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Rat protein tyrosine phosphatase η physically interacts with the PDZ domains of syntenin
Author(s) -
Iuliano Rodolfo,
Trapasso Francesco,
Samà Irene,
Le Pera Ilaria,
Martelli Maria Luisa,
Lembo Francesca,
Santoro Massimo,
Viglietto Giuseppe,
Chiariotti Lorenzo,
Fusco Alfredo
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02580-7
Subject(s) - pdz domain , protein tyrosine phosphatase , tyrosine , microbiology and biotechnology , phosphatase , complementary dna , phosphorylation , protein–protein interaction , chemistry , biology , biochemistry , gene
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.