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. 2018 Jan 12;8:671. doi: 10.1038/s41598-017-18421-8

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© The Author(s) 2018

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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β-catenin serine 552 phosphorylation enhances translocation to chromatin-bound fraction and increases xenograft tumor growth. (A) RKO cells were transfected with FS, ∆∆, FS 552A and ∆∆ 552A β-catenin and fractionated. WBs were probed with anti-Flag antibody. Fibrillarin served as loading and purity controls for chromatin-bound fractions. (B) RKO cell lines overexpressing wild type and mutated β-catenin were co-transfected with TCF/LEF reporter plasmid and luciferase assay performed. *p = 0.002, **p = 0.001, ***p = 0.005. (C) RKO cells were treated with 20nM epoxomicin and cytosolic lysates precipitated with K48 specific antibody. WBs were developed with Flag tag antibody. Actin served as a loading control. (D) Xenograft mice were injected with RKO cells transfected with control and overexpressing β-catenin constructs. The graph represents volumes of developed tumors. *p = 0.016; **p = 0.04; ***p = 0.003. n = 7. Full size membrane scans for WBs can be seen in Suppl. Fig. SS7. (E) Proposed mechanism of β-catenin transcriptional activation.