Hot spots in β-catenin for interactions with LEF-1, conductin and APC View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-09-01

AUTHORS

Jens Peter von Kries, Georgia Winbeck, Christian Asbrand, Thomas Schwarz-Romond, Natalia Sochnikova, Andrea Dell'Oro, Jürgen Behrens, Walter Birchmeier

ABSTRACT

Interactions between beta-catenin and LEF-1/TCF, APC and conductin/axin are essential for wnt-controlled stabilization of beta-catenin and transcriptional activation. The wnt signal transduction pathway is important in both embryonic development and tumor progression. We identify here amino acid residues in beta-catenin that distinctly affect its binding to LEF-1/TCF, APC and conductin. These residues form separate surface clusters, termed hot spots, along the armadillo superhelix of beta-catenin. We also show that complementary charged and hydrophobic amino acids are required for formation of the bipartite beta-catenin-LEF-1 transcription factor. Moreover, we demonstrate that conductin/axin binding to beta-catenin is essential for beta-catenin degradation, and that APC acts as a cofactor of conductin/axin in this process. Binding of APC to conductin/axin activates the latter and occurs between their SAMP and RGS domains, respectively. More... »

PAGES

nsb0900_800

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/79039

DOI

http://dx.doi.org/10.1038/79039

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1023944848

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10966653


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