| pubmed-article:10770944 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10770944 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:10770944 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:10770944 | lifeskim:mentions | umls-concept:C0903738 | lld:lifeskim |
| pubmed-article:10770944 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10770944 | lifeskim:mentions | umls-concept:C0009085 | lld:lifeskim |
| pubmed-article:10770944 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:10770944 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:10770944 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:10770944 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:10770944 | lifeskim:mentions | umls-concept:C0167464 | lld:lifeskim |
| pubmed-article:10770944 | pubmed:issue | 30 | lld:pubmed |
| pubmed-article:10770944 | pubmed:dateCreated | 2000-8-31 | lld:pubmed |
| pubmed-article:10770944 | pubmed:abstractText | Beta-arrestins are cytosolic proteins that regulate the signaling and the internalization of G protein-coupled receptors (GPCRs). Although termination of receptor coupling requires beta-arrestin binding to agonist-activated receptors, GPCR endocytosis involves the coordinate interactions between receptor-beta-arrestin complexes and other endocytic proteins such as adaptor protein 2 (AP-2) and clathrin. Clathrin interacts with a conserved motif in the beta-arrestin C-terminal tail; however, the specific molecular determinants in beta-arrestin that bind AP-2 have not been identified. Moreover, the respective contributions of the interactions of beta-arrestin with AP-2 and clathrin toward the targeting of GPCRs to clathrin-coated vesicles have not been established. Here, we identify specific arginine residues (Arg(394) and Arg(396)) in the beta-arrestin 2 C terminus that mediate beta-arrestin binding to AP-2 and show, in vitro, that these domains in beta-arrestin 1 and 2 interact equally well with AP-2 independently of clathrin binding. We demonstrate in HEK 293 cells by fluorescence microscopy that beta(2)-adrenergic receptor-beta-arrestin complexes lacking the beta-arrestin-clathrin binding motif are still targeted to clathrin-coated pits. In marked contrast, receptor-beta-arrestin complexes lacking the beta-arrestin/AP-2 interactions are not effectively compartmentalized in punctated areas of the plasma membrane. These results reveal that the binding of a receptor-beta-arrestin complex to AP-2, not to clathrin, is necessary for the initial targeting of beta(2)-adrenergic receptor to clathrin-coated pits. | lld:pubmed |
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| pubmed-article:10770944 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10770944 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10770944 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10770944 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10770944 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10770944 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10770944 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10770944 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10770944 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10770944 | pubmed:author | pubmed-author:CaronM GMG | lld:pubmed |
| pubmed-article:10770944 | pubmed:author | pubmed-author:HoltJ AJA | lld:pubmed |
| pubmed-article:10770944 | pubmed:author | pubmed-author:BarakL SLS | lld:pubmed |
| pubmed-article:10770944 | pubmed:author | pubmed-author:OakleyR HRH | lld:pubmed |
| pubmed-article:10770944 | pubmed:author | pubmed-author:LaporteS ASA | lld:pubmed |
| pubmed-article:10770944 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10770944 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:10770944 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10770944 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10770944 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10770944 | pubmed:pagination | 23120-6 | lld:pubmed |
| pubmed-article:10770944 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10770944 | pubmed:meshHeading | pubmed-meshheading:10770944... | lld:pubmed |
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| pubmed-article:10770944 | pubmed:meshHeading | pubmed-meshheading:10770944... | lld:pubmed |
| pubmed-article:10770944 | pubmed:meshHeading | pubmed-meshheading:10770944... | lld:pubmed |
| pubmed-article:10770944 | pubmed:meshHeading | pubmed-meshheading:10770944... | lld:pubmed |
| pubmed-article:10770944 | pubmed:meshHeading | pubmed-meshheading:10770944... | lld:pubmed |
| pubmed-article:10770944 | pubmed:meshHeading | pubmed-meshheading:10770944... | lld:pubmed |
| pubmed-article:10770944 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10770944 | pubmed:articleTitle | The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits. | lld:pubmed |
| pubmed-article:10770944 | pubmed:affiliation | Howard Hughes Medical Institute Laboratories and the Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA. | lld:pubmed |
| pubmed-article:10770944 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10770944 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10770944 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:408 | entrezgene:pubmed | pubmed-article:10770944 | lld:entrezgene |
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