Rat protein tyrosine phosphatase η physically interacts with the PDZ domains of syntenin
Open Access
- 26 June 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 500 (1-2) , 41-44
- https://doi.org/10.1016/s0014-5793(01)02580-7
Abstract
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.Keywords
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