ArticleBiophysical journal2009
Structural changes in the cytoplasmic domain of the mechanosensitive channel MscS during opening.
Article in Biophysical journal, 2009. 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.
- Charged pore-lining residues are required for normal channel kinetics in the eukaryotic mechanosensitive ion channel MSL1.Channels (Austin, Tex.) · 2020Article
- Transmembrane TM3b of Mechanosensitive Channel MscS Interacts With Cytoplasmic Domain Cyto-Helix.Frontiers in physiology · 2018Article
- The evolutionary 'tinkering' of MscS-like channels: generation of structural and functional diversity.Pflugers Archiv : European journal of physiology · 2015Review
- Article
- The activation mode of the mechanosensitive ion channel, MscL, by lysophosphatidylcholine differs from tension-induced gating.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- The cytoplasmic cage domain of the mechanosensitive channel MscS is a sensor of macromolecular crowding.The Journal of general physiology · 2014Article
- Selectivity mechanisms in MscS-like channels: From structure to function.Channels (Austin, Tex.) · 2014Article
- Electrophysiological characterization of the mechanosensitive channel MscCG in Corynebacterium glutamicum.Biophysical journal · 2013Article
- MscS-like mechanosensitive channels in plants and microbes.Biochemistry · 2013Review
- 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
- 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
- Functional analysis of conserved motifs in the mechanosensitive channel homolog MscS-Like2 from Arabidopsis thaliana.PloS one · 2012Article
- Bacterial mechanosensitive channels--MscS: evolution's solution to creating sensitivity in function.Annual review of biophysics · 2012Review
- Mechanosensitive channels: what can they do and how do they do it?Structure (London, England : 1993) · 2011Review
- Defining the role of the tension sensor in the mechanosensitive channel of small conductance.Biophysical journal · 2011Article
- Cytoplasmic domain filter function in the mechanosensitive channel of small conductance.Biophysical journal · 2011Article
- Adaptive MscS gating in the osmotic permeability response in E. coli: the question of time.Biochemistry · 2011Article
- Genetic screen for potassium leaky small mechanosensitive channels (MscS) in Escherichia coli: recognition of cytoplasmic β domain as a new gating element.The Journal of biological chemistry · 2011Article
- Fluorescence anisotropy and resonance energy transfer: powerful tools for measuring real time protein dynamics in a physiological environment.Current opinion in pharmacology · 2010Review
- Mechanosensitivity of ion channels based on protein-lipid interactions.Journal of the Royal Society, Interface · 2010Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial mechanosensitive channel MscS forms a homoheptamer of subunits composed of a transmembrane (TM) domain and a large cytoplasmic (CP) domain. Recent studies suggest that a lateral expansion of the TM domain, structural change in the CP domain, and TM-CP interactions are essential to open the channel. However, it has not been examined whether the CP domain undergoes structural changes during channel opening. The aim of this study was to estimate structural changes in the CP domain during channel opening using fluorescence resonance energy transfer (FRET) spectroscopy. To monitor changes in the horizontal diameter of the CP domain, four point mutants (A132C, F178C, L246C, and R259C), all of which had channel activity, were created and labeled with Alexa488 and Alexa568 for FRET analysis. The FRET efficiency of these mutants decreased when lysophosphatidylcholine was applied to open the channel, suggesting that the CP domain swells up when the channel opens. The degree of the decease in FRET efficiency after lysophosphatidylcholine treatment was smaller in the D62N/F178C mutant, which was deficient in the TM-CP interactions, than in the F178C mutant. These findings provide the first, to our knowledge, experimental evidence that the CP domain swells up during channel opening, and the swelling is mediated by the TM-CP interactions.
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