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. 2021 Oct 13;40:318. doi: 10.1186/s13046-021-02119-x

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© The Author(s) 2021

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 — SETD1A binds to β-catenin via its SET domain, A, Schematic representation of SETD1A mutants. B, HEK293T cells were cotransfected with the indicated plasmids of Flag-tagged SETD1A mutants and HA-tagged full length β-catenin. Cell lysates were immunoprecipitated with anti-Flag antibody. C, The total, cytoplasmic and nuclear β-catenin levels were detected by western blot analysis following transfection with the empty vector, wild-type SETD1A plasmid and ΔSET plasmid. D, Sphere formation ability was determined following transfection with the empty vector, wild-type SETD1A plasmid and ΔSET plasmid. Scale bar, 100 μm. E, Cisplatin sensitivity was detected by the CCK-8 assay following transfection with the empty vector, wild type SETD1A plasmid and ΔSET plasmid. Data are shown as means ± SD. *P < 0.05, **P < 0.01.