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. 2009 Jan 30;284(5):3323–3333. doi: 10.1074/jbc.M808048200

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Copyright © 2009, The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 4. — Sox9 nuclear localization is both necessary and sufficient to promote β-catenin degradation. A and B, CHO cells were transiently transfected with β-CATENIN-HA and a cytoplasmic mutant, Sox9-NLS^*-Flag (top panel) or a nuclear mutant, Sox9-NLS^*-NLS(TA)-Flag (bottom panel). Cells were stained with anti-HA (green) and anti-FLAG (red) antibodies (A) or analyzed by Western blot (B). Tubulin was used as a loading control. C and D, CHO cells were transiently transfected with β-CATENIN-HA and with a cytoplasmic mutant, Sox9HMG-Flag (top panel), or a nuclear mutant, Sox9HMG-NLS(TA)(bottom panel). Immunofluorescent staining and Western blot analysis was performed 24 h later as in A and B. Lanes 1 and 2 were put together with lanes 3 and 4 by deleting irrelevant lanes in between on the same membrane. E, CHO cells were transiently transfected with the indicated plasmids and TOPFLASH activity was measured 24 h later. IB, immunoblot.

Inline graphic — Sox9 nuclear localization is both necessary and sufficient to promote β-catenin degradation. A and B, CHO cells were transiently transfected with β-CATENIN-HA and a cytoplasmic mutant, Sox9-NLS^*-Flag (top panel) or a nuclear mutant, Sox9-NLS^*-NLS(TA)-Flag (bottom panel). Cells were stained with anti-HA (green) and anti-FLAG (red) antibodies (A) or analyzed by Western blot (B). Tubulin was used as a loading control. C and D, CHO cells were transiently transfected with β-CATENIN-HA and with a cytoplasmic mutant, Sox9HMG-Flag (top panel), or a nuclear mutant, Sox9HMG-NLS(TA)(bottom panel). Immunofluorescent staining and Western blot analysis was performed 24 h later as in A and B. Lanes 1 and 2 were put together with lanes 3 and 4 by deleting irrelevant lanes in between on the same membrane. E, CHO cells were transiently transfected with the indicated plasmids and TOPFLASH activity was measured 24 h later. IB, immunoblot.