Evidence map›Paper›PMID 22547800›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

BK potassium channel modulation by leucine-rich repeat-containing proteins.

Jiusheng Yan, Richard W Aldrich

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
145citing papers in PubMed, 1 pooled it
–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

145 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  5. Article
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  7. 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
  8. Article
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  11. Neuronal plasticity at puberty in mouse hypothalamicProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Article
  14. Tuning the gate and the gear: The LRRC26 (bioRxiv : the preprint server for biology · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. The mechanism of CaThe Journal of biological chemistry · 2025
    Article
  20. Review

85 more citing papers are in PubMed but not listed here.

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.

Jiusheng YanSection of Neurobiology, Center for Learning and Memory, University of Texas, Austin, TX 78712, USA. jshyan@mail.utexas.edu
Richard W Aldrich

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 NS075118NINDS NIH HHS R01 NS078152NINDS NIH HHS R21 NS075118
6 · The paper itself

Abstract

Molecular diversity of ion channel structure and function underlies variability in electrical signaling in nerve, muscle, and nonexcitable cells. Regulation by variable auxiliary subunits is a major mechanism to generate tissue- or cell-specific diversity of ion channel function. Mammalian large-conductance, voltage- and calcium-activated potassium channels (BK, K(Ca)1.1) are ubiquitously expressed with diverse functions in different tissues or cell types, consisting of the pore-forming, voltage- and Ca(2+)-sensing α-subunits (BKα), either alone or together with the tissue-specific auxiliary β-subunits (β1-β4). We recently identified a leucine-rich repeat (LRR)-containing membrane protein, LRRC26, as a BK channel auxiliary subunit, which causes an unprecedented large negative shift (∼140 mV) in voltage dependence of channel activation. Here we report a group of LRRC26 paralogous proteins, LRRC52, LRRC55, and LRRC38 that potentially function as LRRC26-type auxiliary subunits of BK channels. LRRC52, LRRC55, and LRRC38 produce a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction by ∼100 mV, 50 mV, and 20 mV, respectively, in the absence of calcium. They along with LRRC26 show distinct expression in different human tissues: LRRC26 and LRRC38 mainly in secretory glands, LRRC52 in testis, and LRRC55 in brain. LRRC26 and its paralogs are structurally and functionally distinct from the β-subunits and we designate them as a γ family of the BK channel auxiliary proteins, which potentially regulate the channel's gating properties over a spectrum of different tissues or cell types.

Indexed as

Models, MolecularBrainDNA PrimersHEK293 CellsHumansIon Channel GatingLarge-Conductance Calcium-Activated Potassium ChannelsMaleMembrane ProteinsNeoplasm ProteinsPatch-Clamp TechniquesReal-Time Polymerase Chain ReactionTestisDNA PrimersLarge-Conductance Calcium-Activated Potassium ChannelsLRRC26 protein, humanLRRC38 protein, humanLRRC52 protein, humanLRRC55 protein, humanMembrane ProteinsNeoplasm Proteins

Identifiers

PMID22547800
PMCPMC3356614

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.