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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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Published in: | Nature (London) 1996-08, Vol.382 (6592), p.638-642 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0028-0836 1476-4687 |
DOI: | 10.1038/382638a0 |