Evidence map›Paper›PMID 17591990›Full record

ArticleThe Journal of general physiology2007

Modes of operation of the BKCa channel beta2 subunit.

Nicoletta Savalli, Andrei Kondratiev, Sarah Buxton de Quintana, Ligia Toro, Riccardo Olcese

Open access · greenAbstract read
In one paragraph

Article in The Journal of general physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

28 citing papers in PubMed, 40 citations in OpenAlex.

  1. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  2. An epilepsy-associated KProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. Inhibition of BKCell death discovery · 2022
    Article
  4. Effect of an autism-associatedCurrent research in physiology · 2022
    Article
  5. Regulatory mechanisms of mitochondrial BKChannels (Austin, Tex.) · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Modulation of BK channel voltage gating by different auxiliary β subunits.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

5 authors at 2 institutions in 3 countries.

Nicoletta SavalliDepartment of Anesthesiology-Division of Molecular Medicine, David Geffen School of Medicine at University of California Los Angeles, Los Angeles, CA 90095, USA.
Andrei Kondratiev
Sarah Buxton de Quintana
Ligia Toro
Riccardo Olcese
Institute of Molecular Medicine · INUniversity 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
Structural Changes in BKCa Channels During GatingR01NS043240 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI OLCESE, RICCARDO · 2003 to 2006
$1.4M
NHLBI NIH HHS HL054970NHLBI NIH HHS R01 HL054970NINDS NIH HHS R01 NS043240NINDS NIH HHS R01NS043240
6 · The paper itself

Abstract

The beta(2) subunit of the large conductance Ca(2+)- and voltage-activated K(+) channel (BK(Ca)) modulates a number of channel functions, such as the apparent Ca(2+)/voltage sensitivity, pharmacological and kinetic properties of the channel. In addition, the N terminus of the beta(2) subunit acts as an inactivating particle that produces a relatively fast inactivation of the ionic conductance. Applying voltage clamp fluorometry to fluorescently labeled human BK(Ca) channels (hSlo), we have investigated the mechanisms of operation of the beta(2) subunit. We found that the leftward shift on the voltage axis of channel activation curves (G(V)) produced by coexpression with beta(2) subunits is associated with a shift in the same direction of the fluorescence vs. voltage curves (F(V)), which are reporting the voltage dependence of the main voltage-sensing region of hSlo (S4-transmembrane domain). In addition, we investigated the inactivating mechanism of the beta(2) subunits by comparing its properties with the ones of the typical N-type inactivation process of Shaker channel. While fluorescence recordings from the inactivated Shaker channels revealed the immobilization of the S4 segments in the active conformation, we did not observe a similar feature in BK(Ca) channels coexpressed with the beta(2) subunit. The experimental observations are consistent with the view that the beta(2) subunit of BK(Ca) channels facilitates channel activation by changing the voltage sensor equilibrium and that the beta(2)-induced inactivation process does not follow a typical N-type mechanism.

Indexed as

Amino Acid SequenceAnimalsCysteineElectrophysiologyHumansIon Channel GatingLarge-Conductance Calcium-Activated Potassium ChannelsOocytesPatch-Clamp TechniquesProtein SubunitsShaker Superfamily of Potassium ChannelsXenopus laevisCysteineLarge-Conductance Calcium-Activated Potassium ChannelsProtein SubunitsShaker Superfamily of Potassium Channels

Identifiers

PMID17591990
PMCPMC2154362
OpenAlexW2033689106

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.