Evidence map›Paper›PMID 18398461›Full record

ArticlePloS one2008

S1 constrains S4 in the voltage sensor domain of Kv7.1 K+ channels.

Yoni Haitin, Ilanit Yisharel, Eti Malka, Liora Shamgar, Hella Schottelndreier, Asher Peretz, Yoav Paas, Bernard Attali

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Purification and membrane interactions of human KCNQ1Biochimica et biophysica acta. Biomembranes · 2022
    Article
  3. Chemical modulation of Kv7 potassium channels.RSC medicinal chemistry · 2021
    Review
  4. Rare CACNA1A mutations leading to congenital ataxia.Pflugers Archiv : European journal of physiology · 2020
    Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Voltage sensor ring in a native structure of a membrane-embedded potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  13. IKs channels open slowly because KCNE1 accessory subunits slow the movement of S4 voltage sensors in KCNQ1 pore-forming subunits.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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

8 authors at 2 institutions in 1 country.

Yoni HaitinDepartment of Physiology and Pharmacology, Sackler Medical School, Tel Aviv University, Tel Aviv, Israel.
Ilanit Yisharel
Eti Malka
Liora Shamgar
Hella Schottelndreier
Asher Peretz
Yoav Paas
Bernard Attali
Tel Aviv University · ILBar-Ilan University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-gated K(+) channels comprise a central pore enclosed by four voltage-sensing domains (VSDs). While movement of the S4 helix is known to couple to channel gate opening and closing, the nature of S4 motion is unclear. Here, we substituted S4 residues of Kv7.1 channels by cysteine and recorded whole-cell mutant channel currents in Xenopus oocytes using the two-electrode voltage-clamp technique. In the closed state, disulfide and metal bridges constrain residue S225 (S4) nearby C136 (S1) within the same VSD. In the open state, two neighboring I227 (S4) are constrained at proximity while residue R228 (S4) is confined close to C136 (S1) of an adjacent VSD. Structural modeling predicts that in the closed to open transition, an axial rotation (approximately 190 degrees) and outward translation of S4 (approximately 12 A) is accompanied by VSD rocking. This large sensor motion changes the intra-VSD S1-S4 interaction to an inter-VSD S1-S4 interaction. These constraints provide a ground for cooperative subunit interactions and suggest a key role of the S1 segment in steering S4 motion during Kv7.1 gating.

Indexed as

AnimalsCadmiumDisulfidesElectrophysiologyFemaleIon Channel GatingKCNQ1 Potassium ChannelModels, BiologicalModels, MolecularMutationOocytesPatch-Clamp TechniquesProtein Structure, SecondaryProtein Structure, TertiaryXenopusCadmiumDisulfidesKCNQ1 Potassium Channel

Identifiers

PMID18398461
PMCPMC2275789
OpenAlexW2042728738

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.