| Interacting proteins: P04629 and P35568 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P04629 and P35568 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04629 and P35568 |
Pubmed |
SVM Score :0.0 |
| This BDNF stimulated signaling via IRS 1 and 2 was inhibited by K 252a , an inhibitor of Trk tyrosine kinase . ^^^ |
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| Interacting proteins: P04629 and P35568 |
Pubmed |
SVM Score :0.0 |
| Phosphopeptide assays developed to compare PTB domain specificities show that the Shc PTB domain binds with highest affinity to psi XN beta 1 beta 2 pY motifs derived from middle T ( mT ) , TrkA , ErbB 4 , or epidermal growth factor receptors ( psi = hydrophobic , beta = beta turn forming ) ; the IRS 1 PTB domain does not bind with this motif . ^^^ |
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| Interacting proteins: P04629 and P35568 |
Pubmed |
SVM Score :0.0 |
| The PTB domains of Shc and IRS 1 both recognize autophosphorylation sites in RTKs with the consensus sequence NPXpY , but show distinct abilities to bind stably to RTKs such as the TrkA nerve growth factor receptor and the insulin receptor . ^^^ |
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| Interacting proteins: P04629 and P35568 |
Pubmed |
SVM Score :0.0 |
| IRS 1 and IRS 2 are recruited by TrkA receptor and oncogenic TRK T 1 . ^^^ To study TRK T 1 oncogenic signaling and compare it to that induced by the genuine receptor TrkA , we investigated the involvement of IRS 1 , a docking protein implicated in mitogenic signaling induced by several growth factors , in TRK T 1 and TrkA signaling . ^^^ Here , we show that IRS 1 and IRS 2 are phosphorylated on tyrosine in presence of both TRK T 1 and the activated TrkA receptor . ^^^ On the whole , our results suggest that IRS 1 and IRS 2 could be substrates of TRK T 1 and TrkA , and hence could participate in their signal generation . . ^^^ |
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| Interacting proteins: P04629 and P35568 |
Pubmed |
SVM Score :0.0 |
| We also show that Dok 1 does not recognize peptide sequences from TrkA and IL 4 , which are recognized by Shc and IRS 1 , respectively . . ^^^ |
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