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.
journal_name
Proc Natl Acad Sci U S Aauthors
Huang J,Gao X,Li S,Cao Zdoi
10.1073/pnas.94.24.12829subject
Has Abstractpub_date
1997-11-25 00:00:00pages
12829-32issue
24eissn
0027-8424issn
1091-6490journal_volume
94pub_type
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