Evidence map›Paper›PMID 22710124›Full record

ArticleFEBS letters2012

The first transmembrane domain (TM1) of β2-subunit binds to the transmembrane domain S1 of α-subunit in BK potassium channels.

Francisco J Morera, Abderrahmane Alioua, Pallob Kundu, Marcelo Salazar, Carlos Gonzalez, Agustin D Martinez, Enrico Stefani, Ligia Toro, Ramon Latorre

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Molecular mechanism underlying β1 regulation in voltage- and calcium-activated potassium (BK) channels.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  5. Article
  6. MaxiK channel and cell signalling.Pflugers Archiv : European journal of physiology · 2014
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
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

9 authors at 3 institutions in 2 countries.

Francisco J MoreraCentro Interdisciplinario de Neurociencia de Valparaiso, Facultad de Ciencias, Universidad de Valparaíso, Valparaiso, Chile.
Abderrahmane Alioua
Pallob Kundu
Marcelo Salazar
Carlos Gonzalez
Agustin D Martinez
Enrico Stefani
Ligia Toro
Ramon Latorre
University of California, Los Angeles · USUniversity of Valparaíso · CLAustral University of Chile · CL

Funding

Revealing Cardiovascular Stress Regulation beyond the Diffraction LimitR01HL088640 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI STEFANI, ENRICO · 2007 to 2011
$5.3M
STRUCTURAL DETERMINANTS OF K(CA) CHANNEL FUNCTIONR01HL054970 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORO DE STEFANI, LIGIA G. · 1995 to 2009
$3.2M
Novel interactions of Slo1 channel and Thromboxane A2 receptor in blood vesselsR01HL096740 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI STEFANI, ENRICO, TORO DE STEFANI, LIGIA G. · 2009 to 2010
$1.3M
NHLBI NIH HHS HL088640NHLBI NIH HHS HL096740NHLBI NIH HHS HL54970NHLBI NIH HHS R01 HL054970NHLBI NIH HHS R01 HL088640NHLBI NIH HHS R01 HL096740
6 · The paper itself

Abstract

The BK channel is one of the most broadly expressed ion channels in mammals. In many tissues, the BK channel pore-forming α-subunit is associated to an auxiliary β-subunit that modulates the voltage- and Ca(2+)-dependent activation of the channel. Structural components present in β-subunits that are important for the physical association with the α-subunit are yet unknown. Here, we show through co-immunoprecipitation that the intracellular C-terminus, the second transmembrane domain (TM2) and the extracellular loop of the β2-subunit are dispensable for association with the α-subunit pointing transmembrane domain 1 (TM1) as responsible for the interaction. Indeed, the TOXCAT assay for transmembrane protein-protein interactions demonstrated for the first time that TM1 of the β2-subunit physically binds to the transmembrane S1 domain of the α-subunit.

Indexed as

AnimalsCalciumDose-Response Relationship, DrugEpitopesExonsHEK293 CellsHumansImmunoprecipitationKineticsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsPatch-Clamp TechniquesPotassiumPotassium ChannelsProtein Structure, TertiaryTransfectionCalciumEpitopesKCNMA1 protein, humanLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsPotassiumPotassium Channels

Identifiers

PMID22710124
PMCPMC3568673
OpenAlexW2017301720

What OpenQuestion holds

Textmetadata
LicenceTDM
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.