Fig. 1. Delineation of the domains mediating mutual interactions between T-catenin and plakophilins (PKP3 and PKP2). Yeast two-hybrid analysis was performed on various deletion mutants of (A) T-catenin (yellow), (B) PKP3 (blue) and (C) PKP2 (purple). We also used a chimeric construct in which the amino-terminal half of T-catenin was replaced with that of E-catenin (green; row A.6). Each open reading frame (T-catenin, PKP3 and PKP2) was fused to the GAL4-DNA binding domain (DBD, grey boxes) or to the GAL4-activating domain (AD, white boxes). The narrowed down interacting domains are depicted at the bottom in red. Amino acid residue (AA) numbers indicate the positions of the corresponding domains. VH, vinculin homology domain; AMD, adhesion modulation domain; N, amino terminus; C, carboxyl terminus.