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. 2022 Oct 20;20:480. doi: 10.1186/s12967-022-03706-y

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© The Author(s) 2022

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. 5 — The variants locating after vitB12-binding domain of Cubilin affected the localization of AMN. A Human 293 T cells co-transfected with eukaryotic transient-expression plasmids (AMN with CUBN, M1-CUBN, M2-CUBN, M3-CUBN and M4-CUBN respectively) indicated the four variants affected Cubilin expression accompanied by abnormal localization of AMN. B Western blot analysis for AMN expression of the co-transfected recombinant plasmids. C and D Co-IP and Duolink proximity ligation assay were used to analysis the protein interaction between AMN and the variants of Cubilin. Each group was tested in triplicate, and the given data are presented as the mean ± S.D. ns, no significant; ***P < 0.001