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. 2024 Nov 25;14:29133. doi: 10.1038/s41598-024-72408-w

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. 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-nc-nd/4.0/.

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Fig. 4 — SLC4A4 knockdown restores the activity of GSK-3β and enhances phosphorylation of β-catenin in Prostate Cancer cells (A) A significant decrease in the total amount of β-catenin was found in shSLC4A4 prostate cancer cells compared to shCON. Meanwhile, the level of GSK-3β was significantly increased due to its reduced phosphorylation on residues Ser21/9 which led to increase phosphorylation (S33/37) of β-catenin (B) Co-immunoprecipitation (Co-IP) experiments showed that endogenous SLC4A4 inhibited the expression of GSK-3β. However, when prostate cancer cells were transfected with the shSLC4A4 plasmid, there was hypophosphorylation of GSK-3β at Ser21/9, which activated the total GSK-3β to degrade endogenous β-catenin (C) qPCR data confirmed the degradation of endogenous β-catenin in shSLC4A4 prostate cancer cells.