Cross-talk between IRAK-4 and the NADPH oxidase.
作者： Sandrine Pacquelet , Jennifer L. Johnson , Beverly A. Ellis , Agnieszka A. Brzezinska , William S. Lane
DOI: 10.1042/BJ20061184
关键词: Phosphorylation 、 Stimulation 、 TLR4 、 NADPH oxidase 、 Oxidase test 、 Protein kinase A 、 Chemistry 、 Protein kinase C 、 Molecular biology 、 Kinase
摘要: Exposure of neutrophils to LPS (lipopolysaccharide) triggers their oxidative response. However, the relationship between signalling downstream TLR4 (Toll-like receptor 4) after stimulation and activation oxidase remains elusive. Phosphorylation cytosolic factor p47phox is essential for NADPH oxidase. In present study, we examined hypothesis that IRAK-4 (interleukin-1 receptor-associated kinase-4), main regulatory kinase activation, regulates through phosphorylation p47phox. We show a substrate IRAK-4. Unlike PKC (protein C), phosphorylates not only at serine residues, but also threonine residues. Target residues were identified by tandem MS, revealing novel threonine-rich domain. phosphorylated in granulocytes response stimulation. LPS-dependent was enhanced inhibition p38 MAPK (mitogen-activated protein kinase), confirming operates upstream MAPK. IRAK-4-phosphorylated activated cell-free system, overexpression increased activity LPS. have shown endogenous interacts with they co-localize plasma membrane stimulation, using immunoprecipitation assays immunofluorescence microscopy respectively. found Thr133, Ser288 Thr356, targets vitro, are conclude
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