| Interacting proteins: O95297 and Q06124 |
Pubmed |
SVM Score :0.0 |
| Purification and cloning of PZR , a binding protein and putative physiological substrate of tyrosine phosphatase SHP 2 . ^^^ Stimulation of cells with pervanadate resulted in tyrosine phosphorylation of PZR and a near stoichiometric association of PZR with SHP 2 . ^^^ As a binding protein and a putative substrate of SHP 2 , PZR protein may have an important role in cell signaling . . ^^^ |
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| Interacting proteins: O95297 and Q06124 |
Pubmed |
SVM Score :0.0 |
| Sequence comparison of P ( 0 ) with PZR , a tyrosine phosphatase SHP 2 binding protein we recently cloned , revealed the presence of an immunoreceptor tyrosine based inhibitory motif ( ITIM ) in the intracellular portion of the P ( 0 ) molecule . ^^^ |
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| Interacting proteins: O95297 and Q06124 |
Pubmed |
SVM Score :0.0 |
| Dissecting the interaction of SHP 2 with PZR , an immunoglobulin family protein containing immunoreceptor tyrosine based inhibitory motifs . ^^^ Recently , we have isolated a transmembrane protein designated PZR that specifically binds tyrosine phosphatase SHP 2 , which has two SH 2 domains ( Zhao , Z . ^^^ The interaction between PZR and SHP 2 requires involvement of both tyrosyl residues of the former and both SH 2 domains of the latter , since its was disrupted by mutating a single tyrosyl residue or an SH 2 domain . ^^^ Overexpression of catalytically inactive but not active forms of SHP 2 bearing intact SH 2 domains in cells caused hyperphosphorylation of PZR . ^^^ In vitro , tyrosine phosphorylated PZR was efficiently dephosphorylated by the full length form of SHP 2 but not by its SH 2 domain truncated form . ^^^ |
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| Interacting proteins: O95297 and Q06124 |
Pubmed |
SVM Score :0.0 |
| Among these proteins , PZR and PECAM were identified as major SHP 2 binding proteins while LAIR 1 was shown to be a major SHP 1 binding protein . ^^^ |
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| Interacting proteins: O95297 and Q06124 |
Pubmed |
SVM Score :0.0 |
| Tyrosine phosphorylation of PZR was accompanied by recruitment of SHP 2 and was inhibited by PP 1 , a selective inhibitor of the Src family tyrosine kinases . ^^^ |
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| Interacting proteins: O95297 and Q06124 |
Pubmed |
SVM Score :0.0 |
| Novel mesenchymal and haematopoietic cell isoforms of the SHP 2 docking receptor , PZR : identification , molecular cloning and effects on cell migration . ^^^ In the present study , we describe a unique monoclonal antibody , WM 78 , which interacts with PZR , a SHP 2 binding partner . ^^^ The PZR intracellular domain contains two SHP 2 binding immunoreceptor tyrosine based inhibitory motifs ( VIY ( 246 ) AQL and VVY ( 263 ) ADI ) which are not present in PZRa and PZRb . ^^^ Importantly , using SHP 2 mutant ( Delta 46 110 ) and SHP 2 rescue of embryonic fibroblasts stably expressing the PZR isoforms , we demonstrate for the first time that PZR , but not PZRa or PZRb , facilitates fibronectin dependent migration of cells expressing a competent SHP 2 molecule . ^^^ |
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| Interacting proteins: O95297 and Q06124 |
Pubmed |
SVM Score :0.0 |
| PZR is an immunoglobulin superfamily protein that specifically binds tyrosine phosphatase SHP 2 through its intracellular immunoreceptor tyrosine based inhibitory motifs ( ITIMs ) . ^^^ PZR1b shares the same extracellular region with PZR , but it lacks intracellular ITIMs and thus the ability to recruit SHP 2 . ^^^ More importantly , overexpression of PZR1b in human HT 1080 cells had a dominant negative effect by blocking concanavalin A induced tyrosine phosphorylation of full length PZR and recruitment of tyrosine phosphatase SHP 2 . ^^^ |
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| Interacting proteins: O95297 and Q06124 |
Pubmed |
SVM Score :0.0 |
| One such cell surface protein is PZR , which contains two tyrosine based inhibition motifs responsible for binding of SHP 2 . ^^^ The data suggest that the exogenously introduced PZR protein specifically binds SHP 2 , blocks its translocation , and renders it functionally incompetent . ^^^ This is further supported by the fact that the phosphorylated PZR protein had no inhibitory effects on fibroblasts derived from mice expressing only a mutant SHP 2 protein lacking most of the N terminal SH 2 domain . ^^^ |
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