Rat protein tyrosine phosphatase eta physically interacts with the PDZ domains of syntenin

Autor: Rodolfo Iuliano, Ilaria Le Pera, Lorenzo Chiariotti, Giuseppe Viglietto, Francesca Lembo, Alfredo Fusco, Massimo Santoro, Francesco Trapasso, Marialuisa Martelli, Irene Samà
Přispěvatelé: Iuliano, R, Trapasso, F, Samà, I, Le Pera, I, Martelli, Ml, Lembo, Francesca, Santoro, Massimo, Viglietto, G, Chiariotti, Lorenzo, Fusco, Alfredo
Jazyk: angličtina
Rok vydání: 2001
Předmět:
Zdroj: FEBS letters
500 (2001): 41–44.
info:cnr-pdr/source/autori: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/titolo:Rat protein tyrosine phosphatase eta physically interacts with the PDZ domains of syntenin./doi:/rivista:FEBS letters (Print)/anno:2001/pagina_da:41/pagina_a:44/intervallo_pagine:41–44/volume:500
Popis: 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.
Databáze: OpenAIRE