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- W1984086028 abstract "Abstract IFNλR1 is a member of the class II cytokine receptor family, and it associates with IL‐10R2 to form a functional receptor complex, IFNλR. This receptor complex transduces signals from IFNλs (IFNλ1, IFNλ2, and IFNλ3), promoting antiviral and antiproliferative activities similar to those of type I IFNs. In an effort to further understand signal transduction through IFNλR1, we used bioinformatics analysis and identified a tumor necrosis factor receptor‐associated factor 6 (TRAF6)‐binding motif in the intracellular domain of IFNλR1. In subsequent immunoprecipitation and GST pull‐down assays, IFNλR1 was shown to immunoprecipitate with TRAF6 and was pulled down by GST‐TRAF6. Endogenous IFNλR1 and TRAF‐6 interaction implies that these proteins really interact in the cells. This interaction was abrogated upon mutation of the TRAF6‐binding motif in IFNλR1. Furthermore, the interaction between IFNλR1 and TRAF6 inhibited TRAF6‐induced NF‐κB activation, likely due to a reduction in TRAF6 autoubiquitination. Moreover, co‐expression of IFNλR1 with TRAF6 significantly increased the stability of IFNλR1, thereby prolonging its half‐life and enhancing its steady‐state level in cultured cells. J. Cell. Biochem. 113: 3371–3379, 2012. © 2012 Wiley Periodicals, Inc." @default.
- W1984086028 created "2016-06-24" @default.
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- W1984086028 date "2012-09-18" @default.
- W1984086028 modified "2023-09-27" @default.
- W1984086028 title "Interaction of IFNλR1 with TRAF6 regulates NF‐κB activation and IFNλR1 stability" @default.
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- W1984086028 doi "https://doi.org/10.1002/jcb.24213" @default.
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