Cadherins mediate both the association between PS1 and beta-catenin and the effects of PS1 on beta-catenin stability.
Presenilin1 (PS1), a protein involved in cellular development, forms functional complexes with beta-catenin, a regulator of Wnt signaling and cell-cell adhesion. In addition, both proteins have been shown to play important roles in disease including cancer and Alzheimer disease. Although PS1 and beta-catenin are found in the same complexes, it ... is not clear whether they bind directly to each other or a third complex component, like cadherin, may mediate their interactions. Here we show that PS1 and beta-catenin form no detectable complexes in cells that express no cadherin. In contrast, these complexes are readily found in E-cadherin containing cells. Furthermore, binding of both PS1 and beta-catenin to E-cadherin is necessary for the formation of PS1/beta-catenin complexes. Importantly, our data show that binding of PS1 to cadherin mediates the effects of PS1 on the phosphorylation, ubiquitination, and destabilization of beta-catenin. Thus, cadherins mediate both the association of PS1 and beta-catenin and the effects of PS1 on the cellular levels of beta-catenin.
Mesh Terms:
Blotting, Western, Cadherins, Cell Adhesion, Cell Line, Tumor, Detergents, Humans, Immunoprecipitation, Macromolecular Substances, Membrane Proteins, Phosphorylation, Plasmids, Presenilin-1, Protein Binding, Protein Structure, Tertiary, Signal Transduction, Transfection, Ubiquitin, beta Catenin
Blotting, Western, Cadherins, Cell Adhesion, Cell Line, Tumor, Detergents, Humans, Immunoprecipitation, Macromolecular Substances, Membrane Proteins, Phosphorylation, Plasmids, Presenilin-1, Protein Binding, Protein Structure, Tertiary, Signal Transduction, Transfection, Ubiquitin, beta Catenin
J. Biol. Chem.
Date: Oct. 28, 2005
PubMed ID: 16126725
View in: Pubmed Google Scholar
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