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dc.creatorRodríguez Gallardo, Sofíaes
dc.creatorSabido Bozo, Susanaes
dc.creatorIkeda, Atsukoes
dc.creatorAraki, Misakoes
dc.creatorOkazaki, Koutaes
dc.creatorNakano, Miyakoes
dc.creatorAguilera Romero, María Auxiliadoraes
dc.creatorCortés Gómez, Alejandroes
dc.creatorLópez Martín, Sergioes
dc.creatorWaga, Mihoes
dc.creatorNakano, Akihikoes
dc.creatorKurokawa, Kazuoes
dc.creatorMuñiz Guinea, Manueles
dc.creatorFunato, Kouichies
dc.date.accessioned2022-05-23T15:21:35Z
dc.date.available2022-05-23T15:21:35Z
dc.date.issued2022
dc.identifier.citationRodríguez Gallardo, S., Sabido Bozo, S., Ikeda, A., Araki, M., Okazaki, K., Nakano, M.,...,Funato, K. (2022). Quality-controlled ceramide-based GPI-anchored protein sorting into selective ER exit sites. Cell Reports, 39 (5), 110768.
dc.identifier.issn2211-1247es
dc.identifier.urihttps://hdl.handle.net/11441/133541
dc.description.abstractGlycosylphosphatidylinositol-anchored proteins (GPI-APs) exit the endoplasmic reticulum (ER) through a specialized export pathway in the yeast Saccharomyces cerevisiae. We have recently shown that a very-long acyl chain (C26) ceramide present in the ER membrane drives clustering and sorting of GPI-APs into selective ER exit sites (ERES). Now, we show that this lipid-based ER sorting also involves the C26 ceramide as a lipid moiety of GPI-APs, which is incorporated into the GPI anchor through a lipid-remodeling process after protein attachment in the ER. Moreover, we also show that a GPI-AP with a C26 ceramide moiety is monitored by the GPI-glycan remodelase Ted1, which, in turn, is required for receptor-mediated export of GPI-APs. Therefore, our study reveals a quality-control system that ensures lipid-based sorting of GPI-APs into selective ERESs for differential ER export, highlighting the physiological need for this specific export pathway.es
dc.description.sponsorshipJapan Society for the Promotion of Science JP19H02922, JP25221103, JP17H06420, JP18H0527es
dc.description.sponsorshipMinisterio de Ciencia e Innovación PID2020-119505GB-I00, AEI/10.13039/501100011033es
dc.description.sponsorshipJunta de Andalucía ERDF PY20_01240, US- 1380893es
dc.description.sponsorshipUniversidad de Sevilla VIPPIT-2020-I.5es
dc.formatapplication/pdfes
dc.format.extent16 p.es
dc.language.isoenges
dc.publisherElsevieres
dc.relation.ispartofCell Reports, 39 (5), 110768.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectCeramide remodelinges
dc.subjectCP: Cell biologyes
dc.subjectCP: Molecular biologyes
dc.subjectEndoplasmic reticulumes
dc.subjectGlycan remodelinges
dc.subjectGPI-anchored proteines
dc.subjectProtein sortinges
dc.subjectQuality controles
dc.subjectYeast Saccharomyces cerevisiaees
dc.titleQuality-controlled ceramide-based GPI-anchored protein sorting into selective ER exit siteses
dc.typeinfo:eu-repo/semantics/articlees
dcterms.identifierhttps://ror.org/03yxnpp24
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Biología Celulares
dc.relation.projectIDJP19H02922es
dc.relation.projectIDJP25221103es
dc.relation.projectIDJP17H06420es
dc.relation.projectIDJP18H0527es
dc.relation.projectIDPID2020-119505GB-I00es
dc.relation.projectIDAEI/10.13039/501100011033es
dc.relation.projectIDERDF PY20_01240es
dc.relation.projectIDUS- 1380893es
dc.relation.projectIDVIPPIT-2020-I.5es
dc.relation.publisherversionhttps://doi.org/10.1016/j.celrep.2022.110768es
dc.identifier.doi10.1016/j.celrep.2022.110768es
dc.journaltitleCell Reportses
dc.publication.volumen39es
dc.publication.issue5es
dc.publication.initialPage110768es
dc.contributor.funderSociety for the Promotion of Science. Japanes
dc.contributor.funderAgencia Estatal de Investigación. Españaes
dc.contributor.funderJunta de Andalucíaes
dc.contributor.funderUniversidad de Sevillaes
dc.description.awardwinningPremio Anual Publicación Científica Destacada de la US. Facultad de Biología

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