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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 truncation is proteasome dependent. (A) Cytosolic and nuclear lysates from HT29 cells, treated with bortezomib (Borte) were immunoprecipitated for lysine 48 polyubiquitin chain (K48) and probed for N, C and pβ-Cat⁵⁵² epitopes of β-catenin. (B) HT29 cells treated with bortezomib were fractionated to cytosolic (Cyto), membranous (Memb), soluble (Nucl) and chromatin-bound (Chrom) nuclear fractions. WBs were run sequentially for β-catenin antibodies specific for epitopes as indicated. Solid arrows depict decreases in LMW β-catenin with bortezomib. Open arrows depict increases in full length β-catenin after bortezomib treatment. The braces indicate pβ-Cat⁵⁵² likely processed in the nuclear proteasome. α-tubulin is a loading and purity control for cytosolic fraction, histone H3 - for chromatin bound nuclear fraction. Full size membrane scans for WBs can be seen in Suppl. Fig. SS2.