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Figure 5. Sox4 and Sox17 have similar affinities for TCF4 and β-catenin, but Sox4 does not form a stable complex. (A) Sox4 has affinities for TCF4 and β-catenin (β-cat) similar to those of Sox17. The ratios of the input (I) and bound (B) protein fractions are similar for Sox17 and Sox4. (B) Sox17 formed a complex with β-catenin and TCF4. Also, more Sox17 protein was pulled down by TCF4-GST beads in the presence of β-catenin. (C) GST-TCF4 beads were able to pull down either β-catenin or Sox4 but did not efficiently pull down Sox4 in the presence of β-catenin. Moreover, Sox4 binding to TCF4 was somewhat inhibited in the presence of β-catenin, suggesting that Sox4 and β-catenin compete for binding. Image published in: Sinner D et al. (2007) Copyright © 2007. Image reproduced with permission of the Publisher, American Society for Cell Biology (ASCB). This is an Open Access article. Larger Image Printer Friendly View

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