TAK1 regulates multiple protein kinase cascades activated by bacterial lipopolysaccharide.
During inflammation the balance between cell activation and cell death is determined by the tight regulation of multiple intracellular enzyme cascades. Key regulatory steps often involve protein kinases. We show that the prototypical pro-inflammatory molecule, bacterial lipopolysaccharide, activates multiple protein kinases such as p38, JNK, IKK-beta, and PKB/Akt via transforming growth factor beta-activated kinase-1 ( TAK1). We also show that TAK1 plays an important role in similar activation pathways triggered by interleukin-1. Thus TAK1 must be considered as an important component of intracellular pathways in cells involved in host responses to physiological and/or environmental stress signals during inflammation.[1]References
- TAK1 regulates multiple protein kinase cascades activated by bacterial lipopolysaccharide. Lee, J., Mira-Arbibe, L., Ulevitch, R.J. J. Leukoc. Biol. (2000) [Pubmed]
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