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Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state
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dc.contributor.author | Wang, Bolin | |
dc.contributor.author | Lane, Benjamin J | |
dc.contributor.author | Kapsalis, Charalampos | |
dc.contributor.author | Ault, James R | |
dc.contributor.author | Sobott, Frank | |
dc.contributor.author | El Mkami, Hassane | |
dc.contributor.author | Calabrese, Antonio N | |
dc.contributor.author | Kalli, Antreas C | |
dc.contributor.author | Pliotas, Christos | |
dc.date.accessioned | 2022-05-11T15:30:06Z | |
dc.date.available | 2022-05-11T15:30:06Z | |
dc.date.issued | 2022-04-07 | |
dc.identifier.citation | Wang , B , Lane , B J , Kapsalis , C , Ault , J R , Sobott , F , El Mkami , H , Calabrese , A N , Kalli , A C & Pliotas , C 2022 , ' Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state ' , Structure , vol. 30 , no. 4 , pp. 608-622.e5 . https://doi.org/10.1016/j.str.2021.12.004 | en |
dc.identifier.issn | 0969-2126 | |
dc.identifier.other | PURE: 277420872 | |
dc.identifier.other | PURE UUID: 58a4337a-0508-4c7c-a17d-f79ed6fba544 | |
dc.identifier.other | PubMed: 34986323 | |
dc.identifier.other | ORCID: /0000-0002-0552-5784/work/106397169 | |
dc.identifier.other | ORCID: /0000-0002-4309-4858/work/106397462 | |
dc.identifier.other | Scopus: 85127345653 | |
dc.identifier.other | WOS: 000787157700006 | |
dc.identifier.uri | https://hdl.handle.net/10023/25342 | |
dc.description | This project was supported by a Biotechnology and Biological Sciences Research Council (BBSRC) grant (BB/S018069/1) to C.P., who also acknowledges support from the Wellcome Trust (WT) (219999/Z/19/Z) and the Chinese Scholarship Council (CSC) in the form of studentships for B.J.L. and B.W. respectively. A.N.C. is a Sir Henry Dale Fellow jointly funded by the WT and the Royal Society (220628/Z/20/Z). Funding from the BBSRC (BB/M012573/1) enabled the purchase of mass spectrometry equipment. | en |
dc.description.abstract | The mechanosensitive ion channel of large conductance MscL gates in response to membrane tension changes. Lipid removal from transmembrane pockets leads to a concerted structural and functional MscL response, but it remains unknown whether there is a correlation between the tension-mediated state and the state derived by pocket delipidation in the absence of tension. Here, we combined pulsed electron paramagnetic resonance spectroscopy and hydrogen-deuterium exchange mass spectrometry, coupled with molecular dynamics simulations under membrane tension, to investigate the structural changes associated with the distinctively derived states. Whether it is tension- or modification-mediated pocket delipidation, we find that MscL samples a similar expanded subconducting state. This is the final step of the delipidation pathway, but only an intermediate stop on the tension-mediated path, with additional tension triggering further channel opening. Our findings hint at synergistic modes of regulation by lipid molecules in membrane tension-activated mechanosensitive channels. | |
dc.format.extent | 21 | |
dc.language.iso | eng | |
dc.relation.ispartof | Structure | en |
dc.rights | Copyright © 2021 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). | en |
dc.subject | Lipids | en |
dc.subject | MscL | en |
dc.subject | MscS | en |
dc.subject | Mechnoasensitive channels | en |
dc.subject | EPR spectroscopy | en |
dc.subject | HDX | en |
dc.subject | MD | en |
dc.subject | ESSEM | en |
dc.subject | Mass spectrometry | en |
dc.subject | Force-from-lipid | en |
dc.subject | QD Chemistry | en |
dc.subject | QH301 Biology | en |
dc.subject | DAS | en |
dc.subject.lcc | QD | en |
dc.subject.lcc | QH301 | en |
dc.title | Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state | en |
dc.type | Journal article | en |
dc.description.version | Publisher PDF | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. School of Physics and Astronomy | en |
dc.identifier.doi | https://doi.org/10.1016/j.str.2021.12.004 | |
dc.description.status | Peer reviewed | en |
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