Phosphorylation and free pool of beta-catenin are regulated by tyrosine kinases and tyrosine phosphatases during epithelial cell migration.

Détails

ID Serval
serval:BIB_12467
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Phosphorylation and free pool of beta-catenin are regulated by tyrosine kinases and tyrosine phosphatases during epithelial cell migration.
Périodique
Journal of Biological Chemistry
Auteur(s)
Müller T., Choidas A., Reichmann E., Ullrich A.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
1999
Volume
274
Numéro
15
Pages
10173-83
Langue
anglais
Résumé
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 essential for the maintenance of functional epithelia, they need to be rapidly disassembled during migration. The transmembrane cell adhesion protein E-cadherin and the cytoplasmic catenins are molecular elements of these structures. Here we demonstrate that epithelial cell migration is accompanied by tyrosine phosphorylation of beta-catenin and an increase of its free cytoplasmic pool. We show further that the protein-tyrosine phosphatase LAR (leukocyte common antigen related) colocalizes with the cadherin-catenin complex in epithelial cells and associates with beta-catenin and plakoglobin. Interestingly, ectopic expression of protein-tyrosine phosphatase (PTP) LAR inhibits epithelial cell migration by preventing phosphorylation and the increase in the free pool of beta-catenin; moreover, it inhibits tumor formation in nude mice. These data support a function for PTP LAR in the regulation of epithelial cell-cell contacts at adherens junctions as well as in the control of beta-catenin signaling functions. Thus PTP-LAR appears to play an important role in the maintenance of epithelial integrity, and a loss of its regulatory function may contribute to malignant progression and metastasis.
Mots-clé
Animals, Cadherins/metabolism, Cell Adhesion Molecules/metabolism, Cell Communication, Cell Movement, Cell Transformation, Neoplastic, Cytoskeletal Proteins/metabolism, Desmoplakins, Desmosomes/metabolism, Epithelial Cells/cytology, Epithelial Cells/physiology, Humans, Mice, Mice, Nude, Neoplasm Invasiveness, Neoplasm Metastasis, Nerve Tissue Proteins, Phosphorylation, Protein Tyrosine Phosphatases/metabolism, Protein-Tyrosine Kinases/metabolism, Rats, Receptor-Like Protein Tyrosine Phosphatases, Class 2, Receptor-Like Protein Tyrosine Phosphatases, Class 4, Receptors, Cell Surface/metabolism, Trans-Activators, Tumor Cells, Cultured, beta Catenin, gamma Catenin
Pubmed
Web of science
Open Access
Oui
Création de la notice
19/11/2007 12:03
Dernière modification de la notice
20/08/2019 12:40
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