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. 2021 Oct 4;8:222. doi: 10.1038/s41438-021-00684-y

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© The Author(s) 2021

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. 5 — A PbrMPK18 interacts with the intracellular domain of PbrCrRLK1L13 in yeast two-hybrid assays. The intracellular domain of PbrCrRLK1L13 fused to the pGADT7 vector and that of PbrMPK18 fused to the pGBKT7 vector. Growth in the medium that lacked Trp, Leu, His, and Ade indicated protein–protein interactions. B PbrMPK18 and PbrCrRLK1L13 interact in the plasma membrane of N. benthamiana leaf epidermal cells in the LCI assay. Fluorescence on the leaf surface indicated protein–protein interactions. C PbrMPK18 and PbrCrRLK1L13 interact in the plasma membrane of N. benthamiana leaf epidermal cells in the BiFC assay. The GFP signal indicates the interaction between PbrMPK18 and PbrCrRLK1L13. Chl represents chloroplast autofluorescence. Merge represents the merged image of GFP, Chl, and bright field. Scale bars = 5 μm