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Avidity-driven polarity establishment via multivalent lipid-GTPase module interactions

dc.rights.licenseopenen_US
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorMECA, Julien
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorMASSONI-LAPORTE, Aurelie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorMARTINEZ, Denis
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorSARTOREL, Elodie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorMCCUSKER, Derek
dc.date.accessioned2021-07-16T09:52:01Z
dc.date.available2021-07-16T09:52:01Z
dc.date.issued2019
dc.identifier.issn1460-2075en_US
dc.identifier.otherhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6356062/#en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/109277
dc.description.abstractEnWhile Rho GTPases are indispensible regulators of cellular polarity, the mechanisms underlying their anisotropic activation at membranes have been elusive. Using the budding yeast Cdc42 GTPase module, which includes a guanine nucleotide exchange factor (GEF) Cdc24 and the scaffold Bem1, we find that avidity generated via multivalent anionic lipid interactions is a critical mechanistic constituent of polarity establishment. We identify basic cluster (BC) motifs in Bem1 that drive the interaction of the scaffold-GEF complex with anionic lipids at the cell pole. This interaction appears to influence lipid acyl chain ordering, thus regulating membrane rigidity and feedback between Cdc42 and the membrane environment. Sequential mutation of the Bem1 BC motifs, PX domain, and the PH domain of Cdc24 lead to a progressive loss of cellular polarity stemming from defective Cdc42 nanoclustering on the plasma membrane and perturbed signaling. Our work demonstrates the importance of avidity via multivalent anionic lipid interactions in the spatial control of GTPase activation.
dc.description.sponsorshipRégulation et dynamique d'un module de signaliation de la famille Rhoulation and dynamics of a GTPase signaling module - ANR-13-BSV2-0015en_US
dc.description.sponsorshipNanostructures biologiques et synthétiques étudiées par Résonance Magnétique Nucléaire du Solide - ANR-14-CE09-0020en_US
dc.language.isoENen_US
dc.subject.encell polarity
dc.subject.enlipids
dc.subject.ennanoclustering
dc.subject.enRho GTPase
dc.subject.ensuper‐resolution imaging
dc.title.enAvidity-driven polarity establishment via multivalent lipid-GTPase module interactions
dc.typeArticle de revueen_US
dc.identifier.doi10.15252/embj.201899652en_US
dc.subject.halChimie/Matériauxen_US
dc.identifier.pubmedPMC6356062en_US
bordeaux.journalThe EMBO Journalen_US
bordeaux.volume38en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.issue3en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-02412746
hal.version1
hal.date.transferred2021-11-16T16:19:52Z
hal.exporttrue
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