ArticleJournal of molecular biology2019
Interaction of the Mechanosensitive Channel, MscS, with the Membrane Bilayer through Lipid Intercalation into Grooves and Pockets.
Article in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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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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.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- A Minimalist Model Lipid System Mimicking the Biophysical Properties ofLangmuir : the ACS journal of surfaces and colloids · 2025Article
- Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli.eLife · 2024Article
- Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli.bioRxiv : the preprint server for biology · 2024Article
- Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain.Structure (London, England : 1993) · 2024Article
- LipIDens: simulation assisted interpretation of lipid densities in cryo-EM structures of membrane proteins.Nature communications · 2023Article
- How Functional Lipids Affect the Structure and Gating of Mechanosensitive MscS-like Channels.International journal of molecular sciences · 2022Review
- Effects of Coix Seed Oil on High Fat Diet-Induced Obesity and Dyslipidemia.Foods (Basel, Switzerland) · 2022Article
- Asymmetric effects of amphipathic molecules on mechanosensitive channels.Scientific reports · 2022Article
- Cell Envelope Stress Response in Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022Article
- Molecular Paradigms for Biological Mechanosensing.The journal of physical chemistry. B · 2021Article
- Mechanosensitive channel gating by delipidation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Detergent-free systems for structural studies of membrane proteins.Biochemical Society transactions · 2021Review
- Mechanosensitive channel YnaI has lipid-bound extended sensor paddles.Communications biology · 2021Article
- Essentiality of c-di-AMP in Bacillus subtilis: Bypassing mutations converge in potassium and glutamate homeostasis.PLoS genetics · 2021Article
- Exploring the diversity of mechanosensitive channels in bacterial genomes.European biophysics journal : EBJ · 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
- Review
- In-Lipid Structure of Pressure-Sensitive Domains Hints Mechanosensitive Channel Functional Diversity.Biophysical journal · 2020Article
- Life with Bacterial Mechanosensitive Channels, from Discovery to Physiology to Pharmacological Target.Microbiology and molecular biology reviews : MMBR · 2020Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
All membrane proteins have dynamic and intimate relationships with the lipids of the bilayer that may determine their activity. Mechanosensitive channels sense tension through their interaction with the lipids of the membrane. We have proposed a mechanism for the bacterial channel of small conductance, MscS, that envisages variable occupancy of pockets in the channel by lipid chains. Here, we analyze protein-lipid interactions for MscS by quenching of tryptophan fluorescence with brominated lipids. By this strategy, we define the limits of the bilayer for TM1, which is the most lipid exposed helix of this protein. In addition, we show that residues deep in the pockets, created by the oligomeric assembly, interact with lipid chains. On the cytoplasmic side, lipids penetrate as far as the pore-lining helices and lipid molecules can align along TM3b perpendicular to lipids in the bilayer. Cardiolipin, free fatty acids, and branched lipids can access the pockets where the latter have a distinct effect on function. Cholesterol is excluded from the pockets. We demonstrate that introduction of hydrophilic residues into TM3b severely impairs channel function and that even "conservative" hydrophobic substitutions can modulate the stability of the open pore. The data provide important insights into the interactions between phospholipids and MscS and are discussed in the light of recent developments in the study of Piezo1 and TrpV4.
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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.