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. 2021 Feb 11;11:3588. doi: 10.1038/s41598-021-82954-2

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© The Author(s) 2021

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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Interaction between Nkx2-5 and Smad4 via the MH2 domain. (A) Myc-tagged Nkx2-5 was co-immunoprecipitated with Flag-tagged Smad4 and detected using anti-Nkx2-5- and anti-Myc-antibodies. (B) Flag-tagged Smad4, and MH1- and MH2- deleted versions, were co-immunoprecipitated with Myc-tagged Nkx2-5 and detected using anti-Smad4 and Flag-antibodies. Nkx2-5 interacts with the Flag-tagged MH2 domain but not the MH1 domain. (C) Subcellular distribution of Flag-tagged Smad4 (upper) and Myc-tagged Nkx2-5 (lower) was determined by western blotting for extracts subcellular fractionated from cytoplasm or nuclei. (D) Interaction of Myc-Nkx2-5 to Flag-Smad4-full length, -MH1, or -MH2 is tested by Co-immunoprecipitation of extracts subcellular fractionated from cytoplasm or nuclei.