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| http://purl.uniprot.org/citations/18523139 | http://www.w3.org/2000/01/rdf-schema#comment | "The internalization properties of the alpha1a- and alpha1b-adrenergic receptors (ARs) subtypes transiently expressed in human embryonic kidney (HEK) 293 cells were compared using biotinylation experiments and confocal microscopy. Whereas the alpha1b-AR displayed robust agonist-induced endocytosis, the alpha1a-AR did not. Constitutive internalization of the alpha1a-AR was negligible, whereas the alpha1b-AR displayed significant constitutive internalization and recycling. We investigated the interaction of the alpha1-AR subtypes with beta-arrestins 1 and 2 as well as with the AP50 subunit of the clathrin adaptor complex AP2. The results from both coimmunoprecipitation experiments and beta-arrestin translocation assays indicated that the agonistinduced interaction of the alpha1a-AR with beta-arrestins was much weaker than that of the alpha1b-AR. In addition, the alpha1a-AR did not bind AP50. The alpha1b-AR mutant M8, lacking the main phosphorylation sites in the receptor C tail, was unable to undergo endocytosis and was profoundly impaired in binding beta-arrestins despite its binding to AP50. In contrast, the alpha1b-AR mutant DeltaR8, lacking AP50 binding, bound beta-arrestins efficiently, and displayed delayed endocytosis. RNA interference showed that beta-arrestin 2 plays a prominent role in alpha1b-AR endocytosis. The findings of this study demonstrate differences in internalization between the alpha1a- and alpha1b-AR and provide evidence that the lack of significant endocytosis of the alpha1a-AR is linked to its poor interaction with beta-arrestins as well as with AP50. We also provide evidence that the integrity of the phosphorylation sites in the C tail of the alpha1b-AR is important for receptor/beta-arrestin interaction and that this interaction is the main event triggering receptor internalization."xsd:string |
| http://purl.uniprot.org/citations/18523139 | http://purl.org/dc/terms/identifier | "doi:10.1124/mol.107.043422"xsd:string |
| http://purl.uniprot.org/citations/18523139 | http://purl.uniprot.org/core/author | "Cotecchia S."xsd:string |
| http://purl.uniprot.org/citations/18523139 | http://purl.uniprot.org/core/author | "Abuin L."xsd:string |
| http://purl.uniprot.org/citations/18523139 | http://purl.uniprot.org/core/author | "Dey J."xsd:string |
| http://purl.uniprot.org/citations/18523139 | http://purl.uniprot.org/core/author | "Stanasila L."xsd:string |
| http://purl.uniprot.org/citations/18523139 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18523139 | http://purl.uniprot.org/core/name | "Mol Pharmacol"xsd:string |
| http://purl.uniprot.org/citations/18523139 | http://purl.uniprot.org/core/pages | "562-573"xsd:string |
| http://purl.uniprot.org/citations/18523139 | http://purl.uniprot.org/core/title | "Different internalization properties of the alpha1a- and alpha1b-adrenergic receptor subtypes: the potential role of receptor interaction with beta-arrestins and AP50."xsd:string |
| http://purl.uniprot.org/citations/18523139 | http://purl.uniprot.org/core/volume | "74"xsd:string |
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