Title : The protein-tyrosine phosphatase SHP-1 binds to and dephosphorylates p120 catenin.

Pub. Date : 2000 Aug 25

PMID : 10835420






4 Functional Relationships(s)
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1 A prominent tyrosine-phosphorylated protein of approximately 100 kDa (designated pp100) in epidermal growth factor (EGF)-stimulated A431 cells was found to be a main interaction partner of the protein-tyrosine phosphatase SHP-1 in pull-down experiments with a glutathione S-transferase-SHP-1 fusion protein. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
2 A prominent tyrosine-phosphorylated protein of approximately 100 kDa (designated pp100) in epidermal growth factor (EGF)-stimulated A431 cells was found to be a main interaction partner of the protein-tyrosine phosphatase SHP-1 in pull-down experiments with a glutathione S-transferase-SHP-1 fusion protein. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
3 Different p120(ctn) isoforms expressed in human embryonal kidney 293 cells, exhibited differential binding to SHP-1 that correlated partly with the extent of EGF-dependent p120(ctn) tyrosine phosphorylation. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
4 Functions of p120(ctn), which are regulated by tyrosine phosphorylation, may be modulated by the described SHP-1-p120(ctn) interaction. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens