Stress-induced activation of protein kinase CK2 by direct interaction with p38 mitogen-activated protein kinase
Stress-induced activation of protein kinase CK2 by direct interaction with p38 mitogen-activated protein kinase
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DOI：
10.1074/jbc.m000312200
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发表时间：
2000-06-02
影响因子：
4.8
通讯作者：
Pelech, SL
中科院分区：
文献类型：
--
作者：
Sayed, M;Kim, SO;Pelech, SL
蛋白激酶CK 2与细胞增殖和分化中重要的多种蛋白质的调节有关。在这里，我们证明了压力信号剂茴香霉素，亚砷酸盐，和肿瘤坏死因子-α刺激CK 2在人宫颈癌HeLa细胞的特异性酶活性高达8倍，这可以被阻断的p38 MAP激酶抑制剂SB 203580。我们表明，p38 α MAP激酶，在磷酸化依赖的方式，可以直接与α和β亚基的CK 2激活全酶通过什么似乎是一种变构机制。此外，我们证明，茴香霉素和肿瘤坏死因子-α诱导的p53在Ser-392磷酸化，这是重要的转录活性的生长抑制蛋白，需要p38 MAP激酶和CK 2的活动。
Protein kinase CK2 has been implicated in the regulation of a wide range of proteins that are important in cell proliferation and differentiation. Here we demonstrate that the stress signaling agents anisomycin, arsenite, and tumor necrosis factor-alpha stimulate the specific enzyme activity of CK2 in the human cervical carcinoma HeLa cells by up to 8-fold, and this could be blocked by the p38 MAP kinase inhibitor SB203580. We show that p38 alpha MAP kinase, in a phosphorylation-de pendent manner, can directly interact with the alpha and beta subunits of CK2 to activate the holoenzyme through what appears to be an allosteric mechanism. Furthermore, we demonstrate that anisomycin- and tumor necrosis factor-alpha-induced phosphorylation of p53 at Ser-392, which is important for the transcriptional activity of this growth suppressor protein, requires p38 MAP kinase and CK2 activities.