Overexpression of an enzymically inactive interleukin-1-receptor-associated kinase activates nuclear factor-κB
摘要：
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 κB, suggesting that the kinase activity of IRAK is not required outside of the IL-1R complex.
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DOI：
10.1042/0264-6021:3390227
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年份：
1999
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来源期刊
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2002
被引量：36
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