IRAK: A kinase associated with the interleukin-1 receptor
IRAK: A kinase associated with the interleukin-1 receptor
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DOI：
10.1126/science.271.5252.1128
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发表时间：
1996-02-23
期刊：
影响因子：
56.9
通讯作者：
Gao, XO
中科院分区：
文献类型：
--
作者：
Cao, ZD;Henzel, WJ;Gao, XO
白细胞介素-1 (IL-1) 的多效性生物活性由其 I 型受体 (IL-1RI) 介导。当配体结合时，IL-1RI 启动信号级联，导致转录调节因子 kappa B (NF-kappa B) 的激活。纯化了一种名为 IRAK（IL-1 受体相关激酶）的蛋白激酶，并对其互补 DNA 进行了分子克隆。当过表达 IL-1RI 的人胚胎肾细胞（细胞系 293）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 的一级氨基酸序列相似，Pelle 是一种蛋白激酶，对于果蝇中 NF-kappa B 同源物的激活至关重要。
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) overexpressing 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.