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Rat protein tyrosine phosphatase eta physically interacts with the PDZ domains of syntenin. (Articolo in rivista)

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Rat protein tyrosine phosphatase eta physically interacts with the PDZ domains of syntenin. (Articolo in rivista) (literal)

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Iuliano R. 1, Trapasso F. 1, Sama I. 1, Le Pera I. 1, Martelli M.L. 1, Lembo F. 2, Santoro M. 2, Viglietto G. 2, Chiariotti L. 1, Fusco A. 1-2 (2001)
Rat protein tyrosine phosphatase eta physically interacts with the PDZ domains of syntenin.
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Iuliano R. 1, Trapasso F. 1, Sama I. 1, Le Pera I. 1, Martelli M.L. 1, Lembo F. 2, Santoro M. 2, Viglietto G. 2, Chiariotti L. 1, Fusco A. 1-2 (literal)

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Rat protein tyrosine phosphatase eta physically interacts with the PDZ domains of syntenin. (literal)

Abstract

The tyrosine phosphatase r-PTPeta is able to suppress the malignant phenotype of rat thyroid tumorigenic cell lines. To identify r-PTPeta 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-alpha, beta-ephrins and neurofascin. We show that r-PTPeta 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-PTPeta. The integrity of both PDZ domains of syntenin and the carboxy-terminal region of r-PTPeta are required for the interaction between syntenin and r-PTPeta. (literal)

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