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. 2020 Oct 28;11:85. doi: 10.1186/s13229-020-00385-8

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© The Author(s) 2020

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 4 — Effect of Shank3 N-terminal variants on binding to δ-catenin. a Shank3 WT and variants carrying ASD mutations, as well as Shank1, were coexpressed in 293 cells with GFP-tagged δ-catenin. Cell lysates were subjected to coimmunoprecipitation of GFP-δ-catenin using GFP-trap. b Quantification of the results in A, shown. as the ratio of Shank3 IP/input signals. The L68P mutation significantly increases the binding of δ-catenin to Shank3. Shank1 is also able to interact with δ-catenin via its N-terminal domain (n = 4, one-way ANOVA with Dunnett’s Test, **p < 0.01, mean ± SD). c δ-catenin was coexpressed with RFP-tagged Shank3 WT or variants carrying L68P and P141A mutations; cells were lysed and lysates were subjected to immunoprecipitation using RFP-trap. d Quantification of the results in c, shown as the ratio of GFP-δ-catenin IP/input signals. While the effect of L68P is again significant in improving binding of δ-catenin to Shank3, the de novo mutation P141A slightly (but non-significantly) improves the binding (n = 3, one-way ANOVA with Dunnett’s Test, **p < 0.01, mean ± SD)