The Human Type I Interferon Receptor

We used specific antibodies recognizing the receptor 1 (IFNAR1) and the recently cloned receptor 2.2 (IFNAR2.2) chains of the human type I interferon receptor complex to demonstrate that the interferon β (IFN-β)-specific receptor-associated phosphoprotein is IFNAR2.2 and not an unknown or additional...

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Veröffentlicht in:The Journal of biological chemistry 1996-12, Vol.271 (52), p.33165-33168
Hauptverfasser: Croze, Ed, Russell-Harde, Dean, Wagner, T. Charis, Pu, Haifeng, Pfeffer, Lawrence M., Perez, H. Daniel
Format: Artikel
Sprache:eng
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Zusammenfassung:We used specific antibodies recognizing the receptor 1 (IFNAR1) and the recently cloned receptor 2.2 (IFNAR2.2) chains of the human type I interferon receptor complex to demonstrate that the interferon β (IFN-β)-specific receptor-associated phosphoprotein is IFNAR2.2 and not an unknown or additional receptor component. Immunoprecipitation experiments demonstrated that IFNAR2.2 is present in Daudi cells as a cell surface protein of approximately 90-100 kDa, which is tyrosine-phosphorylated and associated with IFNAR1, upon stimulation of cells with IFN-β. IFNAR2.2 was not detected associated with IFNAR1 in cells stimulated with IFN-α, suggesting differences in receptor interaction between the two type I interferons. Both IFNAR1 and IFNAR2.2 undergo tyrosine phosphorylation upon induction by either IFN-α or IFN-β. Therefore, it is unclear as to why IFNAR2.2 is not detectable in IFNAR1 immunoprecipitates in IFN-β-treated cells. These data suggest that, although IFN-α and IFN-β may utilize similar receptor chains, they interact with IFNAR1 and IFNAR2.2 in different ways.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.271.52.33165