KCNQ1 channel with KCNE5 shifted the voltage activation curve of KCNQ1 by more than 140 mV in the positive direction. The activation threshold of the KCNQ1+KCNE5 complex was +40 mV and the midpoint of activation was +116 mV. The KCNQ1+KCNE5 current activated slowly and deactivated rapidly as compared to the KCNQ1+KCNE1 at 22 degrees C; however, at physiological temperature, the activation time constant of the KCNQ1+KCNE5 current decreased fivefold, thus exceeding the activation rate of the KCNQ1+KCNE1 current. The KCNE5 subunit is specific for the KCNQ1 channel, as none of other members of the KCNQ-family or the human ether a-go-go related channel (hERG1) was affected by KCNE5. Four residues in the transmembrane domain of the KCNE5 protein were found to be important for the control of the voltage-dependent activation of the KCNQ1 current. We speculate that since KCNE5 is expressed in cardiac tissue it may here along with the KCNE1 beta-subunit regulate KCNQ1 channels. It is possible that KCNE5 shapes the I(Ks) current in certain parts of the mammalian heart.

Indexed as

Potassium Channels, Voltage-GatedAction PotentialsAmino Acid SequenceAnimalsBiophysical PhenomenaBiophysicsCHO CellsCricetinaeElectrophysiologyIonsKCNQ1 Potassium ChannelKCNQ Potassium ChannelsKineticsMolecular Sequence DataPotassium ChannelsProtein Structure, TertiaryIonsKCNQ1 Potassium ChannelKCNQ Potassium Channelspotassium channel protein I(sk)Potassium ChannelsPotassium Channels, Voltage-Gated

Identifiers

PMID12324418
PMCPMC1302289
OpenAlexW2024647359

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.