Evidence map›Paper›PMID 19398775›Full record

ArticleThe Journal of general physiology2009

A single charged voltage sensor is capable of gating the Shaker K+ channel.

Dominique G Gagnon, Francisco Bezanilla

Abstract read
In one paragraph

Article in The Journal of general physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Correction to: Inhibition of the KPflugers Archiv : European journal of physiology · 2018
    Article
  6. Inhibition of the KPflugers Archiv : European journal of physiology · 2018
    Article
  7. Heat activation is intrinsic to the pore domain of TRPV1.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Upward movement of IS4 and IIIS4 is a rate-limiting stage in CaPflugers Archiv : European journal of physiology · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Modeling ion channels: past, present, and future.The Journal of general physiology · 2014
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Dominique G GagnonDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Francisco Bezanilla

Funding

The Electrophysiological Studies of Voltage Gated ChannelsR01GM030376 · NIGMS · UNIVERSITY OF CHICAGO · PI BEZANILLA, FRANCISCO J · 1985 to 2025
$9.1M
ELECTROPHYSIOLOGICAL STUDIES OF VOLTAGE GATED CHANNELSR37GM030376 · NIGMS · UNIVERSITY OF CHICAGO · PI BEZANILLA, FRANCISCO J · 1999 to 2008
$3.7M
NIGMS NIH HHS GM30376NIGMS NIH HHS R01 GM030376NIGMS NIH HHS R37 GM030376
6 · The paper itself

Abstract

We sought to determine the contribution of an individual voltage sensor to Shaker's function. Concatenated heterotetramers of Shaker zH4 Delta(6-46) wild type (wt) in combination with a neutral S4 segment Shaker mutant (mut) with stoichiometries 2wt/2mut and 1wt/3mut were studied and compared with the 4wt concatenated homotetramer. A single charged voltage sensor is sufficient to open Shaker conductance with reduced delay (<1 ms) and at more hyperpolarized voltages compared with 4wt. In addition, the wt-like slow inactivation of 1wt/3mut was almost completely eliminated by mutations T449V-I470C in its single wt subunit, indicating that the subunits bearing a neutral S4 were unable to trigger slow inactivation. Our results strongly suggest that a neutral S4 segment of Shaker's subunit is voltage insensitive and its voltage sensor is in the activated position (i.e., ready for pore opening), and provide experimental support to the proposed model of independent voltage sensors with a final, almost voltage-independent concerted step.

Indexed as

Ion Channel GatingAnimalsGene Transfer TechniquesKineticsMembrane PotentialsMicroinjectionsModels, BiologicalMutationOocytesPermeabilityPotassiumProtein SubunitsShaker Superfamily of Potassium ChannelsXenopusPotassiumProtein SubunitsShaker Superfamily of Potassium Channels

Identifiers

PMID19398775
PMCPMC2712970

What OpenQuestion holds

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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.