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. 2023 Aug 28;13:14054. doi: 10.1038/s41598-023-41008-5

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Mutation localized in the β1 propeller domain of LRP4 inhibits its binding to Wnt11 in vitro. (A) Wild-type (WT) or mutant (Mut) LRP4/Wnt11 co-culture and immunoprecipitation experiment. (B) Immunoprecipitation of LRP4-HA with Wnt11-Myc in COS7/HEK293T co-culture. Western blot using anti-HA and anti-Myc antibodies were realized on cell lysates in order to estimate the effect of the mutation in LRP4 on its binding to Wnt11. (C) Wnt11 binding to mutated LRP4 shows a significant decrease compared with control. N = 3 co-culture and immunoprecipitation for each condition. p < 0.05, Student’s test. Source data are provided as a Source Data file. For A the figure was drawn by using BioRender.com.