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http://purl.uniprot.org/citations/15229321http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15229321http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15229321http://www.w3.org/2000/01/rdf-schema#comment"FcgammaRI depends for its biological function on both the intracellular domain of the alpha-chain and associated Fc receptor (FcR) gamma-chains. However, functional protein effectors of FcgammaRI's intracellular domain have not been identified. In this study, we identified periplakin (PPL) as a selective interacting protein for the intracellular tail of FcgammaRI but no other activatory FcRs. The interaction was confirmed by coimmunoprecipitation and blot-overlay assays. PPL and FcgammaRI colocalized at the plasma membrane in monocytes and cell transfectants, and both were up-regulated by IFN-gamma. By expressing C-terminal PPL in transfectants, we established a pivotal role for this protein in FcgammaRI ligand binding, endocytosis, and antigen presentation. These data illustrate that intracellular protein interactions with a multisubunit FcR alpha-chain can confer unique properties to the receptor."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0401217101"xsd:string
http://purl.uniprot.org/citations/15229321http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0401217101"xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/author"van de Winkel J.G.J."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/author"van de Winkel J.G.J."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/author"Beekman J.M."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/author"Beekman J.M."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/author"Leusen J.H.W."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/author"Leusen J.H.W."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/author"Bakema J.E."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/author"Bakema J.E."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/pages"10392-10397"xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/pages"10392-10397"xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/title"Direct interaction between FcgammaRI (CD64) and periplakin controls receptor endocytosis and ligand binding capacity."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/title"Direct interaction between FcgammaRI (CD64) and periplakin controls receptor endocytosis and ligand binding capacity."xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/volume"101"xsd:string
http://purl.uniprot.org/citations/15229321http://purl.uniprot.org/core/volume"101"xsd:string
http://purl.uniprot.org/citations/15229321http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15229321
http://purl.uniprot.org/citations/15229321http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15229321