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J Biol Chem, Vol. 274, Issue 19, 13077-13084, May 7, 1999
B Activity by mPLK/IRAK
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From the Departments of The innate immune response is an important
defense against pathogenic agents. A component of this response is the
NF- Biochemistry and Molecular
Biology and § Microbiology and Immunology, Indiana
University School of Medicine and the Walther Cancer Institute,
Indianapolis, Indiana 46202 and ¶ Department of Pharmacology,
Cancer Research Institute, Kanazawa University,
Kanazawa 920, Japan
B-dependent activation of genes encoding inflammatory
cytokines such as interleukin-8 (IL-8) and cell adhesion molecules like
E-selectin. Members of the serine/threonine innate immune kinase family
of proteins have been proposed to mediate the innate immune response.
One serine/threonine innate immune kinase family member, the
mouse Pelle-like
kinase/human interleukin-1
receptor-associated kinase
(mPLK/IRAK), has been proposed to play an obligate role in promoting
IL-1-mediated inflammation. However, it is currently unknown whether
mPLK/IRAK catalytic activity is required for IL-1-dependent
NF-B activation. The present study demonstrates that mPLK/IRAK
catalytic activity is not required for IL-1-mediated activation of an
NF-B-dependent signal. Intriguingly, catalytically
inactive mPLK/IRAK inhibits type 1 tumor necrosis factor (TNF)
receptor-dependent NF-B activation. The pathway through
which mPLK/IRAK mediates this TNF response is TRADD- and TRAF2-independent. Our data suggest that in addition to its role in
IL-1 signaling, mPLK/IRAK is a component of a novel signal transduction
pathway through which TNF R1 activates NF-B-dependent gene expression.
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