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- W2016060470 abstract "β-arrestin 1 and 2 (also known as arrestin 2 and 3) are homologous adaptor proteins that regulate seven-transmembrane receptor trafficking and signalling. Other proteins with predicted 'arrestin-like' structural domains but lacking sequence homology have been indicated to function like β-arrestin in receptor regulation. We demonstrate that β-arrestin2 is the primary adaptor that rapidly binds agonist-activated β(2) adrenergic receptors (β(2)ARs) and promotes clathrin-dependent internalization, E3 ligase Nedd4 recruitment and ubiquitin-dependent lysosomal degradation of the receptor. The arrestin-domain-containing (ARRDC) proteins 2, 3 and 4 are secondary adaptors recruited to internalized β(2)AR-Nedd4 complexes on endosomes and do not affect the adaptor roles of β-arrestin2. Rather, the role of ARRDC proteins is to traffic Nedd4-β(2)AR complexes to a subpopulation of early endosomes." @default.
- W2016060470 created "2016-06-24" @default.
- W2016060470 creator A5016396161 @default.
- W2016060470 creator A5063246729 @default.
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- W2016060470 date "2012-12-04" @default.
- W2016060470 modified "2023-10-13" @default.
- W2016060470 title "Distinct roles for β‐arrestin2 and arrestin‐domain‐containing proteins in β <sub>2</sub> adrenergic receptor trafficking" @default.
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- W2016060470 doi "https://doi.org/10.1038/embor.2012.187" @default.
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