Functional interaction of beta-catenin with the transcription factor LEF-1.
Behrens, Jurgen; von Kries, Jens P.; Kuhl, Michael; Bruhn, Laurakay; Wedlich, Doris; Grosschedl, Rudolf; Birchmeier, Walter
[Letter] Nature. 382(6592):638-642, August 15, 1996.

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THE cytoplasmic proteins beta-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 beta-catenin. In mammalian cells, coexpressed LEF-1 and beta-catenin form a complex that is localized to the nucleus and can be detected by immunoprecipitation. Moreover, LEF-1 and beta-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 beta-catenin. Thus beta-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.

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