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A nanodomain-anchored scaffolding complex is required for the function and localization of phosphatidylinositol 4-kinase alpha in plants

dc.rights.licenseopenen_US
dc.contributor.authorNOACK, Lise C
dc.contributor.authorBAYLE, Vincent
dc.contributor.authorARMENGOT, Laia
dc.contributor.authorROZIER, Frederique
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMAMODE CASSIM, Adiilah
dc.contributor.authorSTEVENS, Floris D
dc.contributor.authorCAILLAUD, Marie-Cecile
dc.contributor.authorMUNNIK, Teun
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMONGRAND, Sebastien
dc.contributor.authorPLESKOT, Roman
dc.contributor.authorJAILLAIS, Yvon
dc.date.accessioned2022-03-09T17:54:46Z
dc.date.available2022-03-09T17:54:46Z
dc.date.issued2022-01
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/136415
dc.description.abstractEnPhosphoinositides are low-abundant lipids that participate in the acquisition of membrane identity through their spatiotemporal enrichment in specific compartments. Phosphatidylinositol 4-phosphate (PI4P) accumulates at the plant plasma membrane driving its high electrostatic potential, and thereby facilitating interactions with polybasic regions of proteins. PI4Kα1 has been suggested to produce PI4P at the plasma membrane, but how it is recruited to this compartment is unknown. Here, we pin-point the mechanism that tethers Arabidopsis thaliana phosphatidylinositol 4-kinase alpha1 (PI4Kα1) to the plasma membrane via a nanodomain-anchored scaffolding complex. We established that PI4Kα1 is part of a complex composed of proteins from the NO-POLLEN-GERMINATION, EFR3-OF-PLANTS, and HYCCIN-CONTAINING families. Comprehensive knockout and knockdown strategies revealed that subunits of the PI4Kα1 complex are essential for pollen, embryonic, and post-embryonic development. We further found that the PI4Kα1 complex is immobilized in plasma membrane nanodomains. Using synthetic mis-targeting strategies, we demonstrate that a combination of lipid anchoring and scaffolding localizes PI4Kα1 to the plasma membrane, which is essential for its function. Together, this work opens perspectives on the mechanisms and function of plasma membrane nanopatterning by lipid kinases.
dc.description.sponsorshipVers un modèle intégratif de la bicouche lipidique de la membrane plasmique végétale - ANR-19-CE20-0016
dc.description.sponsorshipRégulation de la communication intercellulaire - le rôle de la phosphoprotéine REMORIN liée aux nanodomaines de la membrane plasmique
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.title.enA nanodomain-anchored scaffolding complex is required for the function and localization of phosphatidylinositol 4-kinase alpha in plants
dc.typeArticle de revueen_US
dc.identifier.doi10.1093/plcell/koab135en_US
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale/Botaniqueen_US
dc.identifier.pubmed34010411en_US
bordeaux.journalThe Plant Cellen_US
bordeaux.page302-332
bordeaux.volume34
bordeaux.hal.laboratoriesLaboratoire de Biogenèse Membranaire (LBM) - UMR 5200en_US
bordeaux.issue1
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.identifier.funderIDMinistère de l'Enseignement supérieur, de la Recherche et de l'Innovationen_US
hal.exportfalse
dc.rights.ccCC BYen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=The%20Plant%20Cell&rft.date=2022-01&rft.volume=34&rft.issue=1&rft.spage=302-332&rft.epage=302-332&rft.au=NOACK,%20Lise%20C&BAYLE,%20Vincent&ARMENGOT,%20Laia&ROZIER,%20Frederique&MAMODE%20CASSIM,%20Adiilah&rft.genre=article


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