Evidence map›Paper›PMID 15623895›Full record

ArticleThe Journal of general physiology2005

The cooperative voltage sensor motion that gates a potassium channel.

Medha Pathak, Lisa Kurtz, Francesco Tombola, Ehud Isacoff

Abstract read
In one paragraph

Article in The Journal of general physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing 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

84 citing papers in PubMed.

  1. MultimodalCirculation · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. The tarantula toxin GxTx detains KThe Journal of general physiology · 2019
    Article
  9. Article
  10. Review
  11. Calcium channel gating.Pflugers Archiv : European journal of physiology · 2018
    Review
  12. 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
  13. Deglycosylation of Shaker KThe Journal of general physiology · 2018
    Article
  14. Article
  15. KCNE1 and KCNE3 modulate KCNQ1 channels by affecting different gating transitions.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

24 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

4 authors.

Medha PathakBiophysics Graduate Group, University of California, Berkeley, Berkeley, CA 94720, USA.
Lisa Kurtz
Francesco Tombola
Ehud Isacoff

Funding

STRUCTURAL REARRANGEMENTS IN CHANNEL GATINGR01NS035549 · NINDS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ISACOFF, EHUD · 1996 to 2013
$4.1M
NINDS NIH HHS R01 NS035549
6 · The paper itself

Abstract

The four arginine-rich S4 helices of a voltage-gated channel move outward through the membrane in response to depolarization, opening and closing gates to generate a transient ionic current. Coupling of voltage sensing to gating was originally thought to operate with the S4s moving independently from an inward/resting to an outward/activated conformation, so that when all four S4s are activated, the gates are driven to open or closed. However, S4 has also been found to influence the cooperative opening step (Smith-Maxwell et al., 1998a), suggesting a more complex mechanism of coupling. Using fluorescence to monitor structural rearrangements in a Shaker channel mutant, the ILT channel (Ledwell and Aldrich, 1999), that energetically isolates the steps of activation from the cooperative opening step, we find that opening is accompanied by a previously unknown and cooperative movement of S4. This gating motion of S4 appears to be coupled to the internal S6 gate and to two forms of slow inactivation. Our results suggest that S4 plays a direct role in gating. While large transmembrane rearrangements of S4 may be required to unlock the gating machinery, as proposed before, it appears to be the gating motion of S4 that drives the gates to open and close.

Indexed as

AnimalsCells, CulturedIon Channel GatingKineticsMembrane PotentialsMotionOocytesPotassium ChannelsProtein ConformationRecombinant ProteinsShaker Superfamily of Potassium ChannelsStructure-Activity RelationshipXenopus laevisPotassium ChannelsRecombinant ProteinsShaker Superfamily of Potassium Channels

Identifiers

PMID15623895
PMCPMC1414780

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.