ArticleBiophysical journal2011
Defining the role of the tension sensor in the mechanosensitive channel of small conductance.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Origin, evolution and diversification of plant mechanosensitive channel of small conductance-like (MSL) proteins.BMC plant biology · 2023Article
- Mechanosensitive aquaporins.Biophysical reviews · 2023Review
- How Functional Lipids Affect the Structure and Gating of Mechanosensitive MscS-like Channels.International journal of molecular sciences · 2022Review
- Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance.Nature communications · 2020Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Mutations in a Conserved Domain of E. coli MscS to the Most Conserved Superfamily Residue Leads to Kinetic Changes.PloS one · 2015Article
- The mechanosensitive channel of small conductance (MscS) functions as a Jack-in-the box.Biochimica et biophysica acta · 2015Article
- The evolutionary 'tinkering' of MscS-like channels: generation of structural and functional diversity.Pflugers Archiv : European journal of physiology · 2015Review
- Energetics of gating MscS by membrane tension in azolectin liposomes and giant spheroplasts.Channels (Austin, Tex.) · 2014Article
- MscS-like mechanosensitive channels in plants and microbes.Biochemistry · 2013Review
- Identification and analysis of putative homologues of mechanosensitive channels in pathogenic protozoa.PloS one · 2013Article
- Ss-bCNGa: a unique member of the bacterial cyclic nucleotide gated (bCNG) channel family that gates in response to mechanical tension.European biophysics journal : EBJ · 2012Article
- Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Bacterial mechanosensitive channels--MscS: evolution's solution to creating sensitivity in function.Annual review of biophysics · 2012Review
- Mechanical properties of lipid bilayers and regulation of mechanosensitive function: from biological to biomimetic channels.Channels (Austin, Tex.)Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations that alter the phenotypic behavior of the Escherichia coli mechanosensitive channel of small conductance (MscS) have been identified; however, most of these residues play critical roles in the transition between the closed and open states of the channel and are not directly involved in lipid interactions that transduce the tension response. In this study, we use molecular dynamic simulations to predict critical lipid interacting residues in the closed state of MscS. The physiological role of these residues was then investigated by performing osmotic downshock assays on MscS mutants where the lipid interacting residues were mutated to alanine. These experiments identified seven residues in the first and second transmembrane helices as lipid-sensing residues. The majority of these residues are hydrophobic amino acids located near the extracellular interface of the membrane. All of these residues interact strongly with the lipid bilayer in the closed state of MscS, but do not face the bilayer directly in structures associated with the open and desensitized states of the channel. Thus, the position of these residues relative to the lipid membrane appears related to the ability of the channel to sense tension in its different physiological states.
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