Evidence map›Paper›PMID 25818916›Full record

ArticleNature communications2015

Voltage-dependent gating of KCNH potassium channels lacking a covalent link between voltage-sensing and pore domains.

Éva Lörinczi, Juan Camilo Gómez-Posada, Pilar de la Peña, Adam P Tomczak, Jorge Fernández-Trillo, Ulrike Leipscher, Walter Stühmer, Francisco Barros, Luis A Pardo

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.3field-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

65 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Molecular Determinants of Voltage-Dependent Gating in Kv11.1 Channels.Advances in experimental medicine and biology · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Voltage sensors.Molecular pharmacology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. The ERG1 KFrontiers in molecular neuroscience · 2022
    Review
  18. A second S4 movement opens hyperpolarization-activated HCN channels.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
  20. Article

5 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

9 authors at 3 institutions in 2 countries.

Éva LörincziDepartment of Molecular Biology of Neuronal Signals, Max Planck Institute of Experimental Medicine, Hermann-Rein-Straße 3, 37075 Göttingen, Germany.
Juan Camilo Gómez-PosadaDepartment of Molecular Biology of Neuronal Signals, Max Planck Institute of Experimental Medicine, Hermann-Rein-Straße 3, 37075 Göttingen, Germany.
Pilar de la PeñaDepartamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Edificio Santiago Gascón, Campus de El Cristo, 33006 Oviedo, Spain.
Adam P TomczakOncophysiology Group, Max Planck Institute of Experimental Medicine, Hermann-Rein-Straße 3, 37075 Göttingen, Germany.
Jorge Fernández-TrilloOncophysiology Group, Max Planck Institute of Experimental Medicine, Hermann-Rein-Straße 3, 37075 Göttingen, Germany.
Ulrike LeipscherOncophysiology Group, Max Planck Institute of Experimental Medicine, Hermann-Rein-Straße 3, 37075 Göttingen, Germany.
Walter StühmerDepartment of Molecular Biology of Neuronal Signals, Max Planck Institute of Experimental Medicine, Hermann-Rein-Straße 3, 37075 Göttingen, Germany.
Francisco BarrosDepartamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Edificio Santiago Gascón, Campus de El Cristo, 33006 Oviedo, Spain.
Luis A PardoOncophysiology Group, Max Planck Institute of Experimental Medicine, Hermann-Rein-Straße 3, 37075 Göttingen, Germany.ORCID http://orcid.org/0000-0003-1375-4349
Max Planck Institute of Experimental Medicine · DEUniversidad de Oviedo · ESNanoscale Microscopy and Molecular Physiology of the Brain Cluster of Excellence 171 — DFG Research Center 103 · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-gated channels open paths for ion permeation upon changes in membrane potential, but how voltage changes are coupled to gating is not entirely understood. Two modules can be recognized in voltage-gated potassium channels, one responsible for voltage sensing (transmembrane segments S1 to S4), the other for permeation (S5 and S6). It is generally assumed that the conversion of a conformational change in the voltage sensor into channel gating occurs through the intracellular S4-S5 linker that provides physical continuity between the two regions. Using the pathophysiologically relevant KCNH family, we show that truncated proteins interrupted at, or lacking the S4-S5 linker produce voltage-gated channels in a heterologous model that recapitulate both the voltage-sensing and permeation properties of the complete protein. These observations indicate that voltage sensing by the S4 segment is transduced to the channel gate in the absence of physical continuity between the modules.

Indexed as

AnimalsEther-A-Go-Go Potassium ChannelsImmunoblottingImmunoprecipitationOocytesPatch-Clamp TechniquesPotassium Channels, Voltage-GatedProtein Structure, TertiaryXenopus laevisEther-A-Go-Go Potassium ChannelsPotassium Channels, Voltage-Gated

Identifiers

PMID25818916
PMCPMC4389246
OpenAlexW2085780871

What OpenQuestion holds

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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.