The BioGRID | PUBLICATION VIEW

	Proc. Natl. Acad. Sci. U.S.A. Nov (1997); 94(24):12829-32
Recruitment of IRAK to the interleukin 1 receptor complex requires interleukin 1 receptor accessory protein.
Huang J, Gao X, Li S, Cao Z
Tularik, Inc., South San Francisco, CA 94080, USA.
Abstract: 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.
[PUBMED: 9371760]