Evidence map›Paper›PMID 23440279›Full record

ArticleThe Journal of general physiology2013

The voltage-sensing domain of a phosphatase gates the pore of a potassium channel.

Cristina Arrigoni, Indra Schroeder, Giulia Romani, James L Van Etten, Gerhard Thiel, Anna Moroni

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 52 citations in OpenAlex.

  1. Modular architecture of KEMBO reports · 2025
    Review
  2. Article
  3. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  4. Article
  5. CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021
    Review
  6. Review
  7. Chloroviruses.Viruses · 2019
    Review
  8. Article
  9. Review
  10. Bipolar switching by HCN voltage sensor underlies hyperpolarization activation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019
    Review
  12. Review
  13. Coupling of a viral KCommunications biology · 2019
    Article
  14. Article
  15. Review
  16. Exploring the Viral Channel KcvThe Journal of membrane biology · 2018
    Article
  17. Global versus local mechanisms of temperature sensing in ion channels.Pflugers Archiv : European journal of physiology · 2018
    Review
  18. Article
  19. Regulation of KCNQ/Kv7 family voltage-gated KBiochimica et biophysica acta. Biomembranes · 2017
    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 4 institutions in 3 countries.

Cristina ArrigoniDepartment of Biosciences, Consiglio Nazionale delle Ricerche, Università degli Studi di Milano, 20133 Milano, Italy.
Indra Schroeder
Giulia Romani
James L Van Etten
Gerhard Thiel
Anna Moroni
Technical University of Darmstadt · DEUniversity of Milan · ITNational Research Council · ITUniversity of Nebraska–Lincoln · US

Funding

VIRAL SHUTOFF OF HOST TRANSCRIPTION--PBCV-1 INFECTEDP20RR015635 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI WOOD, CHARLES · 2000 to 2009
$22.1M
NCRR NIH HHS P20 RR015635NCRR NIH HHS P20-RR15635
6 · The paper itself

Abstract

The modular architecture of voltage-gated K(+) (Kv) channels suggests that they resulted from the fusion of a voltage-sensing domain (VSD) to a pore module. Here, we show that the VSD of Ciona intestinalis phosphatase (Ci-VSP) fused to the viral channel Kcv creates Kv(Synth1), a functional voltage-gated, outwardly rectifying K(+) channel. Kv(Synth1) displays the summed features of its individual components: pore properties of Kcv (selectivity and filter gating) and voltage dependence of Ci-VSP (V(1/2) = +56 mV; z of ~1), including the depolarization-induced mode shift. The degree of outward rectification of the channel is critically dependent on the length of the linker more than on its amino acid composition. This highlights a mechanistic role of the linker in transmitting the movement of the sensor to the pore and shows that electromechanical coupling can occur without coevolution of the two domains.

Indexed as

AnimalsCiona intestinalisIon Channel GatingPermeabilityPhosphoric Monoester HydrolasesPotassium Channels, Voltage-GatedProtein Structure, TertiaryRecombinant Fusion ProteinsXenopus laevisPhosphoric Monoester HydrolasesPotassium Channels, Voltage-GatedRecombinant Fusion Proteins

Identifiers

PMID23440279
PMCPMC3581695
OpenAlexW2169753248

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.