ArticleBiophysical journal2004
Water dynamics and dewetting transitions in the small mechanosensitive channel MscS.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.
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114 citing papers in PubMed, 276 citations in OpenAlex.
- Lipid gating of BK channels and activation mechanism by negatively charged lipids.Communications chemistry · 2026Article
- The MscS channel frombioRxiv : the preprint server for biology · 2026Article
- Comparing cryo-EM methods and molecular dynamics simulation to investigate heterogeneity in ligand-bound TRPV1.Nature communications · 2025Article
- CaBMC biology · 2025Article
- Inner pore hydration free energy controls the activation of big potassium channels.Biophysical journal · 2023Article
- A novel force transduction pathway from a tension sensor to the gate in the mechano-gating of MscL channel.Frontiers in chemistry · 2023Article
- When is a hydrophobic gate not a hydrophobic gate?The Journal of general physiology · 2022Article
- Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1.Nature communications · 2022Article
- An open state of a voltage-gated sodium channel involving a π-helix and conserved pore-facing asparagine.Biophysical journal · 2022Article
- Computational methods and theory for ion channel research.Advances in physics: X · 2022Article
- Mechanosensitive channel YnaI has lipid-bound extended sensor paddles.Communications biology · 2021Article
- Molecular Simulations of Hydrophobic Gating of Pentameric Ligand Gated Ion Channels: Insights into Water and Ions.The journal of physical chemistry. B · 2021Article
- Crowding-induced opening of the mechanosensitive Piezo1 channel in silico.Communications biology · 2021Article
- A Novel Approach to Simulating the Gating Transitions of Mechanosensitive Channels.Biophysical journal · 2021Article
- The MscS-like channel YnaI has a gating mechanism based on flexible pore helices.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.Chemical reviews · 2020Review
- Hydrophobic dewetting in gating and regulation of transmembrane protein ion channels.The Journal of chemical physics · 2020Review
- Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance.Nature communications · 2020Article
- Sticky when dry.Nature chemistry · 2020Article
- The Mechanical Microenvironment in Breast Cancer.Cancers · 2020Review
54 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dynamics of confined water in capillaries and nanotubes suggests that gating of ion channels may involve not only changes of the pore geometry, but also transitions between water-filled and empty states in certain locations. The recently solved heptameric structure of the small mechanosensitive channel of Escherichia coli, MscS, has revealed a relatively wide (7-15 A) yet highly hydrophobic transmembrane pore. Continuum estimations based on the properties of pore surface suggest low conductance and a thermodynamic possibility of dewetting. To test the predictions we performed molecular dynamics simulations of MscS filled with flexible TIP3P water. Irrespective to the initial conditions, several independent 6-ns simulations converged to the same stable state with the pore water-filled in the wider part, but predominantly empty in the narrow hydrophobic part, displaying intermittent vapor-liquid transitions. The polar gain-of-function substitution L109S in the constriction resulted in a stable hydration of the entire pore. Steered passages of Cl(-) ions through the narrow part of the pore consistently produced partial ion dehydration and required a force of 200-400 pN to overcome an estimated barrier of 10-20 kcal/mole, implying negligibly low conductance. We conclude that the crystal structure of MscS does not represent an open state. We infer that MscS gate, which is similar to that of the nicotinic ACh receptor, involves a vapor-lock mechanism where limited changes of geometry or surface polarity can locally switch the regime between water-filled (conducting) and empty (nonconducting) states.
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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.