Evidence map›Paper›PMID 16446507›Full record

ArticleThe Journal of general physiology2006

Structural determinants for functional coupling between the beta and alpha subunits in the Ca2+-activated K+ (BK) channel.

Patricio Orio, Yolima Torres, Patricio Rojas, Ingrid Carvacho, Maria L Garcia, Ligia Toro, Miguel A Valverde, Ramon Latorre

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2006. 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
1.6field-weighted citation impact, top 18% 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

40 citing papers in PubMed, 59 citations in OpenAlex.

  1. Effect of an autism-associatedCurrent research in physiology · 2022
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Functional regulation of BK potassium channels by γ1 auxiliary subunits.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  17. 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

8 authors at 6 institutions in 4 countries.

Patricio OrioDepartment of Biophysics, Centro de Estudios Científicos, Valdivia, Chile.
Yolima Torres
Patricio Rojas
Ingrid Carvacho
Maria L Garcia
Ligia Toro
Miguel A Valverde
Ramon Latorre
Centro de Estudios Científicos · CLUniversity of Chile · CLAustral University of Chile · CLMerck & Co., Inc., Rahway, NJ, USA (United States) · USUniversitat Pompeu Fabra · ESUniversity of California, Los Angeles · US

Funding

STRUCTURAL DETERMINANTS OF K(CA) CHANNEL FUNCTIONR01HL054970 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORO DE STEFANI, LIGIA G. · 1995 to 2009
$3.2M
NHLBI NIH HHS HL54970NHLBI NIH HHS R01 HL054970
6 · The paper itself

Abstract

High conductance, calcium- and voltage-activated potassium (BK, MaxiK) channels are widely expressed in mammals. In some tissues, the biophysical properties of BK channels are highly affected by coexpression of regulatory (beta) subunits. The most remarkable effects of beta1 and beta2 subunits are an increase of the calcium sensitivity and the slow down of channel kinetics. However, the detailed characteristics of channels formed by alpha and beta1 or beta2 are dissimilar, the most remarkable difference being a reduction of the voltage sensitivity in the presence of beta1 but not beta2. Here we reveal the molecular regions in these beta subunits that determine their differential functional coupling with the pore-forming alpha-subunit. We made chimeric constructs between beta1 and beta2 subunits, and BK channels formed by alpha and chimeric beta subunits were expressed in Xenopus laevis oocytes. The electrophysiological characteristics of the resulting channels were determined using the patch clamp technique. Chimeric exchange of the different regions of the beta1 and beta2 subunits demonstrates that the NH3 and COOH termini are the most relevant regions in defining the behavior of either subunit. This strongly suggests that the intracellular domains are crucial for the fine tuning of the effects of these beta subunits. Moreover, the intracellular domains of beta1 are responsible for the reduction of the BK channel voltage dependence. This agrees with previous studies that suggested the intracellular regions of the alpha-subunit to be the target of the modulation by the beta1-subunit.

Indexed as

AnimalsFemaleGene ExpressionHumansLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsMembrane PotentialsMyometriumOocytesPatch-Clamp TechniquesPotassium Channels, Voltage-GatedProtein Structure, TertiaryStructure-Activity RelationshipXenopusLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsPotassium Channels, Voltage-Gated

Identifiers

PMID16446507
PMCPMC2151488
OpenAlexW2006983248

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.