ArticleProceedings of the National Academy of Sciences of the United States of America2008
Gating-associated conformational changes in the mechanosensitive channel MscL.
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 34 papers.
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Who cites it
34 citing papers in PubMed.
- Structural basis of the gating mechanism of the large-conductance mechanosensitive channel from Escherichia coli.Nature communications · 2026Article
- Sonogenetics for precision medicine: from molecular toolkit to clinical translation.Theranostics · 2026Review
- Editorial:Frontiers in chemistry · 2024Article
- The principles and promising future of sonogenetics for precision medicine.Theranostics · 2024Review
- Approaches for the modulation of mechanosensitive MscL channel pores.Frontiers in chemistry · 2023Review
- A novel force transduction pathway from a tension sensor to the gate in the mechano-gating of MscL channel.Frontiers in chemistry · 2023Article
- Curcumin activation of a bacterial mechanosensitive channel underlies its membrane permeability and adjuvant properties.PLoS pathogens · 2021Article
- MCAs in Arabidopsis are CaNature communications · 2021Article
- Life with Bacterial Mechanosensitive Channels, from Discovery to Physiology to Pharmacological Target.Microbiology and molecular biology reviews : MMBR · 2020Review
- Simulation of the nodal flow of mutant embryos with a small number of cilia: comparison of mechanosensing and vesicle transport hypotheses.Royal Society open science · 2018Article
- Structural Dynamics of the MscL C-terminal Domain.Scientific reports · 2017Article
- Removal of the mechanoprotective influence of the cytoskeleton reveals PIEZO1 is gated by bilayer tension.Nature communications · 2016Article
- Inducible release of particulates from liposomes using the mechanosensitive channel of large conductance and L-α-lysophosphatidylcholine.European biophysics journal : EBJ · 2015Article
- Molecular dynamics study on protein-water interplay in the mechanogating of the bacterial mechanosensitive channel MscL.European biophysics journal : EBJ · 2015Article
- Functional similarities between heterogeneously and homogenously expressed MscL constructs.European biophysics journal : EBJ · 2015Article
- Gating of a mechanosensitive channel due to cellular flows.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The Effect of Detergent, Temperature, and Lipid on the Oligomeric State of MscL Constructs: Insights from Mass Spectrometry.Chemistry & biology · 2015Article
- MscL: channeling membrane tension.Pflugers Archiv : European journal of physiology · 2015Review
- Global structural changes of an ion channel during its gating are followed by ion mobility mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure and stability of the C-terminal helical bundle of the E. coli mechanosensitive channel of large conductance.Protein science : a publication of the Protein Society · 2013Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Bacterial cells avoid lysis in response to hypoosmotic shock through the opening of the mechanosensitive channel MscL. Upon channel opening, MscL is thought to expand in the plane of the membrane and form a large pore with an estimated diameter of 3-4 nm. Here, we set out to analyze the closed and open structure of cell-free MscL. To this end, we characterized the function and structure of wild-type MscL and a mutant form of the protein (G22N MscL) that spontaneously adopts an open substate. Patch-clamp analysis of MscL that had been reconstituted into liposomes revealed that wild-type MscL was activated only by mechanical stimuli, whereas G22N MscL displayed spontaneous opening to the open substate. In accord with these results, Ca(2+) influx into G22N MscL-containing liposomes occurred in the absence of mechanical stimulation. The electrophoretic migration of chemically cross-linked G22N MscL was slower than that of cross-linked wild-type MscL, suggesting that G22N MscL is in an expanded form. Finally, electron microscopy using low-angle rotary shadowing revealed the presence of a pore at the center of G22N MscL. No pore could be detected in wild-type MscL. However, wild-type MscL possessed a protrusion at one end, which was absent in G22N MscL. The deletion of carboxyl-terminal 27 residues resulted in the loss of protrusion and proper multimerization. The structures of wild-type and G22N MscL reveal that the opening of MscL is accompanied by the dissociation of a carboxyl-terminal protrusion and pore formation.
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