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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. 2 — a Interaction of catenin proteins with Shank3. 293T cells coexpressing mRFP-Shank3 with GFP-/Emerald-tagged catenin variants were lysed and subjected to immunoprecipitation using RFP-trap. Input and precipitate samples were analysed by Western blotting. The result shows that β- and δ-catenin (but not α-catenin) bind to full length Shank3, while only δ-catenin binds to the Shank3 N-terminal fragment (SPN-Ank). b 293T cells expressing GFP-tagged versions of the proteins indicated were lysed (Input samples) and subjected to a pulldown assay using immobilized His₆-SUMO fusion proteins of the complete Shank3 N-terminus (SPN-Ank), the SUMO control protein or the Ank repeats alone. δ-catenin shows strong, specific binding to the Shank3 N-terminus when compared to the other interaction partners; Fodrin binds to the isolated Ank domain only, whereas HCN1 does not show any binding neither to Ank nor to the SPN-Ank fragment