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- W2464564128 abstract "Abstract The bacterial mechanosensitive channel MscL gates in response to membrane tension as a result of mechanical force transmitted directly to the channel from the lipid bilayer. MscL represents an excellent model system to study the basic biophysical principles of mechanosensory transduction. However, understanding of the essential structural components that transduce bilayer tension into channel gating remains incomplete. Here using multiple experimental and computational approaches, we demonstrate that the amphipathic N-terminal helix of MscL acts as a crucial structural element during tension-induced gating, both stabilizing the closed state and coupling the channel to the membrane. We propose that this may also represent a common principle in the gating cycle of unrelated mechanosensitive ion channels, allowing the coupling of channel conformation to membrane dynamics." @default.
- W2464564128 created "2016-07-22" @default.
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- W2464564128 date "2016-06-22" @default.
- W2464564128 modified "2023-10-11" @default.
- W2464564128 title "The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels" @default.
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- W2464564128 doi "https://doi.org/10.1038/ncomms11984" @default.
- W2464564128 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4917966" @default.
- W2464564128 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27329693" @default.
- W2464564128 hasPublicationYear "2016" @default.
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