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. 2023 Aug 9;14:4808. doi: 10.1038/s41467-023-40482-9

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© The Author(s) 2023

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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Fig. 6 — a Schematic representation of intramolecular BRET-based sensors of βarr2 conformation where the N-terminus of βarr2 harbors R-Luc (Renilla luciferase) as the BRET donor, and the FlAsH motif are engineered at indicated positions in βarr2 as BRET acceptor. The structural representation in the lower panel is designed based on alpha fold generated model of βarr2. b CXCL12-induced BRET signal measured in HEK-293 cells expressing the indicated receptor and sensor constructs (mean ± SEM), n = 6 independent experiments; the difference of the net-BRET ratio between the stimulated and unstimulated condition were plotted, Two-way ANOVA, Sidak’s multiple comparison test. The exact p-values are as follows: F1:CXCR4 vs. F1:CXCR7 (p = 0.9746), F2:CXCR4 vs. F2:CXCR7 (p > 0.9999), F3:CXCR4 vs. F3:CXCR7 (p = 0.9991), F4:CXCR4 vs. F4:CXCR7 (0.0010), F5:CXCR4 vs. F5:CXCR7 (p = 0.9052), F6:CXCR4 vs. F6:CXCR7 (p = 0.0420) (*p < 0.05, **p < 0.01, ns non-significant). Source data are provided as a source data file.