Identification of a nuclear protein that promotes NF-κB activation
Identification of a nuclear protein that promotes NF-κB activation
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DOI：
10.1016/j.bbrc.2003.09.074
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发表时间：
2003-10-24
影响因子：
3.1
通讯作者：
Shu, HB
中科院分区：
文献类型：
--
作者：
Chen, DY;Li, ZQ;Shu, HB
受体相互作用蛋白 (RIP) 是一种丝氨酸/苏氨酸蛋白激酶，在肿瘤坏死因子受体 1 (TNF-R1) 诱导的 NF-kappaB 激活中发挥重要作用。在对潜在 RIP 相互作用蛋白的酵母双杂交筛选中，我们鉴定了一种称为 NKAP 的新蛋白。尽管 NKAP 在酵母中与 RIP 相互作用，但在免疫共沉淀实验中 NKAP 不与哺乳动物细胞中的 RIP 相互作用。当 NKAP 在 293 细胞中过表达时，NKAP 以剂量依赖性方式激活 NF-κB。此外，反义RNA下调NKAP显着抑制TNF和IL-1诱导的NF-κB激活。免疫荧光染色表明NKAP定位于细胞核。我们的研究结果表明 NKAP 是 TNF 和 IL-1 诱导的 NF-kappaB 激活的新型核调节因子。 (C) 2003 Elsevier Inc. 保留所有权利。
Receptor-interacting protein (RIP) is a serine/threonine protein kinase that is critically involved in tumor necrosis factor receptor-1 (TNF-R1)-induced NF-kappaB activation. In a yeast two-hybrid screening for potential RIP-interacting proteins, we identified a novel protein designated as NKAP. Although NKAP interacts with RIP in yeast, NKAP does not interact with RIP in mammalian cells in co-immunoprecipitation experiments. When overexpressed in 293 cells, NKAP activated NF-kappaB in a dose-dependent manner. Moreover, down-regulation of NKAP by antisense RNA significantly inhibited TNF- and IL-1-induced NF-kappaB activation. Immunofluorescent staining indicated that NKAP was localized in the nucleus. Our findings suggest that NKAP is a novel nuclear regulator of TNF- and IL-1-induced NF-kappaB activation. (C) 2003 Elsevier Inc. All rights reserved.