ArticleNature communications2015
Two classes of regulatory subunits coassemble in the same BK channel and independently regulate gating.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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.
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.
Who cites it
21 citing papers in PubMed.
- 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 · 2026Article
- Competitive modulation of KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Article
- BK channels of five different subunit combinations underlie the de novo KCNMA1 G375R channelopathy.The Journal of general physiology · 2023Article
- The LRRC family of BK channel regulatory subunits: potential roles in health and disease.The Journal of physiology · 2022Review
- Comparison of KHandbook of experimental pharmacology · 2021Article
- Coronary Large Conductance CaFrontiers in physiology · 2021Review
- Article
- Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance CaAmerican journal of physiology. Lung cellular and molecular physiology · 2020Article
- LRRC52 regulates BK channel function and localization in mouse cochlear inner hair cells.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- MitoBKThe Journal of physiology · 2019Article
- Regulation of BK Channels by Beta and Gamma Subunits.Annual review of physiology · 2019Review
- Regulatory γ1 subunits defy symmetry in functional modulation of BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- One drug-sensitive subunit is sufficient for a near-maximal retigabine effect in KCNQ channels.The Journal of general physiology · 2018Article
- Article
- Activation of the Large-Conductance, Voltage, and CaFrontiers in neurology · 2018Article
- Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017Review
- The GoSlo family of BK channel activators: A no-go for γ subunits?Channels (Austin, Tex.) · 2017Article
- Tagging of Endogenous BK Channels with a Fluorogen-Activating Peptide Reveals β4-Mediated Control of Channel Clustering in Cerebellum.Frontiers in cellular neuroscience · 2017Article
- Presynaptic BK channels control transmitter release: physiological relevance and potential therapeutic implications.The Journal of physiology · 2016Review
- The single transmembrane segment determines the modulatory function of the BK channel auxiliary γ subunit.The Journal of general physiology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
High resolution proteomics increasingly reveals that most native ion channels are assembled in macromolecular complexes. However, whether different partners have additive or cooperative functional effects, or whether some combinations of proteins may preclude assembly of others are largely unexplored topics. The large conductance Ca(2+)-and-voltage activated potassium channel (BK) is well-suited to discern nuanced differences in regulation arising from combinations of subunits. Here we examine whether assembly of two different classes of regulatory proteins, β and γ, in BK channels is exclusive or independent. Our results show that both γ1 and up to four β2-subunits can coexist in the same functional BK complex, with the gating shift caused by β2-subunits largely additive with that produced by the γ1-subunit(s). The multiplicity of β:γ combinations that can participate in a BK complex therefore allow a range of BK channels with distinct functional properties tuned by the specific stoichiometry of the contributing subunits.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.