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Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMR

dc.rights.licenseopenen_US
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLEGRAND, Anthony
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorMARTINEZ, Denis
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGRELARD, Axelle
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBERBON, Melanie
hal.structure.identifierInstitut Européen de Chimie et Biologie [IECB]
dc.contributor.authorMORVAN, Estelle
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorTAWANI, Arpita
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMONGRAND, Sébastien
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
dc.date.accessioned2020-05-13T10:15:35Z
dc.date.available2020-05-13T10:15:35Z
dc.date.issued2019
dc.identifier.issn2296-889Xen_US
dc.identifier.otherhttps://www.frontiersin.org/articles/10.3389/fmolb.2019.00107/full#supplementary-materialen_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/7556
dc.description.abstractEnNanodomains are dynamic membrane subcompartments, enriched in specific lipid, and protein components that act as functional platforms to manage an abundance of cellular processes. The remorin protein of plants is a well-established nanodomain marker and widely serves as a paradigm to study nanodomain clustering. Located at the inner leaflet of the plasma membrane, remorins perform essential functions during signaling. Using deuteriumand phosphorus solid-state NMR, we inquire on themolecular determinants of the lipid-protein and protein-protein interactions driving nanodomain clustering. By monitoring thermotropism properties, lipid acyl chain order and membrane thickness, we report the effects of phosphoinositides and sterols on the interaction of various remorin peptides and protein constructs with the membrane. We probed several critical residues involved in this interaction and the involvement of the coiled-coil homo-oligomerisation domain into the formation of remorin nanodomains. We trace the essential role of the pH in nanodomain clustering based on anionic lipids such as phosphoinositides. Our results reveal a complex interplay between specific remorin residues and domains, the environmental pH and their resulting effects on the lipid dynamics for phosphoinositide-enriched membranes.
dc.description.sponsorshipFacteurs cellulaires recrutés par les potyvirus pour leur transport intercellulaire : de nouvelles sources de résistance des plantes?en_US
dc.language.isoENen_US
dc.title.enNanodomain Clustering of the Plant Protein Remorin by Solid-State NMR
dc.title.alternativeFront. Mol. Biosci.en_US
dc.typeArticle de revueen_US
dc.identifier.doi10.3389/fmolb.2019.00107
dc.subject.halChimie/Matériauxen_US
bordeaux.journalFrontiers in Molecular Biosciencesen_US
bordeaux.volume6en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.identifier.funderIDEuropean Research Councilen_US
hal.identifierhal-03182159
hal.version1
hal.date.transferred2021-03-26T09:56:29Z
hal.exporttrue
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