Evidence map›Paper›PMID 27710769›Full record

ArticleeLife2016

The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel.

Juan Zhao, Rikard Blunck

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. Modular architecture of KEMBO reports · 2025
    Review
  2. Voltage sensors.Molecular pharmacology · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Mapping temperature-dependent conformational change in the voltage-sensing domain of an engineered heat-activated KProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Modulation of hERG KFrontiers in pharmacology · 2020
    Review
  13. Hysteretic Behavior in Voltage-Gated Channels.Frontiers in pharmacology · 2020
    Review
  14. The EAG Voltage-Dependent KFrontiers in pharmacology · 2020
    Review
  15. Article
  16. Review
  17. 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
  18. Article
  19. S4-S5 linker movement during activation and inactivation in voltage-gated KProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. Article
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

2 authors.

Juan ZhaoDepartment of Physics, Université de Montréal, Montréal, Canada.
Rikard BlunckDepartment of Physics, Université de Montréal, Montréal, Canada.ORCID 0000-0003-4484-2907

Funding

CIHR MOP-102689CIHR MOP-136894
6 · The paper itself

Abstract

Domains in macromolecular complexes are often considered structurally and functionally conserved while energetically coupled to each other. In the modular voltage-gated ion channels the central ion-conducting pore is surrounded by four voltage sensing domains (VSDs). Here, the energetic coupling is mediated by interactions between the S4-S5 linker, covalently linking the domains, and the proximal C-terminus. In order to characterize the intrinsic gating of the voltage sensing domain in the absence of the pore domain, the Shaker Kv channel was truncated after the fourth transmembrane helix S4 (Shaker-iVSD). Shaker-iVSD showed significantly altered gating kinetics and formed a cation-selective ion channel with a strong preference for protons. Ion conduction in Shaker-iVSD developed despite identical primary sequence, indicating an allosteric influence of the pore domain. Shaker-iVSD also displays pronounced 'relaxation'. Closing of the pore correlates with entry into relaxation suggesting that the two processes are energetically related.

Indexed as

Amino Acid MotifsAnimalsBinding SitesGene ExpressionHEK293 CellsHumansIon Channel GatingKineticsMembrane PotentialsModels, MolecularMutagenesis, Site-DirectedMutationOocytesPatch-Clamp TechniquesProtein BindingProtein Conformation, alpha-HelicalRecombinant ProteinsShaker Superfamily of Potassium ChannelsZincbiophysicsD. melanogastergatingmode-shiftpotassium channelstructural biologyvoltage-clamp fluorometryvoltage sensorxenopus

Identifiers

PMID27710769
PMCPMC5092046

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.