ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2011
An in vivo screen reveals protein-lipid interactions crucial for gating a mechanosensitive channel.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Atomic structure and dynamics of the mechanosensitive channel MscL fromScience advances · 2026Article
- Mechanosensitive channel MscL gating transitions coupling with constriction point shift.Protein science : a publication of the Protein Society · 2024Article
- In Silico Screen Identifies a New Family of Agonists for the Bacterial Mechanosensitive Channel MscL.Antibiotics (Basel, Switzerland) · 2022Article
- Comparative Analyses of the Transport Proteins Encoded within the Genomes of nine Bifidobacterium Species.Microbial physiology · 2022Article
- Life with Bacterial Mechanosensitive Channels, from Discovery to Physiology to Pharmacological Target.Microbiology and molecular biology reviews : MMBR · 2020Review
- Novel MscL agonists that allow multiple antibiotics cytoplasmic access activate the channel through a common binding site.PloS one · 2020Article
- Novel compounds that specifically bind and modulate MscL: insights into channel gating mechanisms.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Tuning ion channel mechanosensitivity by asymmetry of the transbilayer pressure profile.Biophysical reviews · 2018Review
- Article
- Dihydrostreptomycin Directly Binds to, Modulates, and Passes through the MscL Channel Pore.PLoS biology · 2016Article
- bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles.The Journal of general physiology · 2016Article
- Scanning MscL Channels with Targeted Post-Translational Modifications for Functional Alterations.PloS one · 2015Article
- Mutations in a Conserved Domain of E. coli MscS to the Most Conserved Superfamily Residue Leads to Kinetic Changes.PloS one · 2015Article
- Electrostatics at the membrane define MscL channel mechanosensitivity and kinetics.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Dynamics of protein-protein interactions at the MscL periplasmic-lipid interface.Biophysical journal · 2014Article
- Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The MscS and MscL families of mechanosensitive channels act as microbial emergency release valves.Journal of bacteriology · 2012Review
- Sensing and responding to membrane tension: the bacterial MscL channel as a model system.Biophysical journal · 2012Review
- Differential effects of lipids and lyso-lipids on the mechanosensitivity of the mechanosensitive channels MscL and MscS.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The dynamics of protein-protein interactions between domains of MscL at the cytoplasmic-lipid interface.Channels (Austin, Tex.)Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The bacterial mechanosensitive channel MscL is the best-studied mechanosensor, thus serving as a paradigm of how a protein senses and responds to mechanical force. Models for the transition of Escherichia coli MscL from closed to open states propose a tilting of the transmembrane domains in the plane of the membrane, suggesting dynamic protein-lipid interactions. Here, we used a rapid in vivo assay to assess the function of channels that were post-translationally modified at several different sites in a region just distal to the cytoplasmic end of the second transmembrane helix. We utilized multiple probes with various affinities for the membrane environment. The in vivo functional data, combined with site-directed mutagenesis, single-channel analyses, and tryptophan fluorescence measurements, confirmed that lipid interactions within this region are critical for MscL gating. The data suggest a model in which this region acts as an anchor for the transmembrane domain tilting during gating. Furthermore, the conservation of analogous motifs among many other channels suggests a conserved protein-lipid dynamic mechanism.
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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.