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IL‐1β‐induced phosphorylation of PKB/Akt depends on the presence of IRAK‐1

IL‐1, IL‐18 and LPS are recognized by specific receptor complexes of the Toll/IL‐1R family, characterized by a common intracellular domain indispensable for downstream signaling. Upon ligand binding, these receptors activate the central MyD88–IRAK–TRAF6 signaling module, resulting in the activation of NF‐κB. Ligated receptors also induce activation of other signaling cascades, suchas the PI3‐kinase (PI3‐K) and the p38 mitogen‐activated protein kinase (MAPK) pathways. Unlike the p38MAPK pathway, which couples to the central signaling module, the PI3‐K pathway seems to directly interact with the receptor molecules. Thus, activation of the PI3‐K pathway is thought to be independent of the IRAK‐containing signaling module. Employing two cell lines, we show that the PI3‐K pathways can be activated by IL‐1, IL‐18 or LPS with comparable, but cell type specific kinetics, which can be correlated to biological consequences. This indicates that activation of the PI3‐K pathways may be regulated by an element common for all three receptor types, the MyD88–IRAK–TRAF6 module being a candidate for this function. Using an IRAK‐1‐deficient cell line, we demonstrate that the IRAK‐1‐containing signaling module is essential for the IL‐1‐induced activation of the PI3‐K pathway. Possible models of the interaction between IRAK‐1 and the PI3‐K pathway are discussed.