[鉴定一种激活NF-κB信号通路的新型蛋白质TRIM38]
[Identification A novel protein TRIM38 that activate NF-kappaB signaling pathways].
作者信息
Liu Xin-lei, Lei Xiao-bo, Wang Jian-wei, Hong Tao
机构信息
State Key Laboratory of Molecular Virology and Genetic Engineering, Institute of Pathogen Biology, Peking Union Medical College & Chinese Academy of Medical sciences, Beijing 100730, China.
出版信息
Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi. 2011 Feb;25(1):60-2.
OBJECTIVE
The tripartite motif (TRIM) proteins are a family of more than 70 human members, however only a few of them have been well studied. It has been shown that TRIM proteins are involved in various cellular processes such as cell proliferation, differentiation, apoptosis and antiviral defense. The functions of TRIM38 are largely unknown. In this study we explore the effect of TRIM38 on NF-kappaB signaling pathway.
METHODS
293T cells were transfected with NF-kappaB-Luc and plasmids expressing TRIM38 and its mutants fused to Flag. 24 h after transfection, cells were harvested and luciferase activities were measured. Data are representative of three independent experiments with triplicate samples. The expression of proteins was analyzed by Western Blot.
RESULTS
TRIM38 could activate NF-kappaB signaling pathway. The mutants of TRIM38 affected the function of TRIM38. Only the mutant of SPRY domain deletion had no obviously influence of the function of TRIM38.
CONCLUSION
Our study reveals that NF-kappaB is activated in response to TRIM38.
目的
三联基序（TRIM）蛋白家族有70多个成员，但只有少数得到了深入研究。已有研究表明，TRIM蛋白参与多种细胞过程，如细胞增殖、分化、凋亡及抗病毒防御。TRIM38的功能大多未知。本研究探讨TRIM38对核因子κB（NF-κB）信号通路的影响。
方法
将NF-κB荧光素酶报告基因（NF-κB-Luc）以及与Flag融合表达TRIM38及其突变体的质粒转染至293T细胞。转染24小时后，收获细胞并检测荧光素酶活性。数据代表三个独立实验的结果，每个实验有三个重复样本。通过蛋白质印迹法分析蛋白质表达情况。
结果
TRIM38可激活NF-κB信号通路。TRIM38的突变体影响其功能。只有SPRY结构域缺失突变体对TRIM38的功能无明显影响。
结论
我们的研究表明，NF-κB可被TRIM38激活。
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