ArticleChannels (Austin, Tex.)
The dynamics of protein-protein interactions between domains of MscL at the cytoplasmic-lipid interface.
Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Activation of a Bacterial Mechanosensitive Channel, MscL, Underlies the Membrane Permeabilization of Dual-Targeting Antibacterial Compounds.Antibiotics (Basel, Switzerland) · 2022Article
- In Silico Screen Identifies a New Family of Agonists for the Bacterial Mechanosensitive Channel MscL.Antibiotics (Basel, Switzerland) · 2022Article
- Review
- 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
- Dihydrostreptomycin Directly Binds to, Modulates, and Passes through the MscL Channel Pore.PLoS biology · 2016Article
- Mechanical coupling of the multiple structural elements of the large-conductance mechanosensitive channel during expansion.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Scanning MscL Channels with Targeted Post-Translational Modifications for Functional Alterations.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
- Mechanosensitive ion channels: an evolutionary and scientific tour de force in mechanobiology.Channels (Austin, Tex.)Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The bacterial mechanosensitive channel of large conductance, MscL, is one of the best characterized mechanosensitive channels serving as a paradigm for how proteins can sense and transduce mechanical forces. The physiological role of MscL is that of an emergency release valve that opens a large pore upon a sudden drop in the osmolarity of the environment. A crystal structure of a closed state of MscL shows it as a homopentamer, with each subunit consisting of two transmembrane domains (TM). There is consensus that the TM helices move in an iris like manner tilting in the plane of the membrane while gating. An N-terminal amphipathic helix that lies along the cytoplasmic membrane (S1), and the portion of TM2 near the cytoplasmic interface (TM2(ci)), are relatively close in the crystal structure, yet predicted to be dynamic upon gating. Here we determine how these two regions interact in the channel complex, and study how these interactions change as the channel opens. We have screened 143 double-cysteine mutants of E. coli MscL for their efficiency in disulfide bridging and generated a map of protein-protein interactions between these two regions. Interesting candidates have been further studied by patch clamp and show differences in channel activity under different redox potentials; the results suggest a model for the dynamics of these two domains during MscL gating.
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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.