ArticleProceedings of the National Academy of Sciences of the United States of America2008
Molecular mechanism of pH sensing in KcsA potassium channels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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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.
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Who cites it
88 citing papers in PubMed, 144 citations in OpenAlex.
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- Missense mutations of GPER1 in breast invasive carcinoma: Exploring gene expression, signal transduction and immune cell infiltration with insights from cellular pharmacology.Biomedical reports · 2025Article
- The vacuolar KScience advances · 2024Article
- Cardiolipin binding enhances KcsA channel gating via both its specific and dianion-monoanion interchangeable sites.iScience · 2023Article
- Modeling control and transduction of electrochemical gradients in acid-stressed bacteria.iScience · 2023Article
- Silica/Proteoliposomal Nanocomposite as a Potential Platform for Ion Channel Studies.Molecules (Basel, Switzerland) · 2022Article
- High-Resolution Magic Angle Spinning NMR of KcsA in Liposomes: The Highly Mobile C-Terminus.Biomolecules · 2022Article
- Studying KcsA Channel Clustering Using Single Channel Voltage-Clamp Fluorescence Imaging.Frontiers in physiology · 2022Article
- Mechanisms underlying drug-mediated regulation of membrane protein function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements.International journal of molecular sciences · 2021Article
- Signature of Glycylglutamic Acid Structure.International journal of biochemistry and biophysics · 2021Article
- The leucine zipper EF-hand containing transmembrane protein-1 EF-hand is a tripartite calcium, temperature, and pH sensor.Protein science : a publication of the Protein Society · 2021Article
- NMR studies of lipid regulation of the KBiochimica et biophysica acta. Biomembranes · 2021Article
- Inferring functional units in ion channel pores via relative entropy.European biophysics journal : EBJ · 2021Article
- Selectivity filter ion binding affinity determines inactivation in a potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conformational equilibrium shift underlies altered KNature communications · 2020Article
- 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
- An acid-tolerance response system protecting exponentially growing Escherichia coli.Nature communications · 2020Article
- Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases.Nature communications · 2020Article
- The influence of membrane bilayer thickness on KcsA channel activity.Channels (Austin, Tex.) · 2019Article
28 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The bacterial potassium channel KcsA is gated by high concentrations of intracellular protons, allowing the channel to open at pH < 5.5. Despite prior attempts to determine the mechanism responsible for pH gating, the proton sensor has remained elusive. We have constructed a KcsA channel mutant that remains open up to pH 9.0 by replacing key ionizable residues from the N and C termini of KcsA with residues mimicking their protonated counterparts with respect to charge. A series of individual and combined mutations were investigated by using single-channel recordings in lipid bilayers. We propose that these residues are the proton-binding sites and at neutral pH they form a complex network of inter- and intrasubunit salt bridges and hydrogen bonds near the bundle crossing that greatly stabilize the closed state. In our model, these residues change their ionization state at acidic pH, thereby disrupting this network, modifying the electrostatic landscape near the channel gate, and favoring channel opening.
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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.