双特异性磷酸酶18与应激激活蛋白激酶相互作用，使应激激活蛋白激酶去磷酸化，并在体内抑制应激激活蛋白激酶/应激活化蛋白激酶信号通路。
Dual specificity phosphotase 18, interacting with SAPK, dephosphorylates SAPK and inhibits SAPK/JNK signal pathway in vivo.
作者信息
Wu Qihan, Huang Shengdong, Sun Yaqiong, Gu Shaohua, Lu Fanglin, Dai Jianfeng, Yin Gang, Sun Liyun, Zheng Dan, Dou Chao, Feng Congjing, Ji Chaoneng, Xie Yi, Mao Yumin
机构信息
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University, Shanghai 200433, People's Republic of China.
出版信息
Front Biosci. 2006 Sep 1;11:2714-24. doi: 10.2741/2001.
The SAPK/JNKs play important roles in numerous cellular processes, and for this reason they have become putative drug targets. Most dual-specificity protein phosphatases (DSPs) play important roles in the regulation of mitogenic signal transduction and cell cycle control in response to extracellular stimuli. Dual-specificity phosphatase 18 (DUSP18), a newly recognized SAPK/JNK phosphatase, is widely expressed. This expression is modulated in response to extracellular stimuli. By phosphorylation assay, pull down and coimmunoprecipitation experiments, it is shown here that DUSP18 interacts with SAPK/JNK and dephosphorylates it both in vitro and in vivo. DUSP18 does not dephosphorylate p38 or p44ERK1. Furthermore, DUSP18 inhibits SAPK/JNK pathway in vivo. Based on these findings, DUSP18 appears to serve an important role by regulation of SAPK/JNK pathway.
应激活化蛋白激酶/应激活化蛋白激酶（SAPK/JNK）在众多细胞过程中发挥重要作用，因此它们已成为潜在的药物靶点。大多数双特异性蛋白磷酸酶（DSP）在响应细胞外刺激时对有丝分裂信号转导和细胞周期调控中发挥重要作用。双特异性磷酸酶18（DUSP18）是一种新发现的SAPK/JNK磷酸酶，广泛表达。这种表达会根据细胞外刺激进行调节。通过磷酸化测定、下拉和免疫共沉淀实验，结果表明DUSP18在体外和体内均与SAPK/JNK相互作用并使其去磷酸化。DUSP18不会使p38或p44ERK1去磷酸化。此外，DUSP18在体内抑制SAPK/JNK途径。基于这些发现，DUSP18似乎通过调节SAPK/JNK途径发挥重要作用。
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