Cao Z, Henzel W J, Gao X
Molecular Biology Department, Tularik, Incorporated, South San Francisco, CA 94080, USA.
Science. 1996 Feb 23;271(5252):1128-31. doi: 10.1126/science.271.5252.1128.
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.
白细胞介素-1（IL-1）的多效生物学活性由其I型受体（IL-1RI）介导。当配体结合时，IL-1RI启动信号级联反应，导致转录调节因子核因子κB（NF-κB）的激活。一种名为IRAK（IL-1受体相关激酶）的蛋白激酶被纯化，并对其互补DNA进行了分子克隆。当过表达IL-1RI的人胚肾细胞（293细胞系）或HeLa细胞暴露于IL-1时，IRAK迅速与IL-1RI复合物结合并被磷酸化。IRAK的一级氨基酸序列与Pelle相似，Pelle是一种蛋白激酶，对果蝇中NF-κB同源物的激活至关重要。
