Evidence map›Paper›PMID 25779871›Full record

ArticleThe Journal of general physiology2015

Voltage-dependent gating and gating charge measurements in the Kv1.2 potassium channel.

Itzel G Ishida, Gisela E Rangel-Yescas, Julia Carrasco-Zanini, León D Islas

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Voltage sensors.Molecular pharmacology · 2025
    Review
  3. Article
  4. Review
  5. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  6. Article
  7. Article
  8. An epilepsy-associated KProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Article
  11. Comparison of KHandbook of experimental pharmacology · 2021
    Article
  12. Tracking the motion of the KThe Journal of physiology · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Opening TRPP2 (Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

4 authors at 1 institution in 1 country.

Itzel G IshidaDepartamento de Fisiología, Facultad de Medicina, Universidad Nacional Autónoma de México, Distrito Federal 04510, México.
Gisela E Rangel-YescasDepartamento de Fisiología, Facultad de Medicina, Universidad Nacional Autónoma de México, Distrito Federal 04510, México.
Julia Carrasco-ZaniniDepartamento de Fisiología, Facultad de Medicina, Universidad Nacional Autónoma de México, Distrito Federal 04510, México.
León D IslasDepartamento de Fisiología, Facultad de Medicina, Universidad Nacional Autónoma de México, Distrito Federal 04510, México leon.islas@gmail.com.
Universidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Much has been learned about the voltage sensors of ion channels since the x-ray structure of the mammalian voltage-gated potassium channel Kv1.2 was published in 2005. High resolution structural data of a Kv channel enabled the structural interpretation of numerous electrophysiological findings collected in various ion channels, most notably Shaker, and permitted the development of meticulous computational simulations of the activation mechanism. The fundamental premise for the structural interpretation of functional measurements from Shaker is that this channel and Kv1.2 have the same characteristics, such that correlation of data from both channels would be a trivial task. We tested these assumptions by measuring Kv1.2 voltage-dependent gating and charge per channel. We found that the Kv1.2 gating charge is near 10 elementary charges (eo), ∼25% less than the well-established 13-14 eo in Shaker. Next, we neutralized positive residues in the Kv1.2 S4 transmembrane segment to investigate the cause of the reduction of the gating charge and found that, whereas replacing R1 with glutamine decreased voltage sensitivity to ∼50% of the wild-type channel value, mutation of the subsequent arginines had a much smaller effect. These data are in marked contrast to the effects of charge neutralization in Shaker, where removal of the first four basic residues reduces the gating charge by roughly the same amount. In light of these differences, we propose that the voltage-sensing domains (VSDs) of Kv1.2 and Shaker might undergo the same physical movement, but the septum that separates the aqueous crevices in the VSD of Kv1.2 might be thicker than Shaker's, accounting for the smaller Kv1.2 gating charge.

Indexed as

Ion Channel GatingAmino Acid SequenceAnimalsKv1.2 Potassium ChannelMembrane PotentialsMolecular Sequence DataStatic ElectricityXenopusKv1.2 Potassium Channel

Identifiers

PMID25779871
PMCPMC4380214
OpenAlexW2033080277

What OpenQuestion holds

Textmetadata
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.