Evidence map›Paper›PMID 19029374›Full record

ArticleThe Journal of general physiology2008

Kv channel gating requires a compatible S4-S5 linker and bottom part of S6, constrained by non-interacting residues.

Alain J Labro, Adam L Raes, Alessandro Grottesi, Diane Van Hoorick, Mark S P Sansom, Dirk J Snyders

Abstract read
In one paragraph

Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed.

  1. Article
  2. Review
  3. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  4. Article
  5. Article
  6. Electromechanical coupling of the Kv1.1 voltage-gated KPflugers Archiv : European journal of physiology · 2020
    Article
  7. The EAG Voltage-Dependent KFrontiers in pharmacology · 2020
    Review
  8. Review
  9. Review
  10. Article
  11. 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
  12. Article
  13. A new mechanism of voltage-dependent gating exposed by KThe Journal of general physiology · 2017
    Article
  14. Small molecule modulation of voltage gated sodium channels.Current opinion in structural biology · 2017
    Review
  15. Regulation of KCNQ/Kv7 family voltage-gated KBiochimica et biophysica acta. Biomembranes · 2017
    Review
  16. Article
  17. Article
  18. Article
  19. 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

6 authors.

Alain J LabroLaboratory for Molecular Biophysics, Physiology, and Pharmacology, Department of Biomedical Sciences, University of Antwerp, 2610 Antwerp, Belgium.
Adam L Raes
Alessandro Grottesi
Diane Van Hoorick
Mark S P Sansom
Dirk J Snyders

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-dependent K(+) channels transfer the voltage sensor movement into gate opening or closure through an electromechanical coupling. To test functionally whether an interaction between the S4-S5 linker (L45) and the cytoplasmic end of S6 (S6(T)) constitutes this coupling, the L45 in hKv1.5 was replaced by corresponding hKv2.1 sequence. This exchange was not tolerated but could be rescued by also swapping S6(T). Exchanging both L45 and S6(T) transferred hKv2.1 kinetics to an hKv1.5 background while preserving the voltage dependence. A one-by-one residue substitution scan of L45 and S6(T) in hKv1.5 further shows that S6(T) needs to be alpha-helical and forms a "crevice" in which residues I422 and T426 of L45 reside. These residues transfer the mechanical energy onto the S6(T) crevice, whereas other residues in S6(T) and L45 that are not involved in the interaction maintain the correct structure of the coupling.

Indexed as

Ion Channel GatingAmino Acid SequenceAmino Acid SubstitutionEnergy TransferHumansKineticsMembrane PotentialsMutagenesis, Site-DirectedPotassium Channels, Voltage-GatedProtein Interaction Domains and MotifsProtein Structure, SecondaryStructure-Activity RelationshipPotassium Channels, Voltage-Gated

Identifiers

PMID19029374
PMCPMC2585865

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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.