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http://purl.uniprot.org/citations/12163475http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12163475http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12163475http://www.w3.org/2000/01/rdf-schema#comment"Internalization of beta-adrenergic receptors (betaARs) occurs by the sequential binding of beta-arrestin, the clathrin adaptor AP-2, and clathrin. D-3 phosphoinositides, generated by the action of phosphoinositide 3-kinase (PI3K) may regulate the endocytic process; however, the precise molecular mechanism is unknown. Here we demonstrate that betaARKinase1 directly interacts with the PIK domain of PI3K to form a cytosolic complex. Overexpression of the PIK domain displaces endogenous PI3K from betaARK1 and prevents betaARK1-mediated translocation of PI3K to activated beta2ARs. Furthermore, disruption of the betaARK1/PI3K interaction inhibits agonist-stimulated AP-2 adaptor protein recruitment to the beta2AR and receptor endocytosis without affecting the internalization of other clathrin dependent processes such as internalization of the transferrin receptor. In contrast, AP-2 recruitment is enhanced in the presence of D-3 phospholipids, and receptor internalization is blocked in presence of the specific phosphatidylinositol-3,4,5-trisphosphate lipid phosphatase PTEN. These findings provide a molecular mechanism for the agonist-dependent recruitment of PI3K to betaARs, and support a role for the localized generation of D-3 phosphoinositides in regulating the recruitment of the receptor/cargo to clathrin-coated pits."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200202113"xsd:string
http://purl.uniprot.org/citations/12163475http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200202113"xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Caron M.G."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Caron M.G."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Barak L."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Barak L."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Naga Prasad S.V."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Naga Prasad S.V."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Rockman H.A."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Rockman H.A."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Laporte S.A."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Laporte S.A."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Chamberlain D."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/author"Chamberlain D."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/pages"563-575"xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/pages"563-575"xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/title"Phosphoinositide 3-kinase regulates beta2-adrenergic receptor endocytosis by AP-2 recruitment to the receptor/beta-arrestin complex."xsd:string
http://purl.uniprot.org/citations/12163475http://purl.uniprot.org/core/title"Phosphoinositide 3-kinase regulates beta2-adrenergic receptor endocytosis by AP-2 recruitment to the receptor/beta-arrestin complex."xsd:string