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IRAK: a kinase associated with the interleukin-1 receptor.

Science (New York, N.Y.) | Feb 23, 1996

The pleiotropic biological activities of interleukin-1 (IL-1) are mediated by its type I receptor (IL-1RI). When the ligand binds, IL-1RI initiates a signaling cascade that results in the activation of the transcription regulator nuclear factor kappa B (NF-kappa B). A protein kinase designated IRAK (IL-1 receptor-associated kinase) was purified, and its complementary DNA was molecularly cloned. When human embryonic kidney cells (cell line 293) over-expressing IL-1RI or HeLa cells were exposed to IL-1, IRAK rapidly associated with the IL-1RI complex and was phosphorylated. The primary amino acid sequence of IRAK shares similarity with that of Pelle, a protein kinase that is essential for the activation of a NF-kappa B homolog in Drosophila.

Pubmed ID: 8599092 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Cell Line | Cloning, Molecular | DNA, Complementary | Drosophila | Drosophila Proteins | HeLa Cells | Humans | Interleukin-1 | Interleukin-1 Receptor-Associated Kinases | Molecular Sequence Data | Phosphorylation | Protein Kinases | Protein-Serine-Threonine Kinases | Receptors, Interleukin-1 | Transfection

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