ArticleBiophysical journal2008
Subunit-specific effect of the voltage sensor domain on Ca2+ sensitivity of BK channels.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 26 citations in OpenAlex.
- Incorporating physics to overcome data scarcity in predictive modeling of protein function: A case study of BK channels.PLoS computational biology · 2023Article
- Incorporating physics to overcome data scarcity in predictive modeling of protein function: a case study of BK channels.bioRxiv : the preprint server for biology · 2023Article
- Calcium-Activated KHandbook of experimental pharmacology · 2021Article
- Article
- Modulation of BK Channel Function by Auxiliary Beta and Gamma Subunits.International review of neurobiology · 2016Review
- N-terminal isoforms of the large-conductance Ca²⁺-activated K⁺ channel are differentially modulated by the auxiliary β1-subunit.The Journal of biological chemistry · 2014Article
- Functional insights into modulation of BKCa channel activity to alter myometrial contractility.Frontiers in physiology · 2014Review
- The interface between membrane-spanning and cytosolic domains in Ca²+-dependent K+ channels is involved in β subunit modulation of gating.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Transduction of voltage and Ca2+ signals by Slo1 BK channels.Physiology (Bethesda, Md.) · 2013Review
- Involvement of large conductance Ca(2+)-activated K (+) channel in laminar shear stress-induced inhibition of vascular smooth muscle cell proliferation.Pflugers Archiv : European journal of physiology · 2013Article
- Modulation of BK channel voltage gating by different auxiliary β subunits.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- An extracellular domain of the accessory β1 subunit is required for modulating BK channel voltage sensor and gate.The Journal of general physiology · 2012Article
- Regulation of Voltage-Activated K(+) Channel Gating by Transmembrane β Subunits.Frontiers in pharmacology · 2012Article
- BK-type calcium-activated potassium channels: coupling of metal ions and voltage sensing.The Journal of physiology · 2010Review
- KCNE1 remodels the voltage sensor of Kv7.1 to modulate channel function.Biophysical journal · 2010Article
- Modulation of BK channel gating by the ß2 subunit involves both membrane-spanning and cytoplasmic domains of Slo1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Allosteric interactions and the modular nature of the voltage- and Ca2+-activated (BK) channel.The Journal of physiology · 2010Review
- {beta} subunit-specific modulations of BK channel function by a mutation associated with epilepsy and dyskinesia.The Journal of physiology · 2009Article
- Measuring the influence of the BKCa {beta}1 subunit on Ca2+ binding to the BKCa channel.The Journal of general physiology · 2009Article
- A BK (Slo1) channel journey from molecule to physiology.Channels (Austin, Tex.)Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Large conductance Ca(2+)- and voltage-activated K(+) (BK) channels, composed of pore-forming alpha-subunits and auxiliary beta-subunits, play important roles in diverse physiological processes. The differences in BK channel phenotypes are primarily due to the tissue-specific expression of beta-subunits (beta1-beta4) that modulate channel function differently. Yet, the molecular basis of the subunit-specific regulation is not clear. In our study, we demonstrate that perturbation of the voltage sensor in BK channels by mutations selectively disrupts the ability of the beta1-subunit--but not that of the beta2-subunit--to enhance apparent Ca(2+) sensitivity. These mutations change the number of equivalent gating charges, the voltage dependence of voltage sensor movements, the open-close equilibrium of the channel, and the allosteric coupling between voltage sensor movements and channel opening to various degrees, indicating that they alter the conformation and movements of the voltage sensor and the activation gate. Similarly, the ability of the beta1-subunit to enhance apparent Ca(2+) sensitivity is diminished to various degrees, correlating quantitatively with the shift of voltage dependence of voltage sensor movements. In contrast, none of these mutations significantly reduces the ability of the beta2-subunit to enhance Ca(2+) sensitivity. These results suggest that the beta1-subunit enhances Ca(2+) sensitivity by altering the conformation and movements of the voltage sensor, whereas the similar function of the beta2-subunit is governed by a distinct mechanism.
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.