ArticleFEBS letters2010
A molecular mechanism for proton-dependent gating in KcsA.
Article in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed.
- Article
- Structural motifs for subtype-specific pH-sensitive gating of vertebrate otopetrin proton channels.eLife · 2022Article
- Structures of Gating Intermediates in a KJournal of molecular biology · 2021Article
- NMR studies of lipid regulation of the KBiochimica et biophysica acta. Biomembranes · 2021Article
- Tetraoctylammonium, a Long Chain Quaternary Ammonium Blocker, Promotes a Noncollapsed, Resting-Like Inactivated State in KcsA.International journal of molecular sciences · 2021Article
- Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structure, function, and ion-binding properties of a KProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Accessibility of Cations to the Selectivity Filter of KcsA in the Inactivated State: An Equilibrium Binding Study.International journal of molecular sciences · 2019Article
- Selective exclusion and selective binding both contribute to ion selectivity in KcsA, a model potassium channel.The Journal of biological chemistry · 2017Article
- Activation of the mechanosensitive ion channel MscL by mechanical stimulation of supported Droplet-Hydrogel bilayers.Scientific reports · 2017Article
- Efficient implementation of constant pH molecular dynamics on modern graphics processors.Journal of computational chemistry · 2016Article
- Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.The Journal of general physiology · 2016Article
- Channel function reconstitution and re-animation: a single-channel strategy in the postcrystal age.The Journal of physiology · 2015Review
- The Hydrophobic Effect Contributes to the Closed State of a Simplified Ion Channel through a Conserved Hydrophobic Patch at the Pore-Helix Crossing.Frontiers in pharmacology · 2015Article
- Molecular determinants of tetramerization in the KcsA cytoplasmic domain.Protein science : a publication of the Protein Society · 2014Article
- Conformational dynamics at the inner gate of KcsA during activation.Biochemistry · 2014Article
- A KcsA/MloK1 chimeric ion channel has lipid-dependent ligand-binding energetics.The Journal of biological chemistry · 2014Article
- Regulation of ion channel function by the host lipid bilayer examined by a stopped-flow spectrofluorometric assay.Biophysical journal · 2014Article
- Transmembrane allosteric coupling of the gates in a potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Molecular interactions involved in proton-dependent gating in KcsA potassium channels.The Journal of general physiology · 2013Article
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
Activation gating in KcsA is elicited by changes in intracellular proton concentration. Thompson et al. identified a charge cluster around the inner gate that plays a key role in defining proton activation in KcsA. Here, through functional and spectroscopic approaches, we confirmed the role of this charge cluster and now provide a mechanism of pH-dependent gating. Channel opening is driven by a set of electrostatic interactions that include R117, E120 and E118 at the bottom of TM2 and H25 at the end of TM1. We propose that electrostatic compensation in this charge cluster stabilizes the closed conformation at neutral pH and that its disruption at low pH facilitates the transition to the open conformation by means of helix-helix repulsion.
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.