| Interacting proteins: P42224 and P63244 |
Pubmed |
SVM Score :0.0 |
| Interestingly , the interaction between the human type 1 IFN receptor and STAT 1 is not direct but mediated by the adapter protein receptor for activated protein kinase C ( RACK 1 ) . ^^^ Disruption of the IFNalpha receptor RACK 1 interaction abolishes not only IFNalpha induced tyrosine phosphorylation of STAT 1 but also activation of STAT 2 , indicating that RACK 1 plays a central role in early signaling through the Jak STAT pathway . ^^^ These findings demonstrate the involvement of RACK 1 in STAT 1 activation and raise the possibility that other STATs may pre associate with cytokine receptors through similar adapter STAT mediated interactions . . ^^^ |
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| Interacting proteins: P42224 and P63244 |
Pubmed |
SVM Score :0.0 |
| Association of mumps virus 5 protein with RACK 1 results in dissociation of STAT 1 from the alpha interferon receptor complex . ^^^ On the other hand , in uninfected cells , STAT 1 was associated with the long form of the beta subunit of the alpha IFN receptor , and this association was mediated by the function of RACK 1 as an adaptor protein . ^^^ Furthermore , RACK 1 interacted with mumps virus 5 protein with a higher affinity than STAT 1 did . ^^^ Therefore , it is suggested that mumps virus 5 protein has the ability to interact strongly with RACK 1 and consequently to bring about the disruption of the complex formed from STAT 1 , RACK 1 , and the IFN receptor . . ^^^ |
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| Interacting proteins: P42224 and P63244 |
Pubmed |
SVM Score :0.0 |
| We performed immunoprecipitation experiments using antibodies against type 1 IFN receptor chain 1 ( INFAR 1 ) and antibody against RACK 1 , which is reported to be a scaffold protein interacting with type 1 IFN receptor chain 2 and STAT 1 . ^^^ These experiments indicated that IFNAR 1 forms a complex containing the MeV accessory proteins C and 5 , RACK 1 , and STAT 1 in MeV infected cells but not in uninfected cells . ^^^ |
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| Interacting proteins: P42224 and P63244 |
Pubmed |
SVM Score :0.0 |
| In the IFN system , RACK 1 functions as an adaptor recruiting the transcription factor STAT 1 to the receptor complex . ^^^ However , RACK 1 should play a broader role in type 1 IFN signaling because mutation of the RACK 1 binding site in the IFN alpha receptor 2 / beta subunit of the type 1 IFN receptor abrogates not only STAT 1 , but also STAT 2 , activation . ^^^ In this study , we demonstrate that RACK 1 serves as a scaffold protein for a multiprotein complex that includes the IFN alpha receptor 2 / beta chain of the receptor , STAT 1 , Janus kinase 1 , and tyrosine kinase 2 . ^^^ |
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