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. 2017 Jun 7;7:2968. doi: 10.1038/s41598-017-02916-5

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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RXFP1 - G protein interactions and treatment with H2 relaxin or ML290. HEK-RXFP1-Rluc8 cells were transiently co-transfected with Gγ2-Venus, Gβ1 and one of Gα subunits (Gα_s, Gα_oB, Gα_i3). Interactions between RXFP1 and G proteins were detected prior to and after treatment with H2 relaxin (0.1 μM) or ML290 (0.1 μM or 10 μM) using real-time BRET assays. Both ML290 and H2 relaxin induced interactions between RXFP1-Rluc8 and Gα_s, Gα_oB, and to a lesser extent Gα_i3 (A–C). Shifts in BRET ratio between RXFP1 and Gα_s were quantitatively and qualitatively similar with ML290 and H2 relaxin. However the ML290 RXFP1- Gα_oB ligand-induced BRET ratio moved in the opposite direction to that to H2 relaxin (B) suggesting that each ligand induces a different receptor conformation. Interactions between RXFP1 and Gα_i3 with H2 relaxin and ML290 were weak but qualitatively similar. There were no interactions between RXFP1-Rluc8 and Gγ2-Venus in the absence of Gα subunits (D). Ligand-induced BRET ratios were calculated by subtracting the BRET ratio for the vehicle-treated sample from that obtained from each ligand-treated sample as described in Materials and Methods. Data are mean ± SEM of 4 independent experiments.