Evidence map›Paper›PMID 21464282›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Control of a final gating charge transition by a hydrophobic residue in the S2 segment of a K+ channel voltage sensor.

Jérôme J Lacroix, Francisco Bezanilla

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 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. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  13. Review
  14. Modulation of the IBBA advances · 2023
    Article
  15. Article
  16. Article
  17. Structural mechanisms for the activation of human cardiac KCNQ1 channel by electro-mechanical coupling enhancers.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Article
  20. Complex effects on CaScientific reports · 2022
    Article

3 more citing papers are in PubMed but not listed here.

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.

Jérôme J LacroixDepartment of Biochemistry and Molecular Biology, University of Chicago, Gordon Center for Integrative Sciences W244, 929 East 57th Street, 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 GM030376NIGMS NIH HHS R01 GM030376NIGMS NIH HHS R37 GM030376
6 · The paper itself

Abstract

It is now well established that the voltage-sensor domains present in voltage-gated ion channels and some phosphatases operate by transferring several charged residues (gating charges), mainly arginines located in the S4 segment, across the electric field. The conserved phenylalanine F(290) located in the S2 segment of the Shaker K channel is an aromatic residue thought to interact with all the four gating arginines carried by the S4 segment and control their transfer [Tao X, et al. (2010) Science 328:67-73]. In this paper we study the possible interaction of the gating charges with this residue by directly detecting their movement with gating current measurements in 12 F(290) mutants. Most mutations do not significantly alter the first approximately 80-90% of the gating charge transfer nor the kinetics of the gating currents during activation. The effects of the F(290) mutants are (i) the modification of a final activation transition accounting for approximately 10-20% of the total charge, similar to the effect of the ILT mutant [Ledwell JL, et al. (1999) J Gen Physiol 113:389-414] and (ii) the modification of the kinetics of the gating charge movement during deactivation. These effects are well correlated with the hydrophobicity of the substituted residue, showing that a hydrophobic residue at position 290 controls the energy barrier of the final gating transition. Our results suggest that F(290) controls the transfer of R(371), the fourth gating charge, during gating while not affecting the movement of the other three gating arginines.

Indexed as

AnimalsHumansHydrophobic and Hydrophilic InteractionsIon Channel GatingKineticsMutation, MissenseProtein Structure, SecondaryShaker Superfamily of Potassium ChannelsXenopus laevisShaker Superfamily of Potassium Channels

Identifiers

PMID21464282
PMCPMC3081032

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.