Specific Phosphorylation of p120-Catenin Regulatory Domain Differently Modulates Its Binding to RhoA

@article{Castao2006SpecificPO,
  title={Specific Phosphorylation of p120-Catenin Regulatory Domain Differently Modulates Its Binding to RhoA},
  author={Julio Casta{\~n}o and Guiomar Solanas and David Casagolda and Imma Raurell and Patricia Villagrasa and Xos{\'e} R. Bustelo and Antonio Garc{\'i}a de Herreros and Mireia Du{\~n}ach},
  journal={Molecular and Cellular Biology},
  year={2006},
  volume={27},
  pages={1745 - 1757}
}
ABSTRACT p120-catenin is an adherens junction-associated protein that controls E-cadherin function and stability. p120-catenin also binds intracellular proteins, such as the small GTPase RhoA. In this paper, we identify the p120-catenin N-terminal regulatory domain as the docking site for RhoA. Moreover, we demonstrate that the binding of RhoA to p120-catenin is tightly controlled by the Src family-dependent phosphorylation of p120-catenin on tyrosine residues. The phosphorylation induced by… 
Interaction of p190RhoGAP with C-terminal Domain of p120-catenin Modulates Endothelial Cytoskeleton and Permeability*
TLDR
A stretch of 23 amino acids within the C-terminal domain of p120 catenin is identified as the minimal sequence responsible for the recruitment of p190RhoGAP, which promotes activation of Rac and down-regulation of Rho signaling, leading to increased endothelial barrier.
PTP-PEST targets a novel tyrosine site in p120 catenin to control epithelial cell motility and Rho GTPase activity
TLDR
The data suggest that PTP-PEST affects epithelial cell motility by controlling the distribution and phosphorylation of p120 and its availability to control Rho GTPase activity.
Wnt controls the transcriptional activity of Kaiso through CK1ε-dependent phosphorylation of p120-catenin
TLDR
Results indicate that, when released from E-cadherin by Wnt3a-stimulated phosphorylation, p120-catenin controls the activity of the Kaiso transcriptional factor, enhancing its binding to repressed promoters and relieving its inhibition of the β- catenin–Tcf-4 transcriptional complex.
A p120-catenin–CK1ε complex regulates Wnt signaling
TLDR
The results demonstrate a novel and crucial function of p120-catenin in Wnt signaling and unveil additional points of regulation by this factor of β-Catenin transcriptional activity different ofβ- catenin stability.
p120-catenin isoform 3 regulates subcellular localization of Kaiso and promotes invasion in lung cancer cells via a phosphorylation-dependent mechanism.
TLDR
It is established that p120-catenin isoform 3 regulates the nuclear export of Kaiso and promotes invasion in lung cancer cells via a phosphorylation-dependent mechanism.
Generation and characterization of a novel phospho-specific monoclonal antibody to p120-catenin serine 879.
To better understand the mechanisms that regulate p120-catenin (p120) and E-cadherin function, we are systematically generating phospho-specific monoclonal antibodies (MAb) to the major p120
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References

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TLDR
Two-dimensional tryptic mapping was employed to directly identify the major sites of Src-induced p120 phosphorylation and identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified.
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.
The Protein-tyrosine Phosphatase SHP-1 Binds to and Dephosphorylates p120 Catenin*
A prominent tyrosine-phosphorylated protein of ∼100 kDa (designated pp100) in epidermal growth factor (EGF)-stimulated A431 cells was found to be a main interaction partner of the protein-tyrosine
P120 Catenin Regulates the Actin Cytoskeleton via Rho Family Gtpases
TLDR
A model in which p120ctn can shuttle between a cadherin-bound state and a cytoplasmic pool in which it can interact with regulators of Rho family GTPases is proposed, which suggests that it is a vehicle for cross-talk between cell–cell junctions and the motile machinery of cells.
Continuous association of cadherin with β-catenin requires the non-receptor tyrosine-kinase Fer
TLDR
It is shown that the phosphorylation of β-catenin is regulated by the combined activities of the tyrosine kinase Fer and the tyosine phosphatase PTP1B, and that expression of wild-type Fer or culture in epidermal growth factor restores the cadherin complex and localization at cell-cell contacts.
Receptor Protein-tyrosine Phosphatase RPTPμ Binds to and Dephosphorylates the Catenin p120 ctn *
TLDR
The findings indicate that RPTPμ interacts with p120 ctn independently of cadherins, and they suggest that this interaction may serve to control the tyrosine phosphorylation state of p 120 ctn at sites of cell-cell contact.
EGFR signaling to p120-catenin through phosphorylation at Y228
TLDR
To clarify the role for EGFR and other tyrosine kinases in regulating p120 function, a new phosphospecific antibody is generated and characterized, as well as a novel siRNA-based reconstitution system for analyzing roles of individual p120 phosphorylation events, which suggest Src family kinases are not necessary intermediates for epidermal growth factor-induced signaling to p120 Y228.
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TLDR
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