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Assembly of the cadherin-catenin complex in vitro with recombinant proteins
- Source :
- Journal of Cell Science. 107:3655-3663
- Publication Year :
- 1994
- Publisher :
- The Company of Biologists, 1994.
-
Abstract
- 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.
- Subjects :
- Macromolecular Substances
Recombinant Fusion Proteins
Molecular Sequence Data
Alpha catenin
Plakoglobin
Biology
Structure-Activity Relationship
Heterotrimeric G protein
Escherichia coli
beta Catenin
Binding Sites
Base Sequence
Cell adhesion molecule
Cadherin
Cell Biology
Cadherins
Fusion protein
Cell biology
Cytoskeletal Proteins
Desmoplakins
Catenin
Trans-Activators
gamma Catenin
Catenin complex
alpha Catenin
Protein Binding
Subjects
Details
- ISSN :
- 14779137 and 00219533
- Volume :
- 107
- Database :
- OpenAIRE
- Journal :
- Journal of Cell Science
- Accession number :
- edsair.doi.dedup.....afc7aabb245f7048de2fcd6f5b165db7