• Corpus ID: 12811565

Regulation of beta-catenin structure and activity by tyrosine phosphorylation.

  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},
  volume={276 23},
beta-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 beta-catenin, decreases its binding to E-cadherin. We show here that phosphorylation of Tyr-654 also stimulates the association of beta-catenin to the basal transcription factor TATA-binding protein. The structural bases of these different affinities were investigated. Our results indicate that… 
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