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

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.

authors

Huang J,Gao X,Li S,Cao Z

doi

10.1073/pnas.94.24.12829

subject

Has Abstract

pub_date

1997-11-25 00:00:00

pages

12829-32

issue

24

eissn

0027-8424

issn

1091-6490

journal_volume

94

pub_type

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