Recruitment of IRAK to the interleukin 1 receptor complex requires interleukin 1 receptor accessory protein.

The proinflammatory cytokine interleukin 1 (IL-1) activates the transcription of many genes encoding acute phase and proinflammatory proteins, a function mediated primarily by the transcription factor NF-kappaB. An early IL-1 signaling event is the recruitment of the Ser/Thr kinase IRAK to the type I IL-1 receptor (IL-1RI). Here we describe ...
the function of a previously identified IL-1 receptor subunit designated IL-1 receptor accessory protein (IL-1RAcP). IL-1 treatment of cells induces the formation of a complex containing both IL-1RI and IL-1RAcP. IRAK is recruited to this complex through its association with IL-1RAcP. Overexpression of an IL-1RAcP mutant lacking its intracellular domain, the IRAK-binding domain, prevented the recruitment of IRAK to the receptor complex and blocked IL-1-induced NF-kappaB activation.
Mesh Terms:
Animals, DNA, Complementary, Hela Cells, Humans, Interleukin-1 Receptor Accessory Protein, Interleukin-1 Receptor-Associated Kinases, Mice, Molecular Sequence Data, NF-kappa B, Precipitin Tests, Protein Kinases, Proteins, Receptors, Interleukin-1, Signal Transduction
Proc. Natl. Acad. Sci. U.S.A.
Date: Nov. 25, 1997
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