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Biochem J. 1999 Apr 15;339 ( Pt 2):227-31.

Overexpression of an enzymically inactive interleukin-1-receptor-associated kinase activates nuclear factor-kappaB.

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1
Glaxo Wellcome, Cell Biology Unit, Gunnels Wood Road, Stevenage SG1 2NY, UK. bm45459@GlaxoWellcome.co.uk

Abstract

Upon interleukin 1 (IL-1) stimulation, the IL-1-receptor (IL-1R)-associated kinase (IRAK) is rapidly recruited to the IL-1R complex and undergoes phosphorylation. Here we demonstrate that recombinant wild-type IRAK (IRAK-WT), but not a kinase-defective mutant with Asp340 replaced by an asparagine residue (IRAK-Asp340Asn), is highly phosphorylated and is capable of auto-phosphorylation in vitro. Overexpression of both IRAK-WT and IRAK-Asp340Asn caused activation of nuclear factor kappaB, suggesting that the kinase activity of IRAK is not required outside of the IL-1R complex.

PMID:
10191251
PMCID:
PMC1220149
[Indexed for MEDLINE]
Free PMC Article
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