Xenbase Image ID: 158076

Figure 4 Phosphorylation of the amino-terminal region of β-catenin is necessary and sufficient for recognition by β-Trcp in vitro. (A) Schematic diagram of the wild-type and mutant derivatives of β-catenin. The four critical serine/threonine residues (S33, S37, T41, and S45), alanine substitutions of these residues in the S→A mutant, and surrounding residues are highlighted. Note that the Arm-repeat region that is required for Axin or TCF binding starts from residue 131. (B) Phosphorylation of β-catenin and its mutant derivatives (as GST-fusion proteins) by purified recombinant GSK-3β. Note that GST was not a substrate for GSK-3β. (C) On phosphorylation, N1, N2, and N3, but not β-catenin (S→A) were effectively recognized by β-Trcp. Lanes 1 and 13 represent 50% input of 35S-labeled β-Trcp in each GST-pull-down assay. Image published in: Liu C et al. (1999) Copyright © 1999. Image reproduced with permission of the publisher and the copyright holder. This is an Open Access article distributed under the terms of the Creative Commons Attribution License. Larger Image Printer Friendly View

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