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- W2063372081 abstract "Arrestin regulates almost all G protein-coupled receptor (GPCR)-mediated signaling and trafficking. We report that the multidomain protein, spinophilin, antagonizes these multiple arrestin functions. Through blocking G protein receptor kinase 2 (GRK2) association with receptor-Gbetagamma complexes, spinophilin reduces arrestin-stabilized receptor phosphorylation, receptor endocytosis, and the acceleration of mitogen-activated protein kinase (MAPK) activity following endocytosis. Spinophilin knockout mice were more sensitive than wild-type mice to sedation elicited by stimulation of alpha2 adrenergic receptors, whereas arrestin 3 knockout mice were more resistant, indicating that the signal-promoting, rather than the signal-terminating, roles of arrestin are more important for certain response pathways. The reciprocal interactions of GPCRs with spinophilin and arrestin represent a regulatory mechanism for fine-tuning complex receptor-orchestrated cell signaling and responses." @default.
- W2063372081 created "2016-06-24" @default.
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- W2063372081 date "2004-06-25" @default.
- W2063372081 modified "2023-10-16" @default.
- W2063372081 title "Spinophilin Blocks Arrestin Actions in Vitro and in Vivo at G Protein-Coupled Receptors" @default.
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- W2063372081 doi "https://doi.org/10.1126/science.1098274" @default.
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