Regulation of β-Catenin Structure and Activity by Tyrosine Phosphorylation*

@article{Piedra2001RegulationO,
  title={Regulation of $\beta$-Catenin Structure and Activity by Tyrosine Phosphorylation*},
  author={José A. Piedra and Daniel Martinez and Julio Casta{\~n}o and Susana Miravet and Mireia Du{\~n}ach and Antonio Garcı́a de Herreros},
  journal={The Journal of Biological Chemistry},
  year={2001},
  volume={276},
  pages={20436 - 20443}
}
β-Catenin plays a dual role as a key effector in the regulation of adherens junctions and as a transcriptional coactivator. Phosphorylation of Tyr-654, a residue placed in the last armadillo repeat of β-catenin, decreases its binding to E-cadherin. We show here that phosphorylation of Tyr-654 also stimulates the association of β-catenin to the basal transcription factor TATA-binding protein. The structural bases of these different affinities were investigated. Our results indicate that the… 

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