p120 Catenin-Associated Fer and Fyn Tyrosine Kinases Regulate β-Catenin Tyr-142 Phosphorylation and β-Catenin-α-Catenin Interaction

@article{Piedra2003p120CF,
  title={p120 Catenin-Associated Fer and Fyn Tyrosine Kinases Regulate $\beta$-Catenin Tyr-142 Phosphorylation and $\beta$-Catenin-$\alpha$-Catenin Interaction},
  author={José A. Piedra and Susana Miravet and Julio Casta{\~n}o and H{\'e}ctor Garc{\'i}a P{\'a}lmer and Nora Heisterkamp and Antonio Garc{\'i}a de Herreros and Mireia Du{\~n}ach},
  journal={Molecular and Cellular Biology},
  year={2003},
  volume={23},
  pages={2287 - 2297}
}
ABSTRACT β-Catenin has a key role in the formation of adherens junction through its interactions with E-cadherin and α-catenin. We show here that interaction of β-catenin with α-catenin is regulated by the phosphorylation of β-catenin Tyr-142. This residue can be phosphorylated in vitro by Fer or Fyn tyrosine kinases. Transfection of these kinases to epithelial cells disrupted the association between both catenins. We have also examined whether these kinases are involved in the regulation of… 
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.
Protein kinase D1-mediated phosphorylation and subcellular localization of beta-catenin.
TLDR
Evidence is provided that PKD1 interacts with and phosphorylates beta-Catenin at Thr(112) and Thr(120) residues in vitro and in vivo and provides a novel strategy to target beta-catenin function in cells including prostate cancer.
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.
α-Catenin overrides Src-dependent activation of β-catenin oncogenic signaling
TLDR
This study reveals for the first time that α-catenin is a key regulator of β-Catenin transcriptional activity and that the status of α- catenin expression in tumor tissues might have prognostic value for Src targeted therapy.
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.
Defining the function of β‐catenin tyrosine phosphorylation in cadherin‐mediated cell–cell adhesion
TLDR
It is demonstrated that tyrosine phosphorylation of β‐catenin might regulate cadherin‐mediated cell adhesion in a more complicated way than previously expected.
Phosphorylated Tyr142 β‐catenin localizes to centrosomes and is regulated by Syk
β‐catenin is a central component of adherent junctions and a key effector of canonical Wnt signaling, in which dephosphorylated Ser/Thr β‐catenin regulates gene transcription. β‐catenin
Identification of β-catenin as a target of the intracellular tyrosine kinase PTK6
TLDR
The ability of PTK6 to negatively regulate β-catenin/TCF transcription by modulating levels of TCF4 and TLE/Groucho could contribute to its growth-inhibitory activities in vivo.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 55 REFERENCES
Tyrosine Phosphorylation of Human Keratinocyte β-Catenin and Plakoglobin Reversibly Regulates their Binding to E-Cadherin and α-Catenin
TLDR
The data raise the possibility that β-catenin or plakoglobin released from the adherens junctions by tyrosine phosphorylation may transduce a signal to the nucleus regarding the adhesive state of the cell.
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.
Beta-catenin interacts with low-molecular-weight protein tyrosine phosphatase leading to cadherin-mediated cell-cell adhesion increase.
TLDR
It is proposed that the stability of cell-cell contacts at the adherens junction level is positively influenced by LMW-PTP expression, mainly because of the beta-catenin and LMW -PTP interaction at the plasma membrane level with consequent dephosphorylation.
α-Catenin Inhibits β-Catenin Signaling by Preventing Formation of a β-Catenin·T-cell Factor·DNA Complex*
TLDR
It is shown that loss of α-catenin expression in a colon cancer cell line correlates with increased Tcf-dependent transcription, and α-Catenin inhibits β-catanin signaling in the nucleus by interfering with the formation of a β- catenin·Tcf·DNA complex.
Phosphorylation and Free Pool of β-Catenin Are Regulated by Tyrosine Kinases and Tyrosine Phosphatases during Epithelial Cell Migration*
Cell migration requires precise control, which is altered or lost when tumor cells become invasive and metastatic. Although the integrity of cell-cell contacts, such as adherens junctions, is
Geldanamycin abrogates ErbB2 association with proteasome-resistant beta-catenin in melanoma cells, increases beta-catenin-E-cadherin association, and decreases beta-catenin-sensitive transcription.
Beta-catenin undergoes both serine and tyrosine phosphorylation. Serine phosphorylation in the amino terminus targets beta-catenin for proteasome degradation, whereas tyrosine phosphorylation in the
Beta-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor
TLDR
It is suggested that catenins represent an important link between EGF-induced signal transduction and cadherin function.
Identification of a new catenin: the tyrosine kinase substrate p120cas associates with E-cadherin complexes.
p120cas is a tyrosine kinase substrate implicated in ligand-induced receptor signaling through the epidermal growth factor, platelet-derived growth factor, and colony-stimulating factor receptors and
The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin
TLDR
Like beta-catenin and plakoglobin, CAS interacts directly with E-cadherin in vivo; however, unlike beta-Cateninand plakemia, CAS does not interact with APC or alpha-catanin.
/-Catenin Mediates the Interaction of the Cadherin-Catenin Complex with Epidermal Growth Factor Receptor
TLDR
The results suggest that catenins represent an important link between EGF-induced signal transduction and cadherin function.
...
1
2
3
4
5
...