| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| Simultaneous blockade of PDGFR and PI3K or Erk pathway may enhance therapeutic targeting in gliomas . . ^^^ |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| The cooperation of autocrine PDGFR signaling with oncogenic Ras hyperactivates PI3K and is required for survival during EMT . ^^^ |
|
| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| In response to binding of platelet derived growth factor ( PDGF ) , the PDGF receptor ( PDGFR ) beta subunit is phosphorylated on tyrosine residues and associates with numerous signal transduction enzymes , including the GTPase activating protein of ras ( GAP ) and phosphatidylinositol 3 kinase ( PI3K ) . ^^^ Like PI3K , GAP associates only with receptors that have been permitted to autophosphorylate , and GAP itself does not require tyrosine phosphate in order to stably associate with the phosphorylated PDGFR . ^^^ The in vitro and in vivo associations of GAP and PI3K activity to these PDGFR mutants were indistinguishable . ^^^ The distinct tyrosine residue requirements suggest that GAP and PI3K bind different regions of the PDGFR . ^^^ This possibility was also supported by the observation that the antibody to the PDGFR kinase insert Y 751 region that blocks association of PI3K had only a minor effect on the in vitro binding of GAP . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| The beta subunit of the platelet derived growth factor receptor ( PDGFR ) coprecipitates with a phosphatidyl inositol 3 kinase activity ( PI3K ) following stimulation of cells by PDGF . ^^^ Mutagenesis of a tyrosine ( Y ) phosphorylation site , Y 751 , in the PDGFR , greatly reduces PI3K , consistent with the possibility that phosphorylation of Y 751 signals association of PI3K . ^^^ To test this we have reconstituted the binding of the PDGFR beta subunit and PI3K in vitro . ^^^ Binding is rapid , saturable and requires phosphorylation of the PDGFR at Y 751 , but does not require PDGF dependent phosphorylation of PI3K . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| Binding of platelet derived growth factor ( PDGF ) to the PDGF receptor ( PDGFR ) beta subunit triggers receptor tyrosine phosphorylation and the stable association of a number of signal transduction molecules , including phospholipase C gamma ( PLC gamma ) , the GTPase activating protein of ras ( GAP ) , and phosphatidylinositol 3 kinase ( PI3K ) . ^^^ Previous reports have identified three PDGFR tyrosine phosphorylation sites in the kinase insert domain that are important for stable association of GAP and PI3K . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| Our previous studies indicated that PI3K and PLC gamma were required for relay of the mitogenic signal of beta PDGFR , whereas GAP and Syp did not appear to be required for this response . ^^^ Focusing on the PLC gamma dependent branch of beta PDGFR signaling , we constructed a series of mutant beta PDGFRs that contained the binding sites for pairs of the receptor associated proteins : PLC gamma and PI3K , PLC gamma and GAP , or PLC gamma and Syp . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| Upon binding of platelet derived growth factor ( PDGF ) , the PDGF beta receptor ( PDGFR ) undergoes autophosphorylation on distinct tyrosine residues and binds several SH 2 domain containing signal relay enzymes , including phosphatidylinositol 3 kinase ( PI3K ) , phospholipase C gamma ( PLC gamma ) , the GTPase activating protein of Ras ( RasGAP ) , and the tyrosine phosphatase SHP 2 . ^^^ In this study , we have investigated whether PDGF dependent PI3K activation is affected by the other proteins that associate with the PDGFR . ^^^ We constructed and characterized a series of PDGFR mutants which contain binding sites for PI3K as well as one additional protein , either RasGAP , SHP 2 , or PLC gamma . ^^^ Thus , activation of PI3K requires not only binding of PI3K to the tyrosine phosphorylated PDGFR but accumulation of GTP bound Ras as well . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| On ligand induced tyrosine phosphorylation , PDGFR associated with phospholipase C ( PLC ) gamma 1 , Ras GTPase activating protein ( RasGAP ) , and phosphatidylinositol 3 kinase ( PI3K ) but not with the Syp growth factor receptor bound protein 2 Son of Sevenless complex . ^^^ In contrast , PDGF BB stimulation triggered PDGFR associated PI3K activity . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| To investigate the in vivo relevance of this observation , intracellular inositol trisphosphate ( IP 3 ) generation and calcium release were examined in HepG 2 cells expressing a series of PDGFR mutants that activate PLCgamma with or without receptor association with PI3K . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| In conclusion , our results demonstrate that Gi enables the PDGFR to signal more efficiently to p42 / p44 MAPK , and this appears to be achieved through the regulation of c Src and Grb 2 / PI3K , which are intermediates in the p42 / p44 MAPK cascade . . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| Moreover , we further demonstrated a requirement for the activation of phosphatidylinositol 3 kinase ( PI3K ) in this response by using chemical inhibitors of PI3K , mutant PDGFR , and dominant negative PI3K . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| Most likely this was due to the presence of a suramin insensitive intracellular PDGFR pool that allowed activation of PI3K located in intracellular compartments . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| Expression of PDGFR beta mutant proteins demonstrates that these responses require the presence of an intact phosphatidylinositol 3 kinase ( PI3K ) binding site on the overexpressed PDGF receptor . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| By using this system , we showed that endosomal activation of PDGFR recruits various signaling proteins including Grb 2 , SHC , phospholipase C gamma 1 , and the p85alpha subunit of phosphatidylinositol 3 kinase into endosomes and forms signaling complexes with PDGFR . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| Because p85alpha stays bound to the PDGFR during receptor endocytosis , p85alpha will also be localized to the same early endosomal compartment as Rab 5 and Rab 4 . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| Expression of a partially activated A Raf mutant resulted in decreased tyrosine phosphorylation of the PDGFR , specifically on Y 857 ( autophosphorylation site ) and Y 1021 ( phospholipase Cgamma 1 ( PLCgamma 1 ) binding site ) , but not the binding sites for other signalling proteins ( Nck , phosphatidylinositol 3 ' kinase ( PI3K ) , RasGAP , Grb 2 , SHP ) . ^^^ Thus , A Raf can regulate PLCgamma 1 signalling via a PDGFR dependent mechanism and may also regulate PI3K signalling via a PDGFR independent mechanism . . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| We demonstrate for the first time that the redox regulation of PDGFr tyrosine autophosphorylation and its signalling are related to NADPH oxidase activity through protein kinase C ( PKC ) and phosphoinositide 3 kinase ( PI3K ) activation and H2O2 production . ^^^ Therefore , we suggest a redox circuit whereby , upon PDGF stimulation , PKC , PI3K and NADPH oxidase activity contribute to complete c Src kinase activation , thus promoting maximal phosphorylation and activation of PDGFr tyrosine phosphorylation . . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| Analysis of the functional consequences of the Galpha 12 PDGFRalpha signaling axis indicates that Galpha 12 stimulates the phosphatidylinositol 3 kinase ( PI3K ) AKT signaling pathway through PDGFR . ^^^ |
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| Interacting proteins: P09619 and P27986 |
Pubmed |
SVM Score :0.0 |
| The activation of the PI3K pathway after PDGFR stimulation was prolonged in NHERF 1 ( / ) mouse embryonic fibroblasts as compared to wild type cells , consistent with defective PTEN recruitment to PDGFR in the absence of NHERF 1 . ^^^ These data indicate that , in normal cells , NHERF proteins recruit PTEN to PDGFR to restrict the activation of the PI3K . . ^^^ |
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