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dc.rights.licenseopenen_US
dc.contributor.authorMARTINEZ, Denis
dc.contributor.authorLEGRAND, Anthony
dc.contributor.authorGRONNIER, Julien
dc.contributor.authorDECOSSAS, Marion
dc.contributor.authorGOUGUET, Paul
dc.contributor.authorLAMBERT, Olivier
dc.contributor.authorBERBON, Melanie
dc.contributor.authorVERRON, Loris
dc.contributor.authorGRÉLARD, Axelle
dc.contributor.authorGERMAIN, Veronique
dc.contributor.authorLOQUET, Antoine
dc.contributor.authorMONGRAND, Sébastien
dc.contributor.authorHABENSTEIN, Birgit
dc.date.accessioned2019
dc.date.available2019
dc.date.issued2019
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/3805
dc.description.abstractEnREMORINs are nanodomain-organized proteins located in the plasma membrane and involved in cellular re-sponses in plants. The dynamic assembly of the membrane nanodomains represents an essential tool of theversatile membrane barriers to control and modulate cellular functions. Nevertheless, the assembly mechanismsand protein organization strategies of nanodomains are poorly understood and many structural aspects aredifficult to visualize. Using an ensemble of biophysical approaches, including solid-state nuclear magnetic re-sonance, cryo-electron microscopy andin vivoconfocal imaging, we providefirst insights on the role and thestructural mechanisms of REMORIN trimerization. Our results suggest that the formation of REMORIN coiled-coil trimers is essential for membrane recruitment and promotes REMORIN assemblyin vitrointo longfilamentsby trimer-trimer interactions that might participate in nanoclustering into membrane domainsin vivo.
dc.language.isoENen_US
dc.subject.enREMORIN
dc.subject.enNanodomain
dc.subject.enMembrane protein
dc.subject.enSolid-state NMR
dc.subject.enProtein filament
dc.title.enCoiled-coil oligomerization controls localization of the plasma membrane REMORINs.
dc.typeArticle de revueen_US
dc.subject.halInformatique [cs]/Ingénierie assistée par ordinateuren_US
dc.subject.halInformatique [cs]/Interface homme-machine [cs.HC]en_US
dc.subject.halSciences de l'ingénieur [physics]/Mécanique [physics.med-ph]/Génie mécanique [physics.class-ph]en_US
bordeaux.journalJournal of Structural Biologyen_US
bordeaux.page12-19en_US
bordeaux.volume206en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.issue1en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03181424
hal.version1
hal.date.transferred2021-03-25T14:48:34Z
hal.exporttrue
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