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. 2022 Jan 19;40(2):133–148. doi: 10.1093/stmcls/sxab012

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Published by Oxford University Press 2022.

This work is written by (a) US Government employee(s) and is in the public domain in the US.

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Figure 6. — Disrupted protein distribution and trafficking of β-catenin by mCBM. Immunostaining under confocal imaging shows shifted localization of β-catenin from cell membrane to nucleus/cytosol in mCBM iPSCs (A), although the total protein of β-catenin was not significantly changed (B, Western blot). This alteration was further confirmed through a cell fractionation assay (C), showing the absence of β-catenin blot signal in caveolin-enriched fractions 4/5. Finally, mCBM decreased phosphorylation (Ser33/37/Thr41) of β-catenin in iPSCs (D, quantification for panels B, C, and D is shown in panels E, F, and G, respectively. n = 2-4 in panel A, n = 6-8 in panel B, n = 3 in panel C and D). Data are shown as mean ± SE. ∗P < .05 by Student’s t test.

Figure 6. — Disrupted protein distribution and trafficking of β-catenin by mCBM. Immunostaining under confocal imaging shows shifted localization of β-catenin from cell membrane to nucleus/cytosol in mCBM iPSCs (A), although the total protein of β-catenin was not significantly changed (B, Western blot). This alteration was further confirmed through a cell fractionation assay (C), showing the absence of β-catenin blot signal in caveolin-enriched fractions 4/5. Finally, mCBM decreased phosphorylation (Ser33/37/Thr41) of β-catenin in iPSCs (D, quantification for panels B, C, and D is shown in panels E, F, and G, respectively. n = 2-4 in panel A, n = 6-8 in panel B, n = 3 in panel C and D). Data are shown as mean ± SE. ∗P < .05 by Student’s t test.