NDLI: Interleukin 1/Toll-like receptor-induced autophosphorylation activates interleukin 1 receptor-associated kinase 4 and controls cytokine induction in a cell type-specific manner.

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Interleukin 1/Toll-like receptor-induced autophosphorylation activates interleukin 1 receptor-associated kinase 4 and controls cytokine induction in a cell type-specific manner.

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Interleukin 1/Toll-like receptor-induced autophosphorylation activates interleukin 1 receptor-associated kinase 4 and controls cytokine induction in a cell type-specific manner.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Cushing, Leah Stochaj, Wayne Siegel, Marshall Dower, Ken Wright, Quentin Hirschfield, Margaret Rao, Vikram R. Picard, Capucine Lin, Lih-ling Czerwinski, Robert Puel, Anne Casanova, Jean-laurent
Description	Author Affiliation: Cushing L ( From the Inflammation and Remodeling Research Unit and.)
Abstract	IRAK4 is a central kinase in innate immunity, but the role of its kinase activity is controversial. The mechanism of activation for IRAK4 is currently unknown, and little is known about the role of IRAK4 kinase in cytokine production, particularly in different human cell types. We show IRAK4 autophosphorylation occurs by an intermolecular reaction and that autophosphorylation is required for full catalytic activity of the kinase. Phosphorylation of any two of the residues Thr-342, Thr-345, and Ser-346 is required for full activity, and the death domain regulates the activation of IRAK4. Using antibodies against activated IRAK4, we demonstrate that IRAK4 becomes phosphorylated in human cells following stimulation by IL-1R and Toll-like receptor agonists, which can be blocked pharmacologically by a dual inhibitor of IRAK4 and IRAK1. Interestingly, in dermal fibroblasts, although complete inhibition of IRAK4 kinase activity does not inhibit IL-1-induced IL-6 production, NF-κB, or MAPK activation, there is complete ablation of these processes in IRAK4-deficient cells. In contrast, the inhibition of IRAK kinase activity in primary human monocytes reduces R848-induced IL-6 production with minimal effect on NF-κB or MAPK activation. Taken together, these studies define the mechanism of IRAK4 activation and highlight the differential role of IRAK4 kinase activity in different human cell types as well as the distinct roles IRAK4 scaffolding and kinase functions play.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	15
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-04-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Gene Expression Regulation, Enzymologic Interleukin-1 Receptor-Associated Kinases Metabolism Receptors, Interleukin-1 Toll-Like Receptors Amino Acid Sequence Animals Cell-Free System Cloning, Molecular Cytokines Enzyme Inhibitors Pharmacology Fibroblasts HEK293 Cells Immunity, Innate Insects Interleukin-6 MAP Kinase Signaling System Molecular Sequence Data Monocytes Cytology Mutation NF-kappa B Open Reading Frames Phosphorylation Protein Binding Protein Conformation Agonists Signal Transduction Skin Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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