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Regulation of E-cadherin/Catenin Association by Tyrosine Phosphorylation*
TLDR
Transient transfections of different mutants demonstrated that Tyr-654 is phosphorylated in conditions in which adherens junctions are disrupted and evidenced that binding ofβ-catenin to E-cadherin in vivo is controlled by phosphorylation of β- catenin Tyr-652.
p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction.
TLDR
Results indicate that p120 catenin acts as a docking protein facilitating the activation of Fer/Fyn tyrosine kinases by Yes and demonstrate the role of these p 120 caten in-associated kinases in the regulation of beta-catenin-alpha-Catenin interaction.
p120 Catenin-Associated Fer and Fyn Tyrosine Kinases Regulate β-Catenin Tyr-142 Phosphorylation and β-Catenin-α-Catenin Interaction
TLDR
Results indicate that p120 catenin acts as a docking protein facilitating the activation of Fer/Fyn tyrosine kinases by Yes and demonstrate the role of these p 120 caten in-associated kinases in the regulation of β-catenin-α-catanin interaction.
Regulation of beta-catenin structure and activity by tyrosine phosphorylation.
TLDR
The results explain how phosphorylation of beta-catenin in Tyr-654 modifies the tertiary structure of this protein and the interaction with its different partners.
The Transcriptional Factor Tcf-4 Contains Different Binding Sites for β-Catenin and Plakoglobin*
TLDR
It is shown here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58–Ser-59– Ser-60, and that simultaneous binding of the two armadillo proteins to TCF-4 is possible.
Regulation of β-Catenin Structure and Activity by Tyrosine Phosphorylation*
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
Regulation of E-cadherin/catenin association by tyrosine phosphorylation.
Santiago Roura, Susana Miravet, José Piedra, Antonio Garcı́a de Herreros, and Mireia Duñach Several concerns were raised about Figs. 3, 4, and 5 by the journal. Because the original data were no
Beta-catenin N- and C-terminal tails modulate the coordinated binding of adherens junction proteins to beta-catenin.
TLDR
The results indicate that different cofactors of beta-catenin bind coordinately to this protein and indicate how the two terminal ends of Beta-Catenin exquisitely modulate intermolecular binding within junctional complexes.
Tyrosine Phosphorylation of Plakoglobin Causes Contrary Effects on Its Association with Desmosomes and Adherens Junction Components and Modulates β-Catenin-Mediated Transcription
TLDR
The results suggest that tyrosine kinases like Src or Fer modulate desmosomes and adherens junctions differently and contribute to the upregulation of the transcriptional activity of the β-catenin-Tcf-4 complex observed in many epithelial tumor cells.
β-Catenin N- and C-terminal Tails Modulate the Coordinated Binding of Adherens Junction Proteins to β-Catenin*
TLDR
The results indicate that different cofactors of β-catenin bind coordinately to this protein and indicate how the two terminal ends ofβ-Catenin exquisitely modulate intermolecular binding within junctional complexes.
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