β-Arrestin-1 directly interacts with Gαs and regulates its function

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 Gαs. Purified β-arrestin-1 binds to Gαs in a rapid association and dissociation manner. β-Arrestin-1 promotes the binding and the release of GTPγS from Gαs in vitro. β-Arrestin-1 L33K mutant shows reduced interaction with Gαs and has no detectable effects on Gαs function. Our study thus reveals a direct crosstalk of β-arrestin-1 with Gαs. Structured summary of protein interactionsGαqphysically interacts with Beta-arrestin-1 by cross-linking study (View interaction).Gαqphysically interacts with Beta-arrestin-1 by anti tag coimmunoprecipitation (View interaction).Gαsbinds to Beta-arrestin-1 by biophysical (View Interaction: 1, 2).Gαsphysically interacts with Beta-arrestin-1 by anti tag coimmunoprecipitation (View interaction).Beta-arrestin-1physically interacts with Gαs by anti bait coimmunoprecipitation (View interaction).Gαsphysically interacts with Beta-arrestin-1 by cross-linking study (View interaction).