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- W3005288402 abstract "Binding of arrestin to phosphorylated G-protein-coupled receptors (GPCRs) controls many aspects of cell signaling. The number and arrangement of phosphates may vary substantially for a given GPCR, and these phosphorylation patterns trigger different arrestin-mediated effects. How GPCR phosphorylation influences arrestin behavior, however, remains unclear. Here, we use extensive atomic-level molecular dynamics simulation to determine how phosphorylation patterns affect arrestin binding and conformation. We find that patterns favoring binding differ from those favoring conformational change. Both binding and conformation depend more on the arrangement of phosphates than on their total number, with phosphorylation at different positions sometimes exerting opposite effects. Phosphorylation patterns selectively favor a wide variety of arrestin conformations, differently affecting arrestin sites that scaffold distinct signaling proteins. We also reveal molecular mechanisms of these phenomena. Our results provide a foundation for the rational design of drugs that selectively stimulate desired arrestin-mediated effects by favoring particular GPCR phosphorylation patterns." @default.
- W3005288402 created "2020-02-14" @default.
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- W3005288402 date "2020-02-01" @default.
- W3005288402 modified "2023-09-26" @default.
- W3005288402 title "Determining How GPCR Phosphorylation Patterns Affect Arrestin-Mediated Signaling" @default.
- W3005288402 doi "https://doi.org/10.1016/j.bpj.2019.11.1797" @default.
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