Fibronectin Type III Repeats Mediate RGD-independent Adhesion and Signaling through Activated β1 Integrins
| Autor: | Stephen E. Fawell, Betty H. Chao, Gloria Chi-Rosso, Darren P. Baker, Kate Jiang, Leona E. Ling, Victor Koteliansky, Philip Gotwals, Linda C. Burkly, Jianliang Yang |
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| Rok vydání: | 1997 |
| Předmět: |
Stress fiber
Integrin Tenascin Cell Communication Biochemistry Extracellular matrix Focal adhesion Cell Adhesion Animals Receptors Cytokine Molecular Biology Extracellular Matrix Proteins Manganese Binding Sites biology Integrin beta1 Cell Biology Adhesion Protein-Tyrosine Kinases Fibronectins Rats Cell biology Fibronectin Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases biology.protein Phosphorylation Calcium Cell Adhesion Molecules Oligopeptides Signal Transduction |
| Zdroj: | Journal of Biological Chemistry. 272:31447-31452 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.272.50.31447 |
| Popis: | Many cell-surface and extracellular matrix proteins contain multiple modular domains known as fibronectin type III (FNIII) repeats. Cells adhere to the extracellular matrix proteins fibronectin and tenascin in part by the interaction of certain integrins with the Arg-Gly-Asp (RGD) sequence, displayed on specific FNIII repeats. We have found that, after experimental activation of beta1 integrins, a number of cell types adhere and spread on FNIII repeats lacking RGD, derived from extracellular matrix proteins and cytokine receptors. Interaction between individual FNIII domains and beta1 integrins mediates focal adhesion kinase phosphorylation and subsequent stress fiber and focal contact formation. These data suggest that many FNIII-containing proteins may bind and signal through activated beta1 integrins, dramatically expanding the potential for integrin-dependent intercellular and cell-matrix communication. |
| Databáze: | OpenAIRE |
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