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Sphingolipids mediate polar sorting of PIN2 through phosphoinositide consumption at the trans-Golgi network

dc.rights.licenseopenen_US
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorITO, Yoko
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorESNAY, Nicolas
dc.contributor.authorPLATRE, Matthieu Pierre
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorWATTELET-BOYER, Valerie
dc.contributor.authorNOACK, Lise C.
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorFOUGERE, Louise
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMENZEL, Wilhelm
dc.contributor.authorCLAVEROL, Stephane
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorFOUILLEN, Laetitia
ORCID: 0000-0002-1204-9296
IDREF: 136936385
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMOREAU, Patrick
IDREF: 058610723
dc.contributor.authorJAILLAIS, Yvon
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorBOUTTE, Yohann
dc.date.accessioned2022-03-08T09:17:24Z
dc.date.available2022-03-08T09:17:24Z
dc.date.issued2021
dc.identifier.issn20411723en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/136385
dc.description.abstractEnThe lipid composition of organelles acts as a landmark to define membrane identity and specify subcellular function. Phosphoinositides are anionic lipids acting in protein sorting and trafficking at the trans-Golgi network (TGN). In animal cells, sphingolipids control the turnover of phosphoinositides through lipid exchange mechanisms at endoplasmic reticulum/TGN contact sites. In this study, we discover a mechanism for how sphingolipids mediate phosphoinositide homeostasis at the TGN in plant cells. Using multiple approaches, we show that a reduction of the acyl-chain length of sphingolipids results in an increased level of phosphatidylinositol-4-phosphate (PtdIns(4)P or PI4P) at the TGN but not of other lipids usually coupled to PI4P during exchange mechanisms. We show that sphingolipids mediate Phospholipase C (PLC)-driven consumption of PI4P at the TGN rather than local PI4P synthesis and that this mechanism is involved in the polar sorting of the auxin efflux carrier PIN2 at the TGN. Together, our data identify a mode of action of sphingolipids in lipid interplay at the TGN during protein sorting.
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.title.enSphingolipids mediate polar sorting of PIN2 through phosphoinositide consumption at the trans-Golgi network
dc.typeArticle de revueen_US
dc.identifier.doi10.1038/s41467-021-24548-0en_US
dc.identifier.pubmed34257291en_US
bordeaux.journalNature Communicationsen_US
bordeaux.volume12en_US
bordeaux.hal.laboratoriesLaboratoire de Biogenèse Membranaire (LBM) - UMR 5200en_US
bordeaux.issue1en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.identifier.funderIDMinistère de l'Enseignement supérieur, de la Recherche et de l'Innovationen_US
hal.exportfalse
dc.rights.ccCC BYen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Nature%20Communications&rft.date=2021&rft.volume=12&rft.issue=1&rft.eissn=20411723&rft.issn=20411723&rft.au=ITO,%20Yoko&ESNAY,%20Nicolas&PLATRE,%20Matthieu%20Pierre&WATTELET-BOYER,%20Valerie&NOACK,%20Lise%20C.&rft.genre=article


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