Functional characterization of multiple transactivating elements in beta-catenin, some of which interact with the TATA-binding protein in vitro.

@article{Hecht1999FunctionalCO,
  title={Functional characterization of multiple transactivating elements in beta-catenin, some of which interact with the TATA-binding protein in vitro.},
  author={Andreas Hecht and Claudia M Litterst and Otmar Huber and Rolf Kemler},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 25},
  pages={18017-25}
}
beta-Catenin, a member of the family of Armadillo repeat proteins, plays a dual role in cadherin-mediated cell adhesion and in signaling by Wnt growth factors. Upon Wnt stimulation beta-catenin undergoes nuclear translocation and serves as transcriptional coactivator of T cell factor DNA-binding proteins. Previously the transactivation potential of different portions of beta-catenin has been demonstrated, but the precise location of transactivating elements has not been established. Also, the… CONTINUE READING

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