| Interacting proteins: P08069 and P20936 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P08069 and P20936 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P08069 and P20936 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P08069 and P20936 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P08069 and P20936 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P08069 and P20936 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P08069 and P20936 |
Pubmed |
SVM Score :0.0 |
| A fusion protein containing the SH 2 domains of Ras GTPase activating protein also inhibited the association of phosphatidylinositol 3 kinase activity with immobilized IGF 1 receptor , although less effectively than p 85 , whereas a similar construct containing the SH 2 domain of pp60src was without effect . ^^^ Furthermore , these results suggest that Ras GTPase activating protein can also interact with the IGF 1 receptor and that different SH 2 domain containing proteins interact with the IGF 1 receptor with widely differing affinities . . ^^^ |
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| Interacting proteins: P08069 and P20936 |
Pubmed |
SVM Score :0.0 |
| In this study , we demonstrate an association between the IGF 1 receptor and p 85 , Syp , and GAP , but not with PLC gamma in lysates of cells overexpressing the human IGF 1 receptor . ^^^ We further investigated these interactions using glutathione S transferase ( GST ) fusion proteins containing the amino terminal SH 2 domains of p 85 or GAP , or both SH 2 domains of Syp or PLC gamma to precipitate the IGF 1 receptor from purified receptor preparations and from whole cell lysates . p 85 , Syp , and GAP GSTs precipitated the IGF 1 receptor , whereas the PLC gamma GST did not . ^^^ Using phosphopeptides corresponding to IGF 1 receptor phosphorylation sites , we determined that the p 85 and Syp GST association with the IGF 1 receptor could be inhibited by a carboxyl terminal peptide containing pY 1316 and that the GAP GST association could be inhibited by a NPXY domain peptide . ^^^ The GAP GST binding site was confirmed by showing that a mutant IGF 1 receptor with a deletion of the NPXY domain including tyrosine 950 was poorly precipitated by the GAP GST . ^^^ We conclude that p 85 and Syp may bind directly to the IGF 1 receptor at tyrosine 1316 , and that GAP may bind to the IGF 1 receptor at and PLC gamma was not evident . p 85 , Syp , and GAP are potential modulators of IGF 1 receptor signal transduction . . ^^^ |
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| Interacting proteins: P08069 and P20936 |
Pubmed |
SVM Score :0.0 |
| We report here that the intracellular domain of the Xenopus IGF 1 receptor is capable of binding to the Xenopus homolog of mammalian GIPC , a PDZ domain containing protein previously identified as a binding partner of G ( 1 ) specific GAP ( RGS GAIP ) . ^^^ |
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| Interacting proteins: P08069 and P20936 |
Pubmed |
SVM Score :0.0 |
| Direct interaction of effector proteins such as the p 85 regulatory subunit of phosphatidylinositol 3 kinase ( PI 3 kinase ) , SYP ( SH 2 domain containing tyrosine phosphatase ) and GAP ( Ras GTPase activating protein ) with the insulin receptor ( IR ) and insulin like growth factor 1 ( IGF 1 ) type 1 receptor ( IGF 1R ) has been reported in some studies . ^^^ Interaction of SYP and GAP with IR and IGF 1R was re investigated here in the two hybrid system by assessing his3 / lacZ activation in S . cerevisiae . ^^^ The experiments were performed with the cytoplasmic beta domain of IR and IGF 1R and various SH 2 subdomains of SYP and GAP . ^^^ Thus , interaction of SYP and GAP with IR and IGF 1R , if any , would be weak and / or transient as compared to that of p85 . . ^^^ |
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