??-Arrestin-1 directly interacts with G??s and regulates its function

摘要

??-Arrestins function to mediate G protein-coupled receptor (GPCR) desensitization and internalization and to initiate G protein independent signaling of GPCRs. Elucidating how ??-arrestin and G protein signal pathways coordinate with each other is important to fully understand GPCR signaling. Here we report that ??-arrestin-1 directly interacts with G??s. Purified ??-arrestin-1 binds to G??s in a rapid association and dissociation manner. ??-Arrestin-1 promotes the binding and the release of GTP??S from G??s in vitro. ??-Arrestin-1 L33K mutant shows reduced interaction with G??s and has no detectable effects on G??s function. Our study thus reveals a direct crosstalk of ??-arrestin-1 with G??s. Structured summary of protein interactions: G??q physically interacts with Beta-arrestin-1 by cross-linking study (View interaction). G??q physically interacts with Beta-arrestin-1 by anti tag coimmunoprecipitation (View interaction). G??s binds to Beta-arrestin-1 by biophysical (View Interaction: 1, 2). G??s physically interacts with Beta-arrestin-1 by anti tag coimmunoprecipitation (View interaction). Beta-arrestin-1 physically interacts with G??s by anti bait coimmunoprecipitation (View interaction). G??s physically interacts with Beta-arrestin-1 by cross-linking study (View interaction). ? 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.