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首页> 外文期刊>Cytokine >c-Jun and c-Fos cooperate with STAT3 in IL-6-induced transactivation of the IL-6 respone element (IRE).
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c-Jun and c-Fos cooperate with STAT3 in IL-6-induced transactivation of the IL-6 respone element (IRE).

机译：c-Jun和c-Fos与STAT3共同作用于IL-6诱导的IL-6受体元件（IRE）的反式激活。

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摘要

Transcriptional activation of eukaryotic genes often requires the cooperative action of many proteins. The interleukin 6 (IL-6) response element (IRE) is activated by signal transducer and activator of transcription 3 (STAT3), and stimulation with IL-6 leads to STAT3 tyr705 phosphorylation, dimerization, translocation to the nucleus and transactivation of target gene promoters containing IREs. Here, we report that IL-6 and 12-O-tetradecanoylphorbol-13-acetate (TPA) synergistically transactivate the IRE in HepG2 cells, which is coupled to a strong upregulation of c-Jun and c-Fos expression by TPA via the mitogen-activated protein kinase (MAPK) pathway. Overexpression of c-Jun and c-Fos strongly enhanced STAT3-driven IRE transactivation as well as transactivation of the human intercellular adhesion molecule (ICAM)-1 promoter. In contrast, c-Jun mutants lacking the transactivation domain, the DNA-binding domain, or mutants in which the serine residues 63 and 73 were replaced by alanine, did not cooperate with STAT3. In immunoprecipitation experiments, a direct association of STAT3 with c-Jun and c-Fos was observed in response to IL-6. Furthermore, c-Jun/STAT3 and c-Fos/STAT3 complexes were detected on IRE probes in electrophoretic mobility shift assay (EMSA) experiments, but did not bind nor transactivate the TPA response element (TRE). These results demonstrate that activator protein-1 (AP-1) transcription factors can cooperate with STAT3 in IRE transactivation in the absence of direct AP-1 DNA binding. Copyright 2001 Academic Press.
机译：真核基因的转录激活通常需要许多蛋白质的协同作用。白介素6（IL-6）反应元件（IRE）被信号转导子和转录激活子3（STAT3）激活，用IL-6刺激导致STAT3 tyr705磷酸化，二聚化，易位至细胞核和目标基因的反式激活含有IREs的启动子。在这里，我们报告说IL-6和12-O-十四烷酰phorbol-13-乙酸盐（TPA）协同转激活IRE在HepG2细胞中，这与TPA通过促细胞分裂剂对c-Jun和c-Fos表达的强烈上调有关激活的蛋白激酶（MAPK）途径。 c-Jun和c-Fos的过度表达大大增强了STAT3驱动的IRE反式激活以及人细胞间粘附分子（ICAM）-1启动子的反式激活。相反，缺乏反式激活结构域，DNA结合结构域或丝氨酸残基63和73被丙氨酸替代的突变体的c-Jun突变体与STAT3不协同作用。在免疫沉淀实验中，观察到STAT3与IL-6的反应直接与c-Jun和c-Fos缔合。此外，在电泳迁移率变动分析（EMSA）实验中，在IRE探针上检测到c-Jun / STAT3和c-Fos / STAT3复合物，但未结合或未激活TPA反应元件（TRE）。这些结果表明，在没有直接AP-1 DNA结合的情况下，激活蛋白1（AP-1）转录因子可以与IRE3中的STAT3协同作用。版权所有2001，学术出版社。

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