| Interacting proteins: P23471 and Q9Y2X7 |
Pubmed |
SVM Score :0.0 |
| VacA bound to Ptprz , and the levels of tyrosine phosphorylation of the G protein coupled receptor kinase interactor 1 ( Git 1 ) , a Ptprz substrate , were higher after treatment with VacA , indicating that VacA behaves as a ligand for Ptprz . ^^^ |
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| Interacting proteins: P23471 and Q9Y2X7 |
Pubmed |
SVM Score :0.0 |
| VacA bound to Ptprz , and the tyrosine phosphorylation level of Git 1 , a Ptprz substrate , was elevated by VacA , indicating that VacA behaves as a ligand for Ptprz . ^^^ |
|
| Interacting proteins: P23471 and Q9Y2X7 |
Pubmed |
SVM Score :0.0 |
| Here , we show that pleiotrophin ( PTN ) , a natural ligand for protein tyrosine phosphatase receptor type Z ( Ptprz ) ( also called PTPzeta / RPTPbeta ) , inactivates Ptprz through oligomerization and increases the tyrosine phosphorylation of substrates for Ptprz , G protein coupled receptor kinase interactor 1 ( Git 1 ) and membrane associated guanylate kinase , WW and PDZ domain containing 1 ( Magi 1 ) . ^^^ |
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| Interacting proteins: P23471 and Q9Y2X7 |
Pubmed |
SVM Score :0.0 |
| Immunoprecipitation experiments to assess VacA binding to RPTPbeta B mutants indicated that five residues ( QTTQP ) at positions 747 751 of the extracellular domain of RPTPbeta B ( which is commonly retained in RPTPbeta A , a long form of RPTPbeta ) play a crucial role in its interaction with VacA , resulting in vacuolation as well as Git 1 phosphorylation . ^^^ |
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