ArticleThe Journal of general physiology2010
The RCK1 domain of the human BKCa channel transduces Ca2+ binding into structural rearrangements.
Article in The Journal of general physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed.
- Cytochrome C-like Domain Within the Human BK Channel.International journal of molecular sciences · 2025Article
- Regulatory mechanisms of mitochondrial BKChannels (Austin, Tex.) · 2021Review
- Physiological Roles and Therapeutic Potential of CaFrontiers in molecular neuroscience · 2018Review
- A genetic variant of the sperm-specific SLO3 KThe Journal of biological chemistry · 2017Article
- Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017Review
- Molecular Mechanisms Underlying Renin-Angiotensin-Aldosterone System Mediated Regulation of BK Channels.Frontiers in physiology · 2017Review
- Modeling a Ca(2+) channel/BKCa channel complex at the single-complex level.Biophysical journal · 2014Article
- The smooth muscle-type β1 subunit potentiates activation by DiBAC4(3) in recombinant BK channels.Channels (Austin, Tex.) · 2014Article
- Transduction of voltage and Ca2+ signals by Slo1 BK channels.Physiology (Bethesda, Md.) · 2013Review
- Free-energy relationships in ion channels activated by voltage and ligand.The Journal of general physiology · 2013Article
- Relative transmembrane segment rearrangements during BK channel activation resolved by structurally assigned fluorophore-quencher pairing.The Journal of general physiology · 2012Article
- The contribution of RCK domains to human BK channel allosteric activation.The Journal of biological chemistry · 2012Article
- Metal-driven operation of the human large-conductance voltage- and Ca2+-dependent potassium channel (BK) gating ring apparatus.The Journal of biological chemistry · 2011Article
- Relative motion of transmembrane segments S0 and S4 during voltage sensor activation in the human BK(Ca) channel.The Journal of general physiology · 2010Article
- SLO-2 isoforms with unique Ca(2+) - and voltage-dependence characteristics confer sensitivity to hypoxia in C. elegans.Channels (Austin, Tex.)Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Large-conductance voltage- and Ca(2+)-activated K(+) (BK(Ca)) channels play a fundamental role in cellular function by integrating information from their voltage and Ca(2+) sensors to control membrane potential and Ca(2+) homeostasis. The molecular mechanism of Ca(2+)-dependent regulation of BK(Ca) channels is unknown, but likely relies on the operation of two cytosolic domains, regulator of K(+) conductance (RCK)1 and RCK2. Using solution-based investigations, we demonstrate that the purified BK(Ca) RCK1 domain adopts an alpha/beta fold, binds Ca(2+), and assembles into an octameric superstructure similar to prokaryotic RCK domains. Results from steady-state and time-resolved spectroscopy reveal Ca(2+)-induced conformational changes in physiologically relevant [Ca(2+)]. The neutralization of residues known to be involved in high-affinity Ca(2+) sensing (D362 and D367) prevented Ca(2+)-induced structural transitions in RCK1 but did not abolish Ca(2+) binding. We provide evidence that the RCK1 domain is a high-affinity Ca(2+) sensor that transduces Ca(2+) binding into structural rearrangements, likely representing elementary steps in the Ca(2+)-dependent activation of human BK(Ca) channels.
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.