β-Arrestin-1 directly interacts with Gαs and regulates its function
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Updated: May 14, 2026

Parallel Interrogation of β-Arrestin2 Recruitment for Ligand Screening on a GPCR-Wide Scale using PRESTO-Tango Assay
Published on: March 10, 2020
Bo Li1, Congcong Wang, Zhaocai Zhou
1State Key Laboratory of Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Graduate School of the Chinese Academy of Sciences, Shanghai, PR China.
Abstract:
β-Arrestins function to mediate G protein-coupled receptor (GPCR) desensitization and internalization and to initiate G protein independent signaling of GPCRs. Elucidating how β-arrestin and G protein signal pathways coordinate with each other is important to fully understand GPCR signaling. Here we report that β-arrestin-1 directly interacts with Gα(s). Purified β-arrestin-1 binds to Gα(s) in a rapid association and dissociation manner. β-Arrestin-1 promotes the binding and the release of GTPγS from Gα(s) in vitro. β-Arrestin-1 L33K mutant shows reduced interaction with Gα(s) and has no detectable effects on Gα(s) function. Our study thus reveals a direct crosstalk of β-arrestin-1 with Gα(s).
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