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Assembly of the cadherin-catenin complex in vitro with recombinant proteins
H. Aberle, S. Butz, J. Stappert, H. Weissig, R. Kemler, H. Hoschuetzky
Journal of Cell Science 1994 107: 3655-3663;

Summary

The cytoplasmic domain of classical cadherins is tightly associated with three proteins termed alpha-, beta- and gamma-catenin. These accessory proteins are of central importance for the adhesive properties of this class of cell adhesion molecules. In order to examine the molecular architecture of the cadherin-catenin complex in more detail we have expressed the catenins and the cytoplasmic domain of E-cadherin as fusion proteins in Escherichia coli, and analyzed the interaction of purified recombinant cadherin and catenins in combinatorial protein-protein interaction experiments. The cytoplasmic domain of E-cadherin cannot directly associate with alpha-catenin but interacts with high affinity with beta-catenin, whereas the binding of gamma-catenin (plakoglobin) to E-cadherin is less efficient. alpha- and beta-catenin assemble into a 1:1 heterodimeric complex. The analysis of various truncated beta-catenins revealed that an alpha-catenin binding site in beta-catenin is localized between amino acid positions 120 and 151. The central role of beta-catenin for the assembly of the heterotrimeric E-cadherin/alpha-catenin/beta-catenin complex in mixing experiments with all components was demonstrated. The reconstitution in vitro of the cadherin-catenin complex should allow the study of the interaction with signalling molecules and with the actin-based cytoskeleton.

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Journal Articles
Assembly of the cadherin-catenin complex in vitro with recombinant proteins
H. Aberle, S. Butz, J. Stappert, H. Weissig, R. Kemler, H. Hoschuetzky
Journal of Cell Science 1994 107: 3655-3663;
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