ArticleBiophysical journal2011
Role of the KcsA channel cytoplasmic domain in pH-dependent gating.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Article
- Review
- Development of an automated system to measure ion channel currents using a surface-modified gold probe.Scientific reports · 2021Article
- Molecular Mechanisms for Bacterial Potassium Homeostasis.Journal of molecular biology · 2021Review
- Tetraoctylammonium, a Long Chain Quaternary Ammonium Blocker, Promotes a Noncollapsed, Resting-Like Inactivated State in KcsA.International journal of molecular sciences · 2021Article
- A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings.Micromachines · 2020Article
- pH-Dependent Conformational Changes of KcsA Tetramer and Monomer Probed by Raman Spectroscopy.International journal of molecular sciences · 2019Article
- Accessibility of Cations to the Selectivity Filter of KcsA in the Inactivated State: An Equilibrium Binding Study.International journal of molecular sciences · 2019Article
- Reconstitution and functional characterization of ion channels from nanodiscs in lipid bilayers.The Journal of general physiology · 2018Article
- Selective exclusion and selective binding both contribute to ion selectivity in KcsA, a model potassium channel.The Journal of biological chemistry · 2017Article
- 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
- Molecular interactions involved in proton-dependent gating in KcsA potassium channels.The Journal of general physiology · 2013Article
- Lipid bilayer composition can influence the orientation of proteorhodopsin in artificial membranes.Biophysical journal · 2013Article
- Targeted molecular dynamics (TMD) of the full-length KcsA potassium channel: on the role of the cytoplasmic domain in the opening process.Journal of molecular modeling · 2013Article
- Automated parallel recordings of topologically identified single ion channels.Scientific reports · 2013Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The KcsA channel is a representative potassium channel that is activated by changes in pH. Previous studies suggested that the region that senses pH is entirely within its transmembrane segments. However, we recently revealed that the cytoplasmic domain also has an important role, because its conformation was observed to change dramatically in response to pH changes. Here, to investigate the effects of the cytoplasmic domain on pH-dependent gating, we made a chimera mutant channel consisting of the cytoplasmic domain of the KcsA channel and the transmembrane region of the MthK channel. The chimera showed a pH dependency similar to that of KcsA, indicating that the cytoplasmic domain can act as a pH sensor. To identify how this region detects pH, we substituted certain cytoplasmic domain amino acids that are normally negatively charged at pH 7 for neutral ones in the KcsA channels. These mutants opened independently of pH, suggesting that electrostatic charges have a major role in the cytoplasmic domain's ability to sense and respond to pH.
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