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. 2022 May 25;13(5):497. doi: 10.1038/s41419-022-04960-0

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© The Author(s) 2022

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — A Top 10 proteins co-precipitated with FAT10 analyzed by LC-MS/MS. #PSMs, peptide spectrum matches. B Mass spectrum showing unique peptides of FOXM1 identified by 2D-LC-MS/MS from the protein lysates prepared from PANC-1 cells following immunoprecipitation with anti-FAT10. C Representative western blot analysis of FAT10 and FOXM1 protein expression in PC and paired paracancerous tissues (T, tumor; NT, non-tumor tissue). D Scatter plots showing a positive correlation between FAT10 and FOXM1 protein expression levels in 40 PC samples (n = 40, r = 0.4642, p = 0.0025, Pearson test). E, F Western blot analyses were used to detect FAT10 and FOXM1 protein expression in cells stably transfected with the shFAT10 or HA-FAT10 plasmid. G Western blot analysis confirming FAT10 silencing and FOXM1 restoration and their effects on EMT-related proteins. H Western blot analysis showing the levels of FAT10 overexpression and FOXM1 inhibition and their effects on EMT-related proteins.