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Structural evidence of a phosphoinositide-binding site in the Rgd1-RhoGAP domain

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.authorLANGLOIS D'ESTAINTOT, Beatrice
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGRANIER, Thierry
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorTOLCHARD, James
dc.contributor.authorCOURREGES, Cecile
dc.contributor.authorPROUZET-MAULEON, Valerie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHUGUES, Michel
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGALLOIS, Bernard
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.accessioned2020-07-09T14:16:43Z
dc.date.available2020-07-09T14:16:43Z
dc.date.issued2017-09
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10289
dc.description.abstractEnPhosphoinositide lipids recruit proteins to the plasma membrane involved in the regulation of cytoskeleton organization and in signalling pathways that control cell polarity and growth. Among those, Rgd1p is a yeast GTPase-activating protein (GAP) specific for Rho3p and Rho4p GTPases, which control actin polymerization and stress signalling pathways. Phosphoinositides not only bind Rgd1p, but also stimulate its GAP activity on the membrane-anchored form of Rho4p. Both F-BAR (F-BAR FCH, and BAR) and RhoGAP domains of Rgd1p are involved in lipid interactions. In the Rgd1p-F-BAR domain, a phosphoinositide-binding site has been recently characterized. We report here the X-ray structure of the Rgd1p-RhoGAP domain, identify by NMR spectroscopy and confirm by docking simulations, a new but cryptic phosphoinositide-binding site, comprising contiguous A1, A1' and B helices. The addition of helix A1', unusual among RhoGAP domains, seems to be crucial for lipid interactions. Such a site was totally unexpected inside a RhoGAP domain, as it was not predicted from either the protein sequence or its three-dimensional structure. Phosphoinositide-binding sites in RhoGAP domains have been reported to correspond to polybasic regions, which are located at the unstructured flexible termini of proteins. Solid-state NMR spectroscopy experiments confirm the membrane interaction of the Rgd1p-RhoGAP domain upon the addition of PtdIns(4,5)P2 and indicate a slight membrane destabilization in the presence of the two partners.
dc.title.enStructural evidence of a phosphoinositide-binding site in the Rgd1-RhoGAP domain
dc.typeArticle de revue
dc.identifier.doi10.1042/bcj20170331
dc.subject.halChimie/Matériaux
bordeaux.journalThe Biochemical Journal
bordeaux.page3307-3319
bordeaux.volume474
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.issue19
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=The%20Biochemical%20Journal&rft.date=2017-09&rft.volume=474&rft.issue=19&rft.spage=3307-3319&rft.epage=3307-3319&rft.au=MARTINEZ,%20Denis&LANGLOIS%20D'ESTAINTOT,%20Beatrice&GRANIER,%20Thierry&TOLCHARD,%20James&COURREGES,%20Cecile&rft.genre=article


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