Files in this item
The role of lipids in mechanosensation
Item metadata
dc.contributor.author | Pliotas, Christos | |
dc.contributor.author | Dahl, A Caroline E | |
dc.contributor.author | Rasmussen, Tim | |
dc.contributor.author | Mahendran, Kozhinjampara R | |
dc.contributor.author | Smith, Terry K | |
dc.contributor.author | Marius, Phedra | |
dc.contributor.author | Gault, Joseph | |
dc.contributor.author | Banda, Thandiwe | |
dc.contributor.author | Rasmussen, Akiko | |
dc.contributor.author | Miller, Samantha | |
dc.contributor.author | Robinson, Carol V | |
dc.contributor.author | Bayley, Hagan | |
dc.contributor.author | Sansom, Mark S P | |
dc.contributor.author | Booth, Ian R | |
dc.contributor.author | Naismith, Jim | |
dc.date.accessioned | 2016-05-18T23:32:36Z | |
dc.date.available | 2016-05-18T23:32:36Z | |
dc.date.issued | 2015-12 | |
dc.identifier | 230743794 | |
dc.identifier | 14059b9e-6190-41cc-b3c4-db3123bc7b03 | |
dc.identifier | 26551077 | |
dc.identifier | 84949530498 | |
dc.identifier | 000366152400012 | |
dc.identifier.citation | Pliotas , C , Dahl , A C E , Rasmussen , T , Mahendran , K R , Smith , T K , Marius , P , Gault , J , Banda , T , Rasmussen , A , Miller , S , Robinson , C V , Bayley , H , Sansom , M S P , Booth , I R & Naismith , J 2015 , ' The role of lipids in mechanosensation ' , Nature Structural and Molecular Biology , vol. 22 , no. 12 , pp. 991-998 . https://doi.org/10.1038/nsmb.3120 | en |
dc.identifier.issn | 1545-9993 | |
dc.identifier.other | ORCID: /0000-0002-4309-4858/work/31524146 | |
dc.identifier.uri | https://hdl.handle.net/10023/8823 | |
dc.description | This work was supported by Wellcome Trust grants WT092552MA (J.H.N. and I.R.B.), Senior Investigator Award WT100209MA (J.H.N.), 093228 (T.K.S.) and 092970 (M.S.P.S.), and Biotechnology and Biological Sciences Research Council grants BB/I019855/1 (M.S.P.S.), BB/H017917/1 (J.H.N. and I.R.B.) and BB/J009784/1 (H.B.). I.R.B. is supported as a Leverhulme Emeritus Fellow. J.H.N. is supported as a Royal Society Wolfson Merit Award holder and as a 1000 Talent Scholar at Sichuan University. A.C.E.D. was supported by an Engineering and Physical Sciences Research Council Systems Biology Doctoral Training Centre student fellowship. | en |
dc.description.abstract | The ability of proteins to sense membrane tension is pervasive in biology. A higher-resolution structure of the Escherichia coli small-conductance mechanosensitive channel MscS identifies alkyl chains inside pockets formed by the transmembrane helices (TMs). Purified MscS contains E. coli lipids, and fluorescence quenching demonstrates that phospholipid acyl chains exchange between bilayer and TM pockets. Molecular dynamics and biophysical analyses show that the volume of the pockets and thus the number of lipid acyl chains within them decreases upon channel opening. Phospholipids with one acyl chain per head group (lysolipids) displace normal phospholipids (with two acyl chains) from MscS pockets and trigger channel opening. We propose that the extent of acyl-chain interdigitation in these pockets determines the conformation of MscS. When interdigitation is perturbed by increased membrane tension or by lysolipids, the closed state becomes unstable, and the channel gates. | |
dc.format.extent | 840617 | |
dc.format.extent | 1688975 | |
dc.format.extent | 902150 | |
dc.format.extent | 928846 | |
dc.format.extent | 1157334 | |
dc.format.extent | 1055574 | |
dc.format.extent | 931806 | |
dc.language.iso | eng | |
dc.relation.ispartof | Nature Structural and Molecular Biology | en |
dc.subject | QH301 Biology | en |
dc.subject | QD Chemistry | en |
dc.subject | NDAS | en |
dc.subject | BDC | en |
dc.subject | R2C | en |
dc.subject.lcc | QH301 | en |
dc.subject.lcc | QD | en |
dc.title | The role of lipids in mechanosensation | en |
dc.type | Journal article | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.sponsor | BBSRC | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | 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. EaSTCHEM | en |
dc.identifier.doi | 10.1038/nsmb.3120 | |
dc.description.status | Peer reviewed | en |
dc.date.embargoedUntil | 2016-05-19 | |
dc.identifier.grantnumber | 092552/C/10/Z | en |
dc.identifier.grantnumber | 100209/Z/12/Z | en |
dc.identifier.grantnumber | BB/H017917/1 | en |
dc.identifier.grantnumber | 093228/Z/10/Z | en |
This item appears in the following Collection(s)
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.