[HTML][HTML] Regulation of β-catenin structure and activity by tyrosine phosphorylation
J Piedra, D Martınez, J Castano, S Miravet… - Journal of Biological …, 2001 - ASBMB
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 β-catenin C-terminal tail interacts with the armadillo repeat domain …
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 β-catenin C-terminal tail interacts with the armadillo repeat domain …