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Polycomb Complex 2 Is Required for E-cadherin Repression by the Snail1 Transcription Factor
It is demonstrated that Snail1 recruits PRC2 to the CDH1 promoter and requires the activity of this complex to repress E-cadherin expression.
Guidelines and definitions for research on epithelial–mesenchymal transition
This Consensus Statement is the outcome of a 2-year-long discussion among EMT researchers and aims to both clarify the nomenclature and provide definitions and guidelines for EMT research in future publications to reduce misunderstanding and misinterpretation of research data generated in various experimental models.
p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction.
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.
Transcriptional crosstalk between TGFβ and stem cell pathways in tumor cell invasion: Role of EMT promoting Smad complexes
Current understanding of the mechanisms involved in the transcriptional crosstalk between TGF-β and stem cell pathways are reviewed and how a fundament for the activation of these mechanisms may lead to the induction of EMT in tumors is discussed.
p120 Catenin-Associated Fer and Fyn Tyrosine Kinases Regulate β-Catenin Tyr-142 Phosphorylation and β-Catenin-α-Catenin Interaction
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 Transcriptional Factor Tcf-4 Contains Different Binding Sites for β-Catenin and Plakoglobin*
- S. Miravet, J. Piedra, F. Miró, E. Itarte, A. García de Herreros, M. Duñach
- Biology, ChemistryThe Journal of Biological Chemistry
- 18 January 2002
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.
Phosphorylation Regulates the Subcellular Location and Activity of the Snail Transcriptional Repressor
- D. Domínguez, B. Montserrat-Sentís, A. García de Herreros
- BiologyMolecular and Cellular Biology
- 15 July 2003
These findings show the existence in tumor cells of an effective and fine-tuning nontranscriptional mechanism of regulation of Snail activity dependent on the extracellular environment.
SPARC represses E-cadherin and induces mesenchymal transition during melanoma development.
Findings provide evidence for the role of SPARC in early transformation of melanocytes and identify a novel mechanism, whereby tumor-derived SPARC promotes tumorigenesis by mediating Snail induction and E-cadherin suppression.
Specific Phosphorylation of p120-Catenin Regulatory Domain Differently Modulates Its Binding to RhoA
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.