Xenbase Image ID: 156720

Figure 6. The C Terminus of XSox17β Binds to β-catenin (A) XSox17β binds β-catenin in vitro. 35S-labeled XTcf-3, ΔNXTcf-3, and XSox17β proteins were incubated with 1 μg of GST-β-catenin fusion protein (β-cat) or 1 μg of GST alone, immobilized to agarose beads. Ten percent of the input proteins (i) and bound proteins were resolved on SDS-PAGE and visualized by fluorography. (B) β-catenin binds to the C terminus of XSox17β. The indicated 35S-labeled XSox17β deletion proteins were incubated with GST-β-catenin agarose. Ten percent of the input proteins (i) and the GST-β-catenin bound proteins (b) were resolved on SDS-PAGE and visualized by fluorography. A representative binding experiment is shown. Relative binding of each mutant, summarized from three to four experiments is shown; +++, 60%–100% of wild-type binding; ++, 30%–60%; +, 10%–30%; ±, ∼10%; and −, <10%. (C) XSox17β associates with β-catenin in vivo. 293T cells were transfected with (+) or without (−) S37A-β-catenin-HA (2 μg) and expression plasmids (8 μg) encoding mLEF1-V5, hTCF4-V5, ΔN-hTCF4-V5, XSox17β-V5, or dSox17β 1–150. The top panel shows an anti-V5 Western of the resulting input lysates. Cell lysates were subjected to immunoprecipitation with anti-HA antibody, followed by anti-HA Western to show levels of β-catenin-HA (middle panel) and an anti-V5 epitope Western (bottom panel) to visualize proteins coprecipitating with β-catenin-HA. Image published in: Zorn AM et al. (1999) Copyright © 1999. Image reproduced with permission of the Publisher, Elsevier B. V. Larger Image Printer Friendly View

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