| Autor: |
Iuliano, Rodolfo, Trapasso, Francesco, Samà, Irene, Le Pera, Ilaria, Martelli, Maria Luisa, Lembo, Francesca, Santoro, Massimo, Viglietto, Giuseppe, Chiariotti, Lorenzo, Fusco, Alfredo |
| Zdroj: |
FEBS Letters; January 2001, Vol. 500 Issue: 1 p41-44, 4p |
| Abstrakt: |
The tyrosine phosphatase r-PTPη is able to suppress the malignant phenotype of rat thyroid tumorigenic cell lines. To identify r-PTPη interacting proteins, a yeast two-hybrid screening was performed and an insert corresponding to the full-length syntenin cDNA was isolated. It encodes a protein containing two PDZ domains that mediates the binding of syntenin to proteins such as syndecan, proTGF-α, β-ephrins and neurofascin. We show that r-PTPη is able to interact with syntenin also in mammalian cells, and although syntenin is a tyrosine-phosphorylated protein it is not a substrate of r-PTPη. The integrity of both PDZ domains of syntenin and the carboxy-terminal region of r-PTPη are required for the interaction between syntenin and r-PTPη. |
| Databáze: |
Supplemental Index |
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