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Molecular mechanisms behind remorin nanodomain formation by solidstate NMR

dc.rights.licenseopenen_US
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
dc.contributor.authorGRONNIER, Julien
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBERBON, Melanie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDECOSSAS, Marion
dc.contributor.authorGOUGET, Paul
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorGERMAIN, Veronique
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.authorLAMBERT, Olivier
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
dc.contributor.authorMONGRAND, Sébastien
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
dc.date.accessioned2021-06-30T15:06:16Z
dc.date.available2021-06-30T15:06:16Z
dc.date.issued2019
dc.identifier.issn0175-7571en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/94947
dc.description.abstractEnProtein and lipid components in biological membranes act as a dynamic network of subtle molecular inter-actions segregating the membrane into particular regions called nanodomains. Nanodomains act as func-tional platforms enriched in specific lipids (such as sterols and phosphoinositides) and proteins to performtheir diverse activities. Remorins (REMs) are plant proteins and well-established nanodomain markers and,as such, they can be considered as paradigm to provide a mechanistic description of membrane organisationinto functional nanodomains. Using solid-state nuclear magnetic resonance (ssNMR) and building upon ourinitial knowledge ofStREM1.3 and its C-terminal membrane anchor, we reveal the delicate balance betweenhydrophobic and electrostatic effects leading up to the protein’s characteristic affinity for negatively chargedphospholipids. In a divide-and-conquer approach, we describe the impact ofStREM1.3’s C-terminal anchor, itsoligomerisation domain and intrinsically disordered region on membrane structure and dynamics. Further-more, we tackle the structural features ofStREM1.3 when associated to nanodomain-mimicking membranes.We reveal thatStREM1.3 drives nanodomain organisation by concerted lipid-protein and protein-protein inter-actions
dc.language.isoENen_US
dc.subject.enSolid-state NMR
dc.subject.enMembrane
dc.subject.enNanodomains
dc.subject.enRemorin
dc.title.enMolecular mechanisms behind remorin nanodomain formation by solidstate NMR
dc.typeArticle de revueen_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalEuropean Biophysics Journal with Biophysics Lettersen_US
bordeaux.pageS246-S246en_US
bordeaux.volume48en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRS
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03275111
hal.version1
hal.date.transferred2021-06-30T15:06:18Z
hal.exporttrue
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