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. 2022 Nov 12;20:528. doi: 10.1186/s12967-022-03749-1

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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 — MICAL1 promoted WNT pathway by phosphorylating TBC1D1. A, B Silver staining (A) and proteomics mass spectrometry analysis (B) of the proteins associated with MICAL1. C Endogenous immunoprecipitation assays were conducted to verify the inosculation between MICAL1 and TBC1D1. D TBC1D1 and phosphorylated TBC1D1 at Ser660 site were detected in indicated PC cells. E, F TOP/FOP flash assays were conducted to evaluate the effect of TBC1D1 silencing (E) or Ser660 site phosphorylation of TBC1D1 (F) on β-catenin-dependent signaling events. H, I Western blot analysis was conducted to evaluate the effect of TBC1D1 silencing (H) or corresponding plasmid transfection (I) on key proteins of WNT pathway