Rat protein tyrosine phosphatase eta physically interacts with the PDZ domains of syntenin.
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.
Mesh Terms:
Carrier Proteins, Cells, Cultured, Humans, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Precipitin Tests, Protein Structure, Tertiary, Protein Tyrosine Phosphatases, Receptor-Like Protein Tyrosine Phosphatases, Class 3, Syntenins, Two-Hybrid System Techniques
Carrier Proteins, Cells, Cultured, Humans, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Precipitin Tests, Protein Structure, Tertiary, Protein Tyrosine Phosphatases, Receptor-Like Protein Tyrosine Phosphatases, Class 3, Syntenins, Two-Hybrid System Techniques
FEBS Lett.
Date: Jun. 29, 2001
PubMed ID: 11434923
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