Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P19235 and P07948 Pubmed SVM Score :1.462258
In vitro binding studies using GST Lyn fusion proteins further showed that the Src homology ( SH ) 2 domain of Lyn specifically binds with the tyrosine phosphorylated EpoR in lysate from Epo stimulated cells , whereas the tyrosine kinase domain of Lyn binds with the unphosphorylated EpoR . 1.462258^^^ In the present study , we demonstrate that Lyn , a Src family tyrosine kinase , physically associates with the EpoR in Epo dependent hematopoietic cell lines , 32D / EpoR Wt and F36E . 1.447321^^^
Interacting proteins: P19235 and P07948 Pubmed SVM Score :0.5138452
Finally , co immunoprecipitation and yeast two hybrid analyses indicated that lyn directly associated with the erythropoietin receptor complex . 0.5138452^^^
Interacting proteins: P19235 and P07948 Pubmed SVM Score :0.0
The erythropoietin ( Epo ) receptor transduces its signals by activating physically associated tyrosine kinases , mainly Jak 2 and Lyn , and thereby inducing tyrosine phosphorylation of various substrates including the Epo receptor ( EpoR ) itself . ^^^ Together , the present study suggests that , upon Epo stimulation , CrkL is recruited to the EpoR through interaction between the CrkL SH 2 domain and phosphorylated Tyr ( 460 ) in the EpoR cytoplasmic domain and undergoes tyrosine phosphorylation by receptor associated Lyn to activate the downstream signaling pathway leading to the activation of Erk and Elk 1 . . ^^^
Interacting proteins: P19235 and P07948 Pubmed SVM Score :0.0
We examined the role of the Src kinase Lyn in phospholipase C gamma 2 ( PLC gamma 2 ) and phosphatidylinositol ( PI ) 3 kinase activation in erythropoietin ( Epo ) stimulated FDC P 1 cells transfected with a wild type ( WT ) Epo receptor ( Epo R ) . ^^^ We also demonstrated that Epo phosphorylated Lyn is associated with tyrosine phosphorylated PLC gamma 2 and PI 3 kinase in WT Epo R FDC P 1 stimulated cells . ^^^
Interacting proteins: P19235 and P07948 Pubmed SVM Score :0.0
Previously we have shown that the tyrosine kinase Lyn associates with the erythropoietin receptor and is essential for hemoglobin synthesis in three erythroleukemic cell lines . ^^^
Interacting proteins: P19235 and P07948 Pubmed SVM Score :0.0
Cells containing the dominant negative Lyn displayed altered intracellular phosphorylation patterns , including mitogen actiated protein kinase , but not erythropoietin receptor , Janus activated kinase ( JAK ) 2 , or STAT 5 . ^^^ Although Lyn was shown to bind several sites on the cytoplasmic domain of the erythropoietin receptor , it was not activated when a receptor mutated at the JAK 2 binding site was ectopically expressed in J2E cells indicating that JAK 2 is the primary kinase in erythropoietin signaling and that Lyn is a secondary kinase . ^^^
Interacting proteins: P19235 and P07948 Pubmed SVM Score :0.0
We have shown previously that the tyrosine kinase Lyn is involved in differentiation signals emanating from an activated erythropoietin receptor . ^^^
Interacting proteins: P19235 and P07948 Pubmed SVM Score :0.0
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Interacting proteins: P19235 and P07948 Pubmed SVM Score :0.0
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Interacting proteins: P19235 and P07948 Pubmed SVM Score :0.0
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Interacting proteins: P19235 and P07948 Pubmed SVM Score :0.0
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