The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels

The activation of bacterial mechanosensitive channels is still not fully understood. Here, Bavi et al. show that the N-terminal helix of MscL dynamically couples membrane tension to channel gating, suggesting a conserved mechanism underlying the mechanosensitivity of ion channels of higher organisms...

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Autores principales:	Navid Bavi, D. Marien Cortes, Charles D. Cox, Paul R. Rohde, Weihong Liu, Joachim W. Deitmer, Omid Bavi, Pavel Strop, Adam P. Hill, Douglas Rees, Ben Corry, Eduardo Perozo, Boris Martinac
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2a07ef9b726d4ac8a5718aab20eb0e33
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spelling	oai:doaj.org-article:2a07ef9b726d4ac8a5718aab20eb0e332021-12-02T14:39:13ZThe role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels10.1038/ncomms119842041-1723https://doaj.org/article/2a07ef9b726d4ac8a5718aab20eb0e332016-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms11984https://doaj.org/toc/2041-1723The activation of bacterial mechanosensitive channels is still not fully understood. Here, Bavi et al. show that the N-terminal helix of MscL dynamically couples membrane tension to channel gating, suggesting a conserved mechanism underlying the mechanosensitivity of ion channels of higher organisms.Navid BaviD. Marien CortesCharles D. CoxPaul R. RohdeWeihong LiuJoachim W. DeitmerOmid BaviPavel StropAdam P. HillDouglas ReesBen CorryEduardo PerozoBoris MartinacNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Navid Bavi D. Marien Cortes Charles D. Cox Paul R. Rohde Weihong Liu Joachim W. Deitmer Omid Bavi Pavel Strop Adam P. Hill Douglas Rees Ben Corry Eduardo Perozo Boris Martinac The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels
description	The activation of bacterial mechanosensitive channels is still not fully understood. Here, Bavi et al. show that the N-terminal helix of MscL dynamically couples membrane tension to channel gating, suggesting a conserved mechanism underlying the mechanosensitivity of ion channels of higher organisms.
format	article
author	Navid Bavi D. Marien Cortes Charles D. Cox Paul R. Rohde Weihong Liu Joachim W. Deitmer Omid Bavi Pavel Strop Adam P. Hill Douglas Rees Ben Corry Eduardo Perozo Boris Martinac
author_facet	Navid Bavi D. Marien Cortes Charles D. Cox Paul R. Rohde Weihong Liu Joachim W. Deitmer Omid Bavi Pavel Strop Adam P. Hill Douglas Rees Ben Corry Eduardo Perozo Boris Martinac
author_sort	Navid Bavi
title	The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels
title_short	The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels
title_full	The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels
title_fullStr	The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels
title_full_unstemmed	The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels
title_sort	role of mscl amphipathic n terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/2a07ef9b726d4ac8a5718aab20eb0e33
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The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels

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