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Functional interaction of β-catenin with the transcription factor LEF-1

THE cytoplasmic proteins β-catenin of vertebrates and armadillo of Drosophila have two functions: they link the cadherin cell-adhesion molecules to the cytoskeleton 1–4 , and they participate in the wnt/wingless signalling pathway 5–7 . Here we show, in a yeast two-hybrid screen, that the architectu...

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Bibliographic Details
Published in:Nature (London) 1996-08, Vol.382 (6592), p.638-642
Main Authors: Behrens, Jürgen, von Kries, Jens P, Kühl, Michael, Bruhn, Laurakay, Wedlich, Doris, Grosschedl, Rudolf, Birchmeier, Walter
Format: Article
Language:English
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Summary:THE cytoplasmic proteins β-catenin of vertebrates and armadillo of Drosophila have two functions: they link the cadherin cell-adhesion molecules to the cytoskeleton 1–4 , and they participate in the wnt/wingless signalling pathway 5–7 . Here we show, in a yeast two-hybrid screen, that the architectural transcription factor LEF-1 (for lymphoid enhancer-binding factor) 8–10 interacts with β-catenin. In mammalian cells, coexpressed LEF-1 and β-catenin form a complex that is localized to the nucleus and can be detected by immunoprecipitation. Moreover, LEF-1 and β-catenin form a ternary complex with DNA that displays an altered DNA bend. Microinjection of LEF-1 into Xenopus embryos induces axis duplication, which is augmented by interaction with β-catenin. Thus β-catenin regulates gene expression by direct interaction with transcription factors such as LEF-1, providing a molecular mechanism for the transmission of signals from cell-adhesion components or wnt protein to the nucleus.
ISSN:0028-0836
1476-4687
DOI:10.1038/382638a0