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dc.creatorMuñiz Guinea, Manueles
dc.creatorNuoffer, Claudees
dc.creatorHauri, Hans Peteres
dc.creatorRiezman, Howardes
dc.date.accessioned2016-04-19T09:34:40Z
dc.date.available2016-04-19T09:34:40Z
dc.date.issued2000
dc.identifier.issn0021-9525es
dc.identifier.urihttp://hdl.handle.net/11441/40070
dc.description.abstractMembers of the yeast p24 family, including Emp24p and Erv25p, form a heteromeric complex re- quired for the efficient transport of selected proteins from the endoplasmic reticulum (ER) to the Golgi ap- paratus. The specific functions and sites of action of this complex are unknown. We show that Emp24p is di- rectly required for efficient packaging of a lumenal cargo protein, Gas1p, into ER-derived vesicles. Emp24p and Erv25p can be directly cross-linked to Gas1p in ER-derived vesicles. Gap1p, which was not af- fected by emp24 mutation, was not cross-linked. These results suggest that the Emp24 complex acts as a cargo receptor in vesicle biogenesis from the ERes
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherRockefeller University Presses
dc.relation.ispartofJournal of Cell Biology,148 (5), 925-930es
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectCOPII-coated vesiclees
dc.subjectERes
dc.subjectErv25pes
dc.subjectSaccharomyces cerevisiaees
dc.subjectprotein sortinges
dc.titleThe Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicleses
dc.typeinfo:eu-repo/semantics/articlees
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.publisherversion10.1083/jcb.148.5.925es
dc.identifier.doi10.1083/jcb.148.5.925es
dc.identifier.idushttps://idus.us.es/xmlui/handle/11441/40070

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Except where otherwise noted, this item's license is described as: Attribution-NonCommercial-NoDerivatives 4.0 Internacional