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Cyclin G associated kinase interacts with interleukin 12 receptor β2 and suppresses interleukin 12 induced IFN‐γ production
Author(s) -
Lin Ying,
Tang Yu Jie,
Zong Hong Liang,
Gu Jian Xin,
Deng Wei Wen,
Wang Chen,
Sun Bing
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.09.056
Subject(s) - interleukin 1 receptor, type i , interleukin 1 receptor , cancer research , interleukin 1 receptor, type ii , interleukin 4 receptor , chemistry , interleukin 12 receptor, beta 1 subunit , interleukin , microbiology and biotechnology , interleukin 1β , interleukin 5 , biology , cytokine , immunology
Interleukin 12 receptor β1 (IL‐12Rβ1) and β2 (IL‐12Rβ2) constitute the functional and high‐affinity receptor complex for interleukin 12 (IL‐12) and mediate important functions in activated T cells. In this study, we identified cyclin G associated kinase (GAK) as a new IL‐12Rβ2‐interacting protein using yeast two‐hybrid system and confirmed it by coimmunoprecipitation assays. Overexpression of GAK in activated T cells suppresses IL‐12 induced IFN‐γ production but has no detectable effects on its proliferation, whereas knockdown of GAK by RNA interference (RNAi) increases IFN‐γ production. These results suggest that GAK associates with IL‐12Rβ2 and may play a role in regulating IL‐12 signaling.