Evidence map›Paper›PMID 24639523›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Functional regulation of BK potassium channels by γ1 auxiliary subunits.

Vivian Gonzalez-Perez, Xiao-Ming Xia, Christopher J Lingle

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Tuning the gate and the gear: The LRRC26 (γ1) subunit modulates intrinsic gating and voltage-sensor coupling of the BK channel.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Tuning the gate and the gear: The LRRC26 (bioRxiv : the preprint server for biology · 2025
    Article
  5. Review
  6. SLO3: A Conserved Regulator of Sperm Membrane Potential.International journal of molecular sciences · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. Vascular mechanotransduction.Physiological reviews · 2023
    Review
  11. Review
  12. Article
  13. Review
  14. Regulatory mechanisms of mitochondrial BKChannels (Austin, Tex.) · 2021
    Review
  15. Goblet cell LRRC26 regulates BK channel activation and protects against colitis in mice.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. Comparison of KHandbook of experimental pharmacology · 2021
    Article
  18. Review
  19. Review
  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

3 authors.

Vivian Gonzalez-PerezDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110.
Xiao-Ming Xia
Christopher J Lingle

Funding

AUXILIARY SUBUNITS OF CA2+ ACTIVATED K+ CHANNELSR01GM081748 · NIGMS · WASHINGTON UNIVERSITY · PI LINGLE, CHRISTOPHER J · 2008 to 2015
$3.2M
Functional consequences of heteromeric assembly of auxiliary subunits in BK channF32GM103138 · NIGMS · WASHINGTON UNIVERSITY · PI GONZALEZ-PEREZ, VIVIAN MARIA · 2012 to 2012
$52k
NIGMS NIH HHS F32 GM103138NIGMS NIH HHS GM-081748NIGMS NIH HHS GM103138NIGMS NIH HHS R01 GM081748
6 · The paper itself

Abstract

Many K(+) channels are oligomeric complexes with intrinsic structural symmetry arising from the homo-tetrameric core of their pore-forming subunits. Allosteric regulation of tetramerically symmetric proteins, whether by intrinsic sensing domains or associated auxiliary subunits, often mirrors the fourfold structural symmetry. Here, through patch-clamp recordings of channel population ensembles and also single channels, we examine regulation of the Ca(2+)- and voltage-activated large conductance Ca(2+)-activated K(+) (BK) channel by associated γ1-subunits. Through expression of differing ratios of γ1:α-subunits, the results reveal an all-or-none functional regulation of BK channels by γ-subunits: channels either exhibit a full gating shift or no shift at all. Furthermore, the γ1-induced shift exhibits a state-dependent labile behavior that recapitulates the fully shifted or unshifted behavior. The γ1-induced shift contrasts markedly to the incremental shifts in BK gating produced by 1-4 β-subunits and adds a new layer of complexity to the mechanisms by which BK channel functional diversity is generated.

Indexed as

Allosteric RegulationAnimalsHumansIon Channel GatingMiceModels, BiologicalNeoplasm ProteinsProtein SubunitsTime FactorsXenopus laevisLRRC26 protein, humanNeoplasm ProteinsProtein SubunitsallosteryasymmetrySlo1 channels

Identifiers

PMID24639523
PMCPMC3977294

What OpenQuestion holds

Textmetadata
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.