Evidence map›Paper›PMID 25360119›Full record

ReviewFrontiers in physiology2014

Regulation of BK channels by auxiliary γ subunits.

Jiyuan Zhang, Jiusheng Yan

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

49 citing papers in PubMed, 82 citations in OpenAlex.

  1. Trial
  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. Tuning the gate and the gear: The LRRC26 (bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Andrology · 2025
    Review
  6. Article
  7. Article
  8. American journal of physiology. Renal physiology · 2024
    Article
  9. Review
  10. KCurrent neuropharmacology · 2023
    Review
  11. Lysosomal Potassium Channels.Handbook of experimental pharmacology · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  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

2 authors at 1 institution in 1 country.

Jiyuan ZhangDepartment of Anesthesiology and Perioperative Medicine, University of Texas MD Anderson Cancer Center Houston, TX, USA.
Jiusheng YanDepartment of Anesthesiology and Perioperative Medicine, University of Texas MD Anderson Cancer Center Houston, TX, USA.
The University of Texas MD Anderson Cancer Center · US

Funding

BK channel regulation by auxiliary LRR proteinsR01NS078152 · NINDS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI YAN, JIUSHENG · 2012 to 2022
$3.5M
Delineation of a LRR family of BK channel auxiliary subunitsR21NS075118 · NINDS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI YAN, JIUSHENG · 2011 to 2012
$415k
NINDS NIH HHS R01 NS078152NINDS NIH HHS R21 NS075118
6 · The paper itself

Abstract

The large-conductance, calcium- and voltage-activated potassium (BK) channel has the largest single-channel conductance among potassium channels and can be activated by both membrane depolarization and increases in intracellular calcium concentration. BK channels consist of pore-forming, voltage- and calcium-sensing α subunits, either alone or in association with regulatory subunits. BK channels are widely expressed in various tissues and cells including both excitable and non-excitable cells and display diverse biophysical and pharmacological characteristics. This diversity can be explained in part by posttranslational modifications and alternative splicing of the α subunit, which is encoded by a single gene, KCNMA1, as well as by tissue-specific β subunit modulation. Recently, a leucine-rich repeat-containing membrane protein, LRRC26, was found to interact with BK channels and cause an unprecedented large negative shift (~-140 mV) in the voltage dependence of the BK channel activation. LRRC26 allows BK channels to open even at near-physiological calcium concentration and membrane voltage in non-excitable cells. Three LRRC26-related proteins, LRRC52, LRRC55, and LRRC38, were subsequently identified as BK channel modulators. These LRRC proteins are structurally and functionally distinct from the BK channel β subunits and were designated as γ subunits. The discovery of the γ subunits adds a new dimension to BK channel regulation and improves our understanding of the physiological functions of BK channels in various tissues and cell types. Unlike BK channel β subunits, which have been intensively investigated both mechanistically and physiologically, our understanding of the γ subunits is very limited at this stage. This article reviews the structure, modulatory mechanisms, physiological relevance, and potential therapeutic implications of γ subunits as they are currently understood.

Indexed as

accessory proteinauxiliary subunitBK channelsKCa1.1KCNMA1modulationregulationSlo1

Identifiers

PMID25360119
PMCPMC4197896
OpenAlexW2110707837

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.