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Connecting the dots: from nanodomains to physiological functions of REMORINs

dc.rights.licenseopenen_US
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorGOUGUET, Paul
dc.contributor.authorGRONNIER, Julien
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLEGRAND, Anthony
dc.contributor.authorPERRAKI, Artemis
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorJOLIVET, Marie-Dominique
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorDEROUBAIX, Anne-Flore
dc.contributor.authorGERMAN-RETANA, Sylvie
dc.contributor.authorBOUDSOCQ, Marie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMONGRAND, Sébastien
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorGERMAIN, Veronique
dc.date.accessioned2021-07-08T13:29:13Z
dc.date.available2021-07-08T13:29:13Z
dc.date.issued2021
dc.identifier.issn0032-0889en_US
dc.identifier.otherhttps://academic.oup.com/plphys/article-lookup/doi/10.1093/plphys/kiaa063#supplementary-dataen_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/106469
dc.description.abstractEnREMORINs (REMs) are a plant-specific protein family, proposed regulators of membrane-associated molecular assemblies and well-established markers of plasma membrane nanodomains. REMs play a diverse set of functions in plant interactions with pathogens and symbionts, responses to abiotic stresses, hormone signaling and cell-to-cell communication. In this review, we highlight the established and more putative roles of REMs throughout the literature. We discuss the physiological functions of REMs, the mechanisms underlying their nanodomain-organization and their putative role as regulators of nanodomain-associated molecular assemblies. Furthermore, we discuss how REM phosphorylation may regulate their functional versatility. Overall, through data-mining and comparative analysis of the literature, we suggest how to further study the molecular mechanisms underpinning the functions of REMs.
dc.description.sponsorshipSaclay Plant Sciences - ANR-10-LABX-0040en_US
dc.language.isoENen_US
dc.title.enConnecting the dots: from nanodomains to physiological functions of REMORINs
dc.typeArticle de revueen_US
dc.identifier.doi10.1093/plphys/kiaa063en_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalPlant Physiologyen_US
bordeaux.page632-649en_US
bordeaux.volume185en_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-03205360
hal.exportfalse
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Plant%20Physiology&rft.date=2021&rft.volume=185&rft.issue=3&rft.spage=632-649&rft.epage=632-649&rft.eissn=0032-0889&rft.issn=0032-0889&rft.au=GOUGUET,%20Paul&GRONNIER,%20Julien&LEGRAND,%20Anthony&PERRAKI,%20Artemis&JOLIVET,%20Marie-Dominique&rft.genre=article


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