| http://purl.uniprot.org/citations/18938240 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18938240 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18938240 | http://www.w3.org/2000/01/rdf-schema#comment | "Clathrin-mediated endocytosis is a complex process regulated at many different levels. We showed previously that activation of the angiotensin type 1 receptor (AT1R), which belongs to the G protein-coupled receptor (GPCR) family, leads to c-Src-dependent tyrosine phosphorylation of beta2-adaptin, a subunit of the clathrin adaptor AP-2. The phosphorylation of beta2-adaptin on tyrosine residue 737 (Y737) negatively regulates its interaction with betaarrestin, another important clathrin adaptor for GPCR internalization. Here we sought to determine whether AP-2 phosphorylation represents a general mechanism for different receptors internalizing through the clathrin pathway. Using a specifically designed antibody against the phosphorylated form of Y737 on beta2-adaptin, we demonstrate that this residue is phosphorylated by AT1R in different cell types like HEK293, COS-7 and vascular smooth muscle cells. Using RNA interference approaches, we reveal that this agonist-mediated event is both betaarrestin- and c-Src-dependent, and that it occurs at the plasma membrane in clathrin-coated vesicles (CCVs). We further show that this is not only a common event employed by other GPCRs like the beta2-adrenergic, vasopressin V2, bradykinin type 2, platelet-activating factor and endothelin A receptors but that the epidermal growth factor receptor is capable of eliciting the phosphorylation of AP-2 in CCVs. Our results imply that tyrosine phosphorylation of Y737 on beta2-adaptin is a common regulatory mechanism employed by different receptors undergoing clathrin-dependent endocytosis, and suggest a wider function for this event than originally anticipated."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cellsig.2008.09.013"xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cellsig.2008.09.013"xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/author | "Lee M.-H."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/author | "Lee M.-H."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/author | "Zimmerman B."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/author | "Zimmerman B."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/author | "Luttrell L.M."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/author | "Luttrell L.M."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/author | "Laporte S.A."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/author | "Laporte S.A."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/author | "Simaan M."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/author | "Simaan M."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/name | "Cell. Signal."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/name | "Cell. Signal."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/pages | "103-110"xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/pages | "103-110"xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/title | "c-Src-mediated phosphorylation of AP-2 reveals a general mechanism for receptors internalizing through the clathrin pathway."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/title | "c-Src-mediated phosphorylation of AP-2 reveals a general mechanism for receptors internalizing through the clathrin pathway."xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/volume | "21"xsd:string |
| http://purl.uniprot.org/citations/18938240 | http://purl.uniprot.org/core/volume | "21"xsd:string |