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Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains

hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorGRONNIER, Julien
dc.contributor.authorCROWET, Jean-Marc
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorNASIR, Mehmet Nail
dc.contributor.authorBAYLE, Vincent
hal.structure.identifierInterdisciplinary Institute for Neuroscience [Bordeaux] [IINS]
dc.contributor.authorHOSY, Eric
dc.contributor.authorPLATRE, Matthieu Pierre
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorGOUGUET, Paul
dc.contributor.authorRAFFAELE, Sylvain
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.authorLOQUET, Antoine
dc.contributor.authorSIMON-PLAS, Francoise
dc.contributor.authorGERBEAU-PISSOT, Patricia
dc.contributor.authorDER, Christophe
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorBAYER, Emmanuelle
dc.contributor.authorJAILLAIS, Yvon
dc.contributor.authorDELEU, Magali
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorGERMAIN, Veronique
dc.contributor.authorLINS, Laurence
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMONGRAND, Sébastien
dc.date.accessioned2020-07-09T14:16:54Z
dc.date.available2020-07-09T14:16:54Z
dc.date.issued2017-07-31
dc.identifier.issn2050-084X
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10322
dc.description.abstractEnPlasma Membrane is the primary structure for adjusting to ever changing conditions. PM sub-compartmentalization in domains is thought to orchestrate signaling. Yet, mechanisms governing membrane organization are mostly uncharacterized. The plant-specific REMORINs are proteins regulating hormonal crosstalk and host invasion. REMs are the best-characterized nanodomain markers via an uncharacterized moiety called REMORIN C-terminal Anchor. By coupling biophysical methods, super-resolution microscopy and physiology, we decipher an original mechanism regulating the dynamic and organization of nanodomains. We showed that targeting of REMORIN is independent of the COP-II-dependent secretory pathway and mediated by PI4P and sterol. REM-CA is an unconventional lipid-binding motif that confers nanodomain organization. Analyses of REM-CA mutants by single particle tracking demonstrate that mobility and supramolecular organization are critical for immunity. This study provides a unique mechanistic insight into how the tight control of spatial segregation is critical in the definition of PM domain necessary to support biological function.
dc.title.enStructural basis for plant plasma membrane protein dynamics and organization into functional nanodomains
dc.typeArticle de revue
dc.identifier.doi10.7554/eLife.26404
dc.subject.halChimie/Matériaux
bordeaux.journalElife
bordeaux.volume6
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
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