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. 2021 Jul 27;12:4541. doi: 10.1038/s41467-021-24731-3

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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. 3 — a Three major interfaces between WLS and Wnt3a and the interaction details. Residues are indicated as one-letter codes here and in all other figures with specific residues highlighted. b Interaction validation between WLS and different Wnt3a variants through co-IP. In total 2.5 µg /well (six-well plate) of plasmids were co-transfected into Hela cells with Wnt3a: WLS DNA ratio at 1:1. Experiments were independently performed for three times with similar results. c Secretion of Wnt variants, detected by western blotting. Experiments were independently performed for three times with similar results. d Signaling activity for different Wnt3a variants. Activity was measured by TOPFlash luciferase reporter assay. Normalized activity for WT Wnt3a is taken as 100%, and activity of Wnt3a mutants is shown as percentage activity compared to WT Wnt3a. 100 ng of Wnt3a DNA per well (24-well plate) was used during transfection. All histograms were generated from n = 3 independent measurements by GraphPad Prism 9. Statistical analysis was performed by two-sided test; mean ± S.D. e Conservation surface of Wnt3a and WLS. The highly conserved regions involved in binding at interfaces are indicated.