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LDIP cooperates with SEIPIN and LDAP to facilitate lipid droplet biogenesis in Arabidopsis

dc.rights.licenseopenen_US
dc.contributor.authorPYC, M.
dc.contributor.authorGIDDA, S.K.
dc.contributor.authorSEAY, D.
dc.contributor.authorESNAY, N.
dc.contributor.authorKRETZSCHMAR, F.K.
dc.contributor.authorCAI, Y.
dc.contributor.authorDONER, N.M.
dc.contributor.authorGREER, M.S.
dc.contributor.authorHULL, J.J.
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorCOULON, Denis
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorBREHELIN, Claire
IDREF: 074179403
dc.contributor.authorYURCHENKO, O.
dc.contributor.authorDE VRIES, J.
dc.contributor.authorVALERIUS, O.
dc.contributor.authorBRAUS, G.H.
dc.contributor.authorISCHEBECK, T.
dc.contributor.authorCHAPMAN, K.D.
dc.contributor.authorDYER, J.M.
dc.contributor.authorMULLEN, R.T.
dc.date.accessioned2022-03-09T13:23:05Z
dc.date.available2022-03-09T13:23:05Z
dc.date.issued2021-09-09
dc.identifier.issn10404651en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/136399
dc.description.abstractEnAbstract Cytoplasmic lipid droplets (LDs) are evolutionarily conserved organelles that store neutral lipids and play critical roles in plant growth, development, and stress responses. However, the molecular mechanisms underlying their biogenesis at the endoplasmic reticulum (ER) remain obscure. Here we show that a recently identified protein termed LD-associated protein [LDAP]-interacting protein (LDIP) works together with both endoplasmic reticulum-localized SEIPIN and the LD-coat protein LDAP to facilitate LD formation in Arabidopsis thaliana. Heterologous expression in insect cells demonstrated that LDAP is required for the targeting of LDIP to the LD surface, and both proteins are required for the production of normal numbers and sizes of LDs in plant cells. LDIP also interacts with SEIPIN via a conserved hydrophobic helix in SEIPIN and LDIP functions together with SEIPIN to modulate LD numbers and sizes in plants. Further, the co-expression of both proteins is required to restore normal LD production in SEIPIN-deficient yeast cells. These data, combined with the analogous function of LDIP to a mammalian protein called LD Assembly Factor 1, are discussed in the context of a new model for LD biogenesis in plant cells with evolutionary connections to LD biogenesis in other eukaryotes.
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subject.enArabidopsis
dc.subject.enArabidopsis proteins
dc.subject.enLipid Droplets
dc.subject.enOrganelle Biogenesis
dc.title.enLDIP cooperates with SEIPIN and LDAP to facilitate lipid droplet biogenesis in Arabidopsis
dc.typeArticle de revueen_US
dc.identifier.doi10.1093/plcell/koab179en_US
dc.subject.halSciences du Vivant [q-bio]en_US
dc.identifier.pubmed34244767en_US
bordeaux.journalPlant Cellen_US
bordeaux.page3076-3103en_US
bordeaux.volume33en_US
bordeaux.hal.laboratoriesLaboratoire de Biogenèse Membranaire (LBM) - UMR 5200en_US
bordeaux.issue9en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.identifier.funderIDCentre National de la Recherche Scientifiqueen_US
bordeaux.identifier.funderIDEuropean Research Councilen_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=Plant%20Cell&rft.date=2021-09-09&rft.volume=33&rft.issue=9&rft.spage=3076-3103&rft.epage=3076-3103&rft.eissn=10404651&rft.issn=10404651&rft.au=PYC,%20M.&GIDDA,%20S.K.&SEAY,%20D.&ESNAY,%20N.&KRETZSCHMAR,%20F.K.&rft.genre=article


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