Evidence map›Paper›PMID 27278891›Full record

ArticleScientific reports2016

Reciprocal voltage sensor-to-pore coupling leads to potassium channel C-type inactivation.

Luca Conti, Jakob Renhorn, Anders Gabrielsson, Fredrik Turesson, Sara I Liin, Erik Lindahl, Fredrik Elinder

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-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

14 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
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  7. Tracking the motion of the KThe Journal of physiology · 2020
    Article
  8. Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Hysteresis in voltage-gated channels.Channels (Austin, Tex.) · 2017
    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

7 authors at 3 institutions in 1 country.

Luca ContiDepartment of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
Jakob RenhornDepartment of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
Anders GabrielssonTheoretical and Computational Biophysics, Department of Theoretical Physics, KTH Royal Institute of Technology, Stockholm, Sweden.
Fredrik TuressonDepartment of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
Sara I LiinDepartment of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
Erik LindahlTheoretical and Computational Biophysics, Department of Theoretical Physics, KTH Royal Institute of Technology, Stockholm, Sweden.
Fredrik ElinderDepartment of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
Linköping University · SEKTH Royal Institute of Technology · SEStockholm University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-gated potassium channels open at depolarized membrane voltages. A prolonged depolarization causes a rearrangement of the selectivity filter which terminates the conduction of ions - a process called slow or C-type inactivation. How structural rearrangements in the voltage-sensor domain (VSD) cause alteration in the selectivity filter, and vice versa, are not fully understood. We show that pulling the pore domain of the Shaker potassium channel towards the VSD by a Cd(2+) bridge accelerates C-type inactivation. Molecular dynamics simulations show that such pulling widens the selectivity filter and disrupts the K(+) coordination, a hallmark for C-type inactivation. An engineered Cd(2+) bridge within the VSD also affect C-type inactivation. Conversely, a pore domain mutation affects VSD gating-charge movement. Finally, C-type inactivation is caused by the concerted action of distant amino acid residues in the pore domain. All together, these data suggest a reciprocal communication between the pore domain and the VSD in the extracellular portion of the channel.

Indexed as

Ion Channel GatingAnimalsCadmiumGene DeletionMembrane PotentialsMolecular Dynamics SimulationMutationPotassiumProtein DomainsShaker Superfamily of Potassium ChannelsStatic ElectricityXenopus laevisCadmiumPotassiumShaker Superfamily of Potassium Channels

Identifiers

PMID27278891
PMCPMC4899724
OpenAlexW2414439838

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.