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hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierUniversité de Bordeaux [UB]
hal.structure.identifierInstitut National de la Recherche Agronomique [INRA]
dc.contributor.authorWATTELET-BOYER, Valérie
hal.structure.identifierBordeaux Imaging Center [BIC]
hal.structure.identifierCentre National de la Recherche Scientifique [CNRS]
hal.structure.identifierInstitut National de la Santé et de la Recherche Médicale [INSERM]
dc.contributor.authorBROCARD, Lysiane
hal.structure.identifierUmea Plant Science Center [UPSC]
dc.contributor.authorJONSSON, Kristoffer
hal.structure.identifierBiologie végétale intégrative [BVI]
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierCentre National de la Recherche Scientifique [CNRS]
hal.structure.identifierInstitut National de la Recherche Agronomique [INRA]
dc.contributor.authorESNAY, Nicolas
hal.structure.identifierBiologie végétale intégrative [BVI]
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierCentre National de la Recherche Scientifique [CNRS]
hal.structure.identifierInstitut National de la Recherche Agronomique [INRA]
dc.contributor.authorJOUBES, Jerome
hal.structure.identifierBiologie végétale intégrative [BVI]
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierUniversité de Bordeaux [UB]
hal.structure.identifierInstitut National de la Recherche Agronomique [INRA]
dc.contributor.authorDOMERGUE, Frédéric
hal.structure.identifierBiologie végétale intégrative [BVI]
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierUniversité de Bordeaux [UB]
hal.structure.identifierInstitut National de la Recherche Agronomique [INRA]
dc.contributor.authorMONGRAND, Sébastien
hal.structure.identifierCenter for Plant Cell Biology - Department of Botany and Plant Sciences
dc.contributor.authorRAIKHEL, Natasha
hal.structure.identifierCollege of Science [Swansea]
hal.structure.identifierUmea Plant Science Center [UPSC]
dc.contributor.authorBHALERAO, Rishikesh P.
hal.structure.identifierBiologie du fruit et pathologie [BFP]
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierUniversité de Bordeaux [UB]
hal.structure.identifierInstitut National de la Recherche Agronomique [INRA]
hal.structure.identifierBordeaux Imaging Center [BIC]
hal.structure.identifierInstitut National de la Santé et de la Recherche Médicale [INSERM]
dc.contributor.authorMOREAU, Patrick
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierUniversité de Bordeaux [UB]
hal.structure.identifierInstitut National de la Recherche Agronomique [INRA]
dc.contributor.authorBOUTTE, Yohann
dc.date.issued2016
dc.identifier.issn2041-1723
dc.description.abstractEnThe post-Golgi compartment trans-Golgi Network (TGN) is a central hub divided into multiple subdomains hosting distinct trafficking pathways, including polar delivery to apical membrane. Lipids such as sphingolipids and sterols have been implicated in polar trafficking from the TGN but the underlying mechanisms linking lipid composition to functional polar sorting at TGN subdomains remain unknown. Here we demonstrate that sphingolipids with alpha-hydroxylated acyl-chains of at least 24 carbon atoms are enriched in secretory vesicle subdomains of the TGN and are critical for de novo polar secretory sorting of the auxin carrier PIN2 to apical membrane of Arabidopsis root epithelial cells. We show that sphingolipid acyl-chain length influences the morphology and interconnections of TGN-associated secretory vesicles. Our results uncover that the sphingolipids acyl-chain length links lipid composition of TGN subdomains with polar secretory trafficking of PIN2 to apical membrane of polarized epithelial cells.
dc.description.sponsorshipDéveloppement d'une infrastructure française distribuée pour la métabolomique dédiée à l'innovation - ANR-11-INBS-0010
dc.language.isoen
dc.publisherNature Publishing Group
dc.title.enEnrichment of hydroxylated C24-and C26-acyl-chain sphingolipids mediates PIN2 apical sorting at trans-Golgi network subdomains
dc.typeArticle de revue
dc.identifier.doi10.1038/ncomms12788
dc.subject.halSciences du Vivant [q-bio]
bordeaux.journalNature Communications
bordeaux.page1-15
bordeaux.volume7
bordeaux.peerReviewedoui
hal.identifierhal-01608825
hal.version1
hal.popularnon
hal.audienceNon spécifiée
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01608825v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Nature%20Communications&rft.date=2016&rft.volume=7&rft.spage=1-15&rft.epage=1-15&rft.eissn=2041-1723&rft.issn=2041-1723&rft.au=WATTELET-BOYER,%20Val%C3%A9rie&BROCARD,%20Lysiane&JONSSON,%20Kristoffer&ESNAY,%20Nicolas&JOUBES,%20Jerome&rft.genre=article


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