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. 2018 Mar 15;28(5):529–543. doi: 10.1038/s41422-018-0027-5

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© The Author(s) 2018

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. 3 — RGS1 dynamically interacts with XLG2 and multiple PRRs. (a-c) RGS1 dynamically interacts with FLS2 (a), LYK5 (b), and XLG2 (c). Luciferase complementation assays were performed on Nicotiana benthamiana plants by Agrobacterium-mediated transient expression of the indicated constructs. Relative strength of protein–protein interactions is expressed as arbitrary relative luminescence units (RLU) (mean ± SD; n ≥ 6). Immunoblots show levels of protein accumulation. d RGS1 C-terminus (RGS1CT) interacts with FLS2 kinase domain (FLS2KD) and EFR kinase domain (EFRKD) in vitro. GST pull-down assays were performed with the indicated recombinant proteins. e, f RGS1 C-terminus (RGS1CT) interacts with LYK5 kinase domain (LYK5KD) (e) and XLG2 C-terminus (XLG2CT) (f) in vitro. Protein interactions were examined by GST pull-down assays. The experiments were performed three times with similar results