ArticleProceedings of the National Academy of Sciences of the United States of America2021
Mechanosensitive channel gating by delipidation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 51 citations in OpenAlex.
- Atomic structure and dynamics of the mechanosensitive channel MscL fromScience advances · 2026Article
- The diverse gating mechanisms of bacterial MscS-like ion channels.Biochemical Society transactions · 2026Review
- The MscS channel frombioRxiv : the preprint server for biology · 2026Article
- Article
- The bacterial mechanosensitive channel MscM gates through concerted changes in its transmembrane and cytoplasmic domains.Nature communications · 2026Article
- Diverse regulation of functional dimerization of a sugar transporter by different interfacial lipids.Nature communications · 2026Article
- Identification of MscS as a Key L-Glutamate Exporter in Bacillus methanolicus.Microbial biotechnology · 2025Article
- Mechanosensitive channel engineering: A study on the mixing and matching of YnaI and MscS sensor paddles and pores.Nature communications · 2025Article
- Lipid interactions and gating hysteresis suggest a physiological role for mechanosensitive channel YnaI.Nature communications · 2025Article
- Lipid-mediated gating of a miniature mechanosensitive MscS channel from Trypanosoma cruzi.Nature communications · 2025Article
- Capture of endogenous lipids in peptidiscs and effect on protein stability and activity.iScience · 2024Article
- 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
- MscS inactivation and recovery are slow voltage-dependent processes sensitive to interactions with lipids.Biophysical journal · 2024Article
- LipIDens: simulation assisted interpretation of lipid densities in cryo-EM structures of membrane proteins.Nature communications · 2023Article
- Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10.Nature communications · 2023Article
- The Effects of Airflow on the Mechanosensitive Channels ofMicroorganisms · 2023Article
- Mechanosensitive aquaporins.Biophysical reviews · 2023Review
- Probing the mechanical properties of ORF3a protein, a transmembrane channel of SARS-CoV-2 virus: Molecular dynamics study.Chemical physics · 2023Article
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Authors and funding
15 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanosensitive channel of small conductance (MscS) protects bacteria against hypoosmotic shock. It can sense the tension in the surrounding membrane and releases solutes if the pressure in the cell is getting too high. The membrane contacts MscS at sensor paddles, but lipids also leave the membrane and move along grooves between the paddles to reside as far as 15 Å away from the membrane in hydrophobic pockets. One sensing model suggests that a higher tension pulls lipids from the grooves back to the membrane, which triggers gating. However, it is still unclear to what degree this model accounts for sensing and what contribution the direct interaction of the membrane with the channel has. Here, we show that MscS opens when it is sufficiently delipidated by incubation with the detergent dodecyl-β-maltoside or the branched detergent lauryl maltose neopentyl glycol. After addition of detergent-solubilized lipids, it closes again. These results support the model that lipid extrusion causes gating: Lipids are slowly removed from the grooves and pockets by the incubation with detergent, which triggers opening. Addition of lipids in micelles allows lipids to migrate back into the pockets, which closes the channel even in the absence of a membrane. Based on the distribution of the aliphatic chains in the open and closed conformation, we propose that during gating, lipids leave the complex on the cytosolic leaflet at the height of highest lateral tension, while on the periplasmic side, lipids flow into gaps, which open between transmembrane helices.
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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.