Integrin-dependent Tyrosine Phosphorylation and Growth Regulation by Vav
| Autor: | Martin A. Schwartz, Ilana Yron, Anil Munshi, Amnon Altman, Mitchell E. Reff, Marcel Deckert |
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| Rok vydání: | 1999 |
| Předmět: |
Time Factors
Integrin CHO Cells macromolecular substances GTPase Transfection Proto-Oncogene Mas Focal adhesion Jurkat Cells chemistry.chemical_compound Cricetinae Cell Adhesion Animals Humans Phosphorylation Proto-Oncogene Proteins c-vav Cell adhesion Paxillin Oncogene Proteins biology Chemistry Integrin beta1 Tyrosine phosphorylation General Medicine Protein-Tyrosine Kinases Phosphoproteins Precipitin Tests Actins Fibronectins Cell biology Cytoskeletal Proteins Kinetics Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases biology.protein Tyrosine Guanine nucleotide exchange factor Cell Adhesion Molecules Cell Division |
| Zdroj: | Cell Adhesion and Communication. 7:1-11 |
| ISSN: | 1029-2314 |
| DOI: | 10.3109/15419069909034388 |
| Popis: | The proto-oncogene product p95Vav (Vav) undergoes rapid phosphorylation on tyrosine following stimulation of the T or B cell antigen receptor, and in response to a variety of other cell surface stimuli. Vav contains, among other, a guanine nucleotide exchange factor domain with homology to the Rho/Rac/CDC42 exchange protein Db1. It has been recently shown that Vav is functionally linked to small GTPases of the Rho family, suggesting that it is an activator of Rho GTPases and may participate in regulation of cytoskeletal organization. The present study shows that cell adhesion to fibronectin triggers rapid phosphorylation of Vav on tyrosine in Vav-transfected CHO cells and in Jurkat T cells. Vav phosphorylation is strongly dependent on adhesion and is mediated by beta 1 integrins. Furthermore, Vav overexpression enhances the adhesion-dependent increase in the rate and extent of phosphorylation on focal adhesion kinase and paxillin, and the formation of stress fibers and lamellipodia. In addition, there is a marked increase in the amount of Vav localized to the triton-insoluble fraction following 1 h of incubation on FN. Finally, Vav increases the growth rate of the cells in an adhesion-dependent manner. Our results strongly implicate Vav as a mediator of integrin signal transduction. |
| Databáze: | OpenAIRE |
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