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Your search keyword '"Inglés-Esteve, Julia"' showing total 18 results
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18 results on '"Inglés-Esteve, Julia"'

1. The Notch/Hes1 Pathway Sustains NF-κB Activation through CYLD Repression in T Cell Leukemia

Author

Espinosa, Lluis, Cathelin, Severine, D'Altri, Teresa, Trimarchi, Thomas, Statnikov, Alexander, Guiu, Jordi, Rodilla, Veronica, Inglés-Esteve, Julia, Nomdedeu, Josep, Bellosillo, Beatriz, Besses, Carles, Abdel-Wahab, Omar, Kucine, Nicole, Sun, Shao-Cong, Song, Guangchan, Mullighan, Charles C., Levine, Ross L., Rajewsky, Klaus, Aifantis, Iannis, and Bigas, Anna

Published
2010
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5. Inhibition of Specific NF-κB Activity Contributes to the Tumor Suppressor Function of 14-3-3σ in Breast Cancer

Author

Inglés-Esteve, Julia, primary, Morales, Mònica, additional, Dalmases, Alba, additional, Garcia-Carbonell, Ricard, additional, Jené-Sanz, Alba, additional, López-Bigas, Núria, additional, Iglesias, Mar, additional, Ruiz-Herguido, Cristina, additional, Rovira, Ana, additional, Rojo, Federico, additional, Albanell, Joan, additional, Gomis, Roger R., additional, Bigas, Anna, additional, and Espinosa, Lluís, additional

Published
2012
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15. Differential effects of anti‐CD45 monoclonal antibody on human B cell proliferation: a monoclonal antibody recognizing a neuraminidase‐sensitive epitope of the T200 molecule enhances anti‐immunoglobulin‐induced proliferation

Author

Alsinet, Emili, primary, Inglés‐Esteve, Julia, additional, Vilella, Ramón, additional, Lozano, Francisco, additional, Milá, Jordi, additional, Rojo, Isabel, additional, Martorell, Jaume, additional, Vives, Jordi, additional, and Gayá, Antoni, additional

Published
1990
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16. Efficient nuclear export of p65-IκBα complexes requires 14-3-3 proteins.

Author

Aguilera, Cristina, Fernández-Majada, Vanessa, Inglés-Esteve, Julia, Rodilla, Verónica, Bigas, Anna, and Espinosa, Lluís

Subjects
CYTOPLASM, PROTEINS, GENE transfection, CHROMATIN, GENES
Abstract

IκB are responsible for maintaining p65 in the cytoplasm under non-stimulating conditions and promoting the active export of p65 from the nucleus following NFκB activation to terminate the signal. We now show that 14-3-3 proteins regulate the NFκB signaling pathway by physically interacting with p65 and IκBα proteins. We identify two functional 14-3-3 binding domains in the p65 protein involving residues 38-44 and 278-283, and map the interaction region of IκBα in residues 60-65. Mutation of these 14-3-3 binding domains in p65 or IκBα results in a predominantly nuclear distribution of both proteins. TNFα treatment promotes recruitment of 14-3-3 and IκBα to NFκB-dependent promoters and enhances the binding of 14-3-3 to p65. Disrupting 14-3-3 activity by transfection with a dominant-negative 14-3-3 leads to the accumulation of nuclear p65-IκBα complexes and the constitutive association of p65 with the chromatin. In this situation, NFκB-dependent genes become unresponsive to TNFα stimulation. Together our results indicate that 14-3-3 proteins facilitate the nuclear export of IκBα-p65 complexes and are required for the appropriate regulation of NFκB signaling. [ABSTRACT FROM AUTHOR]

Published
2006
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18. Phosphorylation by glycogen synthase kinase-3 beta down-regulates Notch activity, a link for Notch and Wnt pathways.

Author

Espinosa L, Inglés-Esteve J, Aguilera C, and Bigas A

Subjects
Ankyrin Repeat, Base Sequence, DNA Primers, Glycogen Synthase Kinase 3 beta, Phosphorylation, Promoter Regions, Genetic, Receptor, Notch2, Receptors, Cell Surface antagonists & inhibitors, Saccharomyces cerevisiae Proteins metabolism, Subcellular Fractions enzymology, Wnt Proteins, Wnt1 Protein, Down-Regulation, Glycogen Synthase Kinase 3 metabolism, Proto-Oncogene Proteins metabolism, Receptors, Cell Surface metabolism, Zebrafish Proteins
Abstract

Phosphorylation of Notch proteins has been indirectly correlated with Notch activation and nuclear translocation as well as cellular transformation. There is evidence that the Wnt signaling pathway, which results in glycogen synthase kinase-3 beta (GSK-3 beta) inhibition, cross-talks with the Notch pathway. In this study, we show that GSK-3 beta is able to bind and phosphorylate Notch2 in vitro and in vivo. We identify three specific phosphorylation sites in the Notch2 serine/threonine-rich domain that are dependent on GSK-3 beta activity. Phosphorylation of the serine/threonine-rich domain has been shown previously to be crucial in regulating cytokine-specific cell differentiation. Coimmunoprecipitation experiments show that full-length Notch2 binds more efficiently than intracellular Notch2 to GSK-3 beta. Nevertheless, only the processed Notch2 is a substrate for the kinase, thus suggesting that GSK-3 beta-dependent phosphorylation may be specifically regulating the activated Notch molecule. Consistent with this, GSK-3 beta inhibits the transcriptional activation of Notch target genes both in vitro and in vivo, whereas lithium chloride treatment or Wnt-1 overexpression that results in GSK-3 beta inhibition leads to the up-regulation of the Hes-1 promoter. Together, our results suggest that cross-talk between Notch and Wnt pathways may be partially mediated by specific regulation of GSK-3 beta-dependent Notch phosphorylation.

Published
2003
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