Avidity-driven polarity establishment via multivalent lipid-GTPase module interactions
dc.rights.license | open | en_US |
hal.structure.identifier | Institut de biochimie et génétique cellulaires [IBGC] | |
dc.contributor.author | MECA, Julien | |
hal.structure.identifier | Institut de biochimie et génétique cellulaires [IBGC] | |
dc.contributor.author | MASSONI-LAPORTE, Aurelie | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | MARTINEZ, Denis | |
hal.structure.identifier | Institut de biochimie et génétique cellulaires [IBGC] | |
dc.contributor.author | SARTOREL, Elodie | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | LOQUET, Antoine | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | HABENSTEIN, Birgit | |
hal.structure.identifier | Institut de biochimie et génétique cellulaires [IBGC] | |
dc.contributor.author | MCCUSKER, Derek | |
dc.date.accessioned | 2021-07-16T09:52:01Z | |
dc.date.available | 2021-07-16T09:52:01Z | |
dc.date.issued | 2019 | |
dc.identifier.issn | 1460-2075 | en_US |
dc.identifier.other | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6356062/# | en_US |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/109277 | |
dc.description.abstractEn | While 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.sponsorship | Régulation et dynamique d'un module de signaliation de la famille Rhoulation and dynamics of a GTPase signaling module - ANR-13-BSV2-0015 | en_US |
dc.description.sponsorship | Nanostructures biologiques et synthétiques étudiées par Résonance Magnétique Nucléaire du Solide - ANR-14-CE09-0020 | en_US |
dc.language.iso | EN | en_US |
dc.subject.en | cell polarity | |
dc.subject.en | lipids | |
dc.subject.en | nanoclustering | |
dc.subject.en | Rho GTPase | |
dc.subject.en | super‐resolution imaging | |
dc.title.en | Avidity-driven polarity establishment via multivalent lipid-GTPase module interactions | |
dc.type | Article de revue | en_US |
dc.identifier.doi | 10.15252/embj.201899652 | en_US |
dc.subject.hal | Chimie/Matériaux | en_US |
dc.identifier.pubmed | PMC6356062 | en_US |
bordeaux.journal | The EMBO Journal | en_US |
bordeaux.volume | 38 | en_US |
bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248 | en_US |
bordeaux.issue | 3 | en_US |
bordeaux.institution | Université de Bordeaux | en_US |
bordeaux.institution | Bordeaux INP | en_US |
bordeaux.institution | CNRS | en_US |
bordeaux.peerReviewed | oui | en_US |
bordeaux.inpress | non | en_US |
hal.identifier | hal-02412746 | |
hal.version | 1 | |
hal.date.transferred | 2021-11-16T16:19:52Z | |
hal.export | true | |
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