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Content Provider | World Health Organization (WHO)-Global Index Medicus |
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Author | Perez-pinera, P. Vega, J. A. Alcantara, S. Dimitrov, T. Deuel, T. F. |
Description | Author Affiliation: Perez-Pinera P ( Department of Molecular, The Scripps Research Institute, La Jolla, CA 92037, USA.); |
Abstract | Regulation of the levels of tyrosine phosphorylation is essential to maintain the functions of proteins in different signaling pathways and other cellular systems, but how the steady-state levels of tyrosine phosphorylation are coordinated in different cellular systems to initiate complex cellular functions remains a formidable challenge. The receptor protein tyrosine phosphatase (RPTP)beta/zeta is a transmembrane tyrosine phosphatase whose substrates include proteins important in intracellular and transmembrane protein-signaling pathways, cytoskeletal structure, cell-cell adhesion, endocytosis, and chromatin remodeling. Pleiotrophin (PTN the protein and Ptn the gene) is a ligand for RPTPbeta/zeta; PTN inactivates RPTPbeta/zeta, leaving unchecked the continued endogenous activity of tyrosine kinases that increase phosphorylation of the substrates of RPTPbeta/zeta at sites dephosphorylated by RPTPbeta/zeta in cells not stimulated by PTN. Thus, through the regulation of the tyrosine phosphatase activity of RPTPbeta/zeta, the PTN/RPTPbeta/zeta signaling pathway coordinately regulates the levels of tyrosine phosphorylation of proteins in many cellular systems. We now demonstrate that PTN disrupts cytoskeletal protein complexes, ablates calcium-dependent homophilic cell-cell adhesion, stimulates ubiquitination and degradation of N-cadherin, reorganizes the actin cytoskeleton, and induces a morphological epithelial-mesenchymal transition (EMT) in PTN-stimulated U373 cells. The data suggest that increased tyrosine phosphorylation of the different substrates of RPTPbeta/zeta in PTN-stimulated cells alone is sufficient to coordinately stimulate the different functions needed for an EMT; it is possible that PTN initiates an EMT in cells at sites where PTN is expressed in development and in malignant cells that inappropriately express Ptn. |
ISSN | 00278424 |
e-ISSN | 10916490 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Issue Number | 47 |
Volume Number | 103 |
Language | English |
Publisher | National Academy of Sciences |
Publisher Date | 2006-11-01 |
Publisher Place | United States |
Access Restriction | Open |
Subject Keyword | Calcium Metabolism Carrier Proteins Cell Adhesion Physiology Cytokines Epithelial Cells Mesoderm Actins Cadherins Genetics Cell Differentiation Cell Line Cytoskeleton Cytology Phosphorylation Protein Tyrosine Phosphatases Receptor-Like Protein Tyrosine Phosphatases, Class 5 Signal Transduction Tyrosine Ubiquitin Beta Catenin Research Support, N.I.H., Extramural Multidisciplinary |
Content Type | Text |
Resource Type | Article |
Subject | Multidisciplinary |
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