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http://purl.uniprot.org/citations/10499588http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10499588http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10499588http://www.w3.org/2000/01/rdf-schema#comment"A fundamental question in cell biology is how membrane proteins are sorted in the endocytic pathway. The sorting of internalized beta2-adrenergic receptors between recycling endosomes and lysosomes is responsible for opposite effects on signal transduction and is regulated by physiological stimuli. Here we describe a mechanism that controls this sorting operation, which is mediated by a family of conserved protein-interaction modules called PDZ domains. The phosphoprotein EBP50 (for ezrinradixin-moesin(ERM)-binding phosphoprotein-50) binds to the cytoplasmic tail of the beta2-adrenergic receptor through a PDZ domain and to the cortical actin cytoskeleton through an ERM-binding domain. Disrupting the interaction of EBP50 with either domain or depolymerization of the actin cytoskeleton itself causes missorting of endocytosed beta2-adrenergic receptors but does not affect the recycling of transferrin receptors. A serine residue at position 411 in the tail of the beta2-adrenergic receptor is a substrate for phosphorylation by GRK-5 (for G-protein-coupled-receptor kinase-5) and is required for interaction with EBP50 and for proper recycling of the receptor. Our results identify a new role for PDZ-domain-mediated protein interactions and for the actin cytoskeleton in endocytic sorting, and suggest a mechanism by which GRK-mediated phosphorylation could regulate membrane trafficking of G-protein-coupled receptors after endocytosis."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.org/dc/terms/identifier"doi:10.1038/45816"xsd:string
http://purl.uniprot.org/citations/10499588http://purl.org/dc/terms/identifier"doi:10.1038/45816"xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/author"von Zastrow M."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/author"von Zastrow M."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/author"Bretscher A."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/author"Bretscher A."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/author"Cao T.T."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/author"Cao T.T."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/author"Deacon H.W."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/author"Deacon H.W."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/author"Reczek D."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/author"Reczek D."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/pages"286-290"xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/pages"286-290"xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/title"A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/title"A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor."xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/volume"401"xsd:string
http://purl.uniprot.org/citations/10499588http://purl.uniprot.org/core/volume"401"xsd:string