Evidence map›Paper›PMID 23542156›Full record

ArticleNature structural & molecular biology2013

Energetic role of the paddle motif in voltage gating of Shaker K(+) channels.

Yanping Xu, Yajamana Ramu, Hyeon-Gyu Shin, Jayden Yamakaze, Zhe Lu

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. 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
–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

18 citing papers in PubMed.

  1. Article
  2. 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
  3. Gating modules of the AMPA receptor pore domain revealed by unnatural amino acid mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Coarse-grained simulations of the gating current in the voltage-activated Kv1.2 channel.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Divining the design principles of voltage sensors.The Journal of general physiology · 2014
    Article
  14. Article
  15. Animal toxins influence voltage-gated sodium channel function.Handbook of experimental pharmacology · 2014
    Review
  16. Article
  17. Article
  18. The design principle of paddle motifs in voltage sensors.Nature structural & molecular biology · 2013
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Yanping XuDepartment of Physiology, Howard Hughes Medical Institute, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA.
Yajamana Ramu
Hyeon-Gyu Shin
Jayden Yamakaze
Zhe Lu

Funding

Permeation of Inward Rectifier K+ ChannelsR01GM055560 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LU, ZHE · 1997 to 2024
$8.4M
Howard Hughes Medical InstituteNIGMS NIH HHS GM55560NIGMS NIH HHS R01 GM055560
6 · The paper itself

Abstract

Voltage-gated ion channels underlie rapid electric signaling in excitable cells. Electrophysiological studies have established that the N-terminal half of the fourth transmembrane segment ((NT)S4) of these channels is the primary voltage sensor, whereas crystallographic studies have shown that (NT)S4 is not located within a proteinaceous pore. Rather, (NT)S4 and the C-terminal half of S3 ((CT)S3 or S3b) form a helix-turn-helix motif, termed the voltage-sensor paddle. This unexpected structural finding raises two fundamental questions: does the paddle motif also exist in voltage-gated channels in a biological membrane, and, if so, what is its function in voltage gating? Here, we provide evidence that the paddle motif exists in the open state of Drosophila Shaker voltage-gated K(+) channels expressed in Xenopus oocytes and that (CT)S3 acts as an extracellular hydrophobic 'stabilizer' for (NT)S4, thus biasing the gating chemical equilibrium toward the open state.

Indexed as

AnimalsCell MembraneDrosophila ProteinsGene ExpressionOocytesRecombinant ProteinsShaker Superfamily of Potassium ChannelsXenopusDrosophila ProteinsRecombinant ProteinsShaker Superfamily of Potassium ChannelsSh protein, Drosophila

Identifiers

PMID23542156
PMCPMC3777420

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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.