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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. 1 — Colocalization of catenin proteins with Shank3 in HEK cells. RFP-tagged Shank3 was expressed either alone (upper panel) or coexpressed with Emerald-tagged α-catenin (middle panel) or GFP-tagged δ-catenin (lower panel) in 293T cells, followed by fixation and confocal microscopic analysis. The results show Shank3 presenting in large nuclear and cytosolic clusters, as described previously [24]; no significant overlap between α-catenin and Shank3; and extensive colocalization of δ-catenin and Shank3 at the plasma membrane (while some δ-catenin/Shank3 clusters remain intracellular). Blue: DAPI staining shows nucleus (scale bar 10 µm)