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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.
Jagged1 is the pathological link between Wnt and Notch pathways in colorectal cancer
TLDR
Notch activation, accomplished by β-catenin-mediated up-regulation of Jagged1, is required for tumorigenesis in the intestine, and this mechanism is operating in human tumors from Familial Adenomatous Polyposis patients.
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.
Specific Phosphorylation of p120-Catenin Regulatory Domain Differently Modulates Its Binding to RhoA
TLDR
A new regulatory mechanism acting on p120-catenin is uncovered that contributes to the fine-tuned regulation of the RhoA pathways during specific signaling events and results obtained in cell lines support the important role of these phosphorylation sites in the regulation of RHoA activity by p120.
Bcr‐Abl stabilizes β‐catenin in chronic myeloid leukemia through its tyrosine phosphorylation
TLDR
It is shown that Bcr‐Abl levels control the degree of β‐catenin protein stabilization by affecting its Y/S/T‐phospho content in CML cells.
Multivesicular GSK3 sequestration upon Wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6.
TLDR
It is reported that internalization of the GSK3-containing Wnt-signalosome complex into MVBs is dependent on the dissociation of p120-catenin/cadherin from this complex, and this mechanism as cause of β- catenin stabilization by Wnt is supported.
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
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