Effects of IL‐1 receptor‐associated kinase (IRAK) expression on IL‐1 signaling are independent of its kinase activity

FEBS Letters

Knop, J.¹  Martin, M.U.¹ 

[1] Institut für Molekularpharmakologie OE 5320, Medizinische Hochschule Hannover, D-30623 Hannover, Germany

关键词: Interleukin-1 signaling;    Interleukin-1 receptor-associated protein kinase;    IL-1;    interleukin-1;    IRAK;    IL-1 receptor-associated kinase;    wt;    wild type;    rh;    recombinant human;   

DOI  :  10.1016/S0014-5793(99)00322-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Interleukin-1 (IL-1) stimulates the association of the IL-1 receptor-associated protein kinase (IRAK) with the heterodimer of IL-1RI and IL-1RAcP via the adapter protein MyD88. In the receptor complex IRAK becomes heavily phosphorylated and concomitantly activated. Here we show that overexpression of a kinase-inactive mutant of IRAK (K239S) inhibits neither IL-1-stimulated activation of the transcription factor NF-κB, nor that of the c-Jun N-terminal kinase nor IL-2 production in murine EL-4 cells, but enhances these effects in a manner comparable to wild type IRAK. This strongly suggests that the intrinsic kinase activity is not required for downstream signaling via IRAK.

【 授权许可】

Unknown