Interferon-gamma induces tyrosine phosphorylation of interferon-gamma receptor and regulated association of protein tyrosine kinases, Jak1 and Jak2, with its receptor.
作者： A.F. Wilks , A.C. Larner , K. Igarashi , L. Ozmen , G. Garotta
DOI: 10.1016/S0021-9258(17)36621-8
关键词:
摘要: Interferon-gamma (IFN-gamma) induces the expression of a set early response genes by tyrosine phosphorylation latent transcription factors such as p91. Although kinases, Jak1 and Jak2, have recently been shown to be critical for signal transduction IFN-gamma, evidence is lacking both IFN-gamma receptor (IFN-gamma R) interaction between Jak1, R. In this report, we show that binding HeLa cells initiated series events resulted in extremely rapid (15 s) not only p91 but also Coimmunoprecipitation experiments revealed was associated with R prior ligand binding, whereas Jak2 became part R-Jak1 complex immediately after binding. H2O2/vanadate treatment 15 min Only 60 did observe assembly factor FcRF gamma binds promoter fcgr1 gene. These data suggest JAK1 associates results recruitment JAK2 into followed complex.
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