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

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.

SUBMITTER: Maschera B 

PROVIDER: S-EPMC1220149 | biostudies-other | 1999 Apr

REPOSITORIES: biostudies-other