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Structural determinants of REMORIN nanodomain formation in anionic membranes

dc.rights.licenseopenen_US
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorLEGRAND, Anthony
dc.contributor.authorGONZALEZ CAVA, Daniel
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorJOLIVET, Marie-Dominique
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDECOSSAS, Marion
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLAMBERT, Olivier
dc.contributor.authorBAYLE, Vincent
dc.contributor.authorJAILLAIS, Yvon
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorGERMAIN, Veronique
dc.contributor.authorBOUDSOCQ, Marie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorVELEZ TIRADO, Marisela
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMONGRAND, Sébastien
dc.date.accessioned2024-04-30T09:53:02Z
dc.date.available2024-04-30T09:53:02Z
dc.date.issued2023
dc.identifier.issn0006-3495en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/199530
dc.description.abstractEnRemorins are a family of multigenic plasma membrane phosphoproteins involved in biotic and abiotic plant inter- action mechanisms, partnering in molecular signaling cascades. Signaling activity of remorins depends on their phosphorylation states and subsequent clustering into nanosized membrane domains. The presence of a coiled-coil domain and a C-terminal domain is crucial to anchor remorins to negatively charged membrane domains; however, the exact role of the N-terminal intrinsically disordered domain (IDD) on protein clustering and lipid interactions is largely unknown. Here, we combine chemical biology and imaging approaches to study the partitioning of group 1 remorin into anionic model membranes mimicking the inner leaflet of the plant plasma membrane. Using reconstituted membranes containing a mix of saturated and unsaturated phosphatidylcholine, phosphatidylinositol phosphates, and sterol, we investigate the clustering of remorins to the membrane and monitor the formation of nanosized membrane domains. REM1.3 promoted membrane nanodomain organization on the exposed external leaflet of both spherical lipid vesicles and flat supported lipid bilayers. Our results reveal that REM1.3 drives a mechanism allowing lipid reorganization, leading to the formation of remorin-enriched nanodomains. Phosphorylation of the N-terminal IDD by the calcium protein kinase CPK3 influences this clustering and can lead to the formation of smaller and more disperse domains. Our work reveals the phosphate-dependent involvement of the N-terminal IDD in the remorin-mem- brane interaction process by driving structural rearrangements at lipid-water interfaces.
dc.description.sponsorshipRégulation de la communication intercellulaire - le rôle de la phosphoprotéine REMORIN liée aux nanodomaines de la membrane plasmique - ANR-19-CE13-0021en_US
dc.description.sponsorshipDéveloppement d'une infrastructure française distribuée pour la métabolomique dédiée à l'innovationen_US
dc.description.sponsorshipSaclay Plant Sciencesen_US
dc.language.isoENen_US
dc.title.enStructural determinants of REMORIN nanodomain formation in anionic membranes
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.bpj.2022.12.035en_US
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaireen_US
bordeaux.journalBiophysical Journalen_US
bordeaux.page2192-2202en_US
bordeaux.volume122en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue11en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-04094094
hal.version1
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biophysical%20Journal&rft.date=2023&rft.volume=122&rft.issue=11&rft.spage=2192-2202&rft.epage=2192-2202&rft.eissn=0006-3495&rft.issn=0006-3495&rft.au=LEGRAND,%20Anthony&GONZALEZ%20CAVA,%20Daniel&JOLIVET,%20Marie-Dominique&DECOSSAS,%20Marion&LAMBERT,%20Olivier&rft.genre=article


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