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. 2018 Nov 19;9(12):1146. doi: 10.1038/s41419-018-1164-y

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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. 2 — a, b Interaction between endogenous EphA2 with Dvl2 or Axin1 in AGS cells. Western blotting of cell lysates subjected to co-IP with indicated antibodies against EphA2, Dvl2 or Axin1. c, d BiFC signal analysis by fluorescence microscopy after transient co-expression of c VN-EphA2 and VC-Dvl2 and d VN-EphA2 and VC-Axin1 in HEK293 cells. e, f Proximity ligation assays (PLA) for EphA2 and Dvl2/Axin1. Interaction between endogenous EphA2 with Dvl2 (e) or Axin1 (f) in AGS cells. g, h Interaction between endogenous EphA2 and Axin1 in AGS cells transfected with Flag-Dvl2 expression vector (g) and si-Dvl2 (h) and analyzed by co-IP using anti-EphA2. Relative accumulations of proteins in different groups compared with the negative control group are indicated. Significant differences were determined with the Student’s t-test. *P < 0.05, **P < 0.01 compared with control group