ArticleThe Journal of general physiology2010
Relative motion of transmembrane segments S0 and S4 during voltage sensor activation in the human BK(Ca) channel.
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 19 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
19 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Structural basis of voltage-dependent gating in BK channels.Nature communications · 2025Article
- A rich conformational palette underlies human CaNature communications · 2025Article
- BK Channel Gating Mechanisms: Progresses Toward a Better Understanding of Variants Linked Neurological Diseases.Frontiers in physiology · 2021Review
- The Large-Conductance, Calcium-Activated Potassium Channel: A Big Key Regulator of Cell Physiology.Frontiers in physiology · 2021Review
- Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances.Nature communications · 2018Article
- β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A specialized molecular motion opens the Hv1 voltage-gated proton channel.Nature structural & molecular biology · 2015Article
- Positions of the cytoplasmic end of BK α S0 helix relative to S1-S6 and of β1 TM1 and TM2 relative to S0-S6.The Journal of general physiology · 2015Article
- BK channels: multiple sensors, one activation gate.Frontiers in physiology · 2015Review
- Both transmembrane domains of BK β1 subunits are essential to confer the normal phenotype of β1-containing BK channels.PloS one · 2014Article
- Transduction of voltage and Ca2+ signals by Slo1 BK channels.Physiology (Bethesda, Md.) · 2013Review
- Orientations and proximities of the extracellular ends of transmembrane helices S0 and S4 in open and closed BK potassium channels.PloS one · 2013Article
- The BK channel: a vital link between cellular calcium and electrical signaling.Protein & cell · 2012Review
- 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
- Mechanism of electromechanical coupling in voltage-gated potassium channels.Frontiers in pharmacology · 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
- 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
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Large-conductance voltage- and Ca(2+)-activated K(+) (BK(Ca)) channel α subunits possess a unique transmembrane helix referred to as S0 at their N terminus, which is absent in other members of the voltage-gated channel superfamily. Recently, S0 was found to pack close to transmembrane segments S3 and S4, which are important components of the BK(Ca) voltage-sensing apparatus. To assess the role of S0 in voltage sensitivity, we optically tracked protein conformational rearrangements from its extracellular flank by site-specific labeling with an environment-sensitive fluorophore, tetramethylrhodamine maleimide (TMRM). The structural transitions resolved from the S0 region exhibited voltage dependence similar to that of charge-bearing transmembrane domains S2 and S4. The molecular determinant of the fluorescence changes was identified in W203 at the extracellular tip of S4: at hyperpolarized potential, W203 quenches the fluorescence of TMRM labeling positions at the N-terminal flank of S0. We provide evidence that upon depolarization, W203 (in S4) moves away from the extracellular region of S0, lifting its quenching effect on TMRM fluorescence. We suggest that S0 acts as a pivot component against which the voltage-sensitive S4 moves upon depolarization to facilitate channel activation.
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.