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dc.rights.licenseopenen_US
dc.relation.isnodouble5fc053a7-6f19-4d78-946e-031242c4f98f*
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorMARTINEZ, Denis
dc.contributor.authorPROUZET-MAULEON, Valerie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHUGUES, Michel
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorDOIGNON, Francois
ORCID: 0000-0002-9007-2408
IDREF: 097088439
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorODAERT, Benoit
dc.date.accessioned2020-04-08T13:15:24Z
dc.date.available2020-04-08T13:15:24Z
dc.date.issued2018
dc.identifier.issn1874-2718en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/4183
dc.description.abstractEnThe protein Rgd1 is involved in the regulation of cytoskeleton formation and in signalling pathways that control cell polarity and growth in Saccharomyces cerevisiae. Rgd1p is composed of a F-BAR domain required for membrane binding and a RhoGAP domain responsible for activating Rho3p and Rho4p, two GTPases respectively involved in bud growth and cytokinesis. Rgd1p is recruited to the membrane through interactions with phosphoinositide lipids, which bind the two isolated domains and stimulate the RhoGAP activity on Rho4p. As previously shown by crystallography, the membrane-binding F-BAR domain contains a conserved inositol phosphate binding site, which explains the preferential binding of phosphoinositides. In contrast, RhoGAP domains are not expected to bind lipids. In order to unravel this puzzling feature, we solved the three-dimensional structure of the isolated protein and found a cryptic phosphoinositide binding site involving non conserved residues (Martinez et al. 2017). The assignment of the resonances and secondary structure of Rgd1-RhoGAP (aa 450-666) is presented here.
dc.language.isoENen_US
dc.subject.enRhoGAP
dc.subject.enRgd1
dc.subject.enAssignment
dc.subject.enNMR
dc.subject.enPhosphoinositide
dc.title.enAssignment of H-1, C-13 and N-15 resonances and secondary structure of the Rgd1-RhoGAP domain
dc.title.alternativeBiomol NMR Assignen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1007/s12104-017-9794-zen_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalBiomolecular Nmr Assignmentsen_US
bordeaux.page129-132en_US
bordeaux.volume12en_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-02537007
hal.version1
hal.date.transferred2020-04-08T13:15:29Z
hal.exporttrue
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