Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
Mitotic , tyrosine phosphorylated Sam 68 bound selectively to recombinant SH 2 domains with significantly different affinities ( c Src approximately Ras GTPase activating protein > p 85 alpha ( amino terminal ) > Grb 2 > > p 85 alpha ( COOH terminal ) ) . ^^^
Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
Employing antibodies specific to two p 85 isoforms , p85alpha and p85beta , we demonstrate that HTC IR cells express both p 85 isoforms , and these isoforms induce the formation of similar signaling complexes in response to insulin . p 60 70 , present in both alpha p85alpha and alpha p85beta immunoprecipitates , is a GAP associated protein , but is distinct from the p 68 src associated protein in mitosis ( Sam 68 ) by several criteria . ^^^ These data suggest that 1 ) GAP associated protein , but not Sam 68 , is a part of insulin signaling complexes ; and 2 ) p85alpha and p85beta form similar , but distinct , insulin receptor signaling complexes . . ^^^
Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
Sam 68 is a Ras GAP associated protein in mitosis . ^^^ During mitosis , Sam 68 undergoes tyrosine phosphorylation , which negatively regulates its nucleic acid binding properties and mediates the interaction of Sam 68 with critical SH 2 containing signaling proteins such as Grb 2 , PLC gamma 1 and Ras GAP . ^^^ However , the interaction of Ras GAP with Sam 68 has been brought into question , based on the lack of co immunoprecipitation between Sam 68 and Ras GAP in interphase cells . ^^^
Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
We have correlated these inhibitions with the disruption of multifunctional complexes containing PLCgamma 1 , p120GAP and Sam 68 , induced by T cell activation . ^^^
Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
Here , we report that the RNA binding and protein binding protein Sam 68 associates with the p 21 ( ras ) GTPase activating protein RasGAP . ^^^
Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
Sam 68 is a docking protein linking GAP and PI3K in insulin receptor signaling . ^^^ In fact , PI3K activity was increased in both anti Sam 68 and anti GAP immmunoprecipitates upon insulin stimulation . ^^^ Moreover , we have found that Sam 68 is a p120GAP associated protein after Tyr phosphorylation by the IR . ^^^ Thus , Sam 68 is linking p120GAP to PI3K signaling pathway . ^^^ We propose that the recruitment of the docking protein Sam 68 to the PI3K pathway may serve to allow the association of other signaling molecules , i . e . p120GAP . ^^^
Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
In the present work , we have found that Sam 68 is tyrosine phosphorylated in peripheral blood mononuclear cells ( PBMC ) from HIV infected subjects , leading to the formation of signalling complexes with p 85 the regulatory subunit of PI3K , GAP and STAT 3 , and decreasing its RNA binding capacity . ^^^
Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
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Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
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Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
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Interacting proteins: Q07666 and P20936 Pubmed SVM Score :1.0928763
We describe herein that Sam 68 associates with p120GAP and PLC gamma 1 in human mature T cells and in a T cell line expressing the CD 4 molecule HUT 78 CD4+ . 1.0928763^^^ It is dependent on CD 4 expression and , in part , on the association of CD 4 with p56lck , as shown by the strongly decreased association of Sam 68 with p120GAP in the CD 4 mutants , HUT 78 CD4 , and by the reduced association of Sam 68 with both p120GAP and p56lck in the HUT 78 T cell line expressing a CD 4 mutant unable to interact with p56lck , HUT 78 C420 / 22 . 0.81485561^^^ Sam 68 was initially described as associated with p120GAP . 0.76310104^^^
Interacting proteins: Q07666 and P20936 Pubmed SVM Score :0.0
Sam 68 associates with the SH 3 domains of Grb 2 recruiting GAP to the Grb 2 SOS complex in insulin receptor signaling . ^^^ We have recently found that Sam 68 is a substrate of the insulin receptor ( IR ) that translocates from the nucleus to the cytoplasm and that Tyr phosphorylated Sam 68 associates with the SH 2 domains of p 85 PI3K and GAP , in vivo and in vitro . ^^^ Besides , we sought to further study the association of Sam 68 with the Ras GAP pathway by assessing the interactions with SH 3 domains of Grb 2 . ^^^ In vivo studies of protein protein interaction were assessed by co immunoprecipitation experiments with specific antibodies against Sam 68 , GAP , Grb 2 , SOS , and phosphotyrosine ; and by affinity precipitation with the fusion proteins ( SH 3 Grb2 ) . ^^^ Insulin stimulation of HTC IR cells promotes phosphorylation of Sam 68 and its association with the SH 2 domains of GAP . ^^^