Silvennoinen O, Schindler C, Schlessinger J, Levy D E
Department of Pharmacology, New York University School of Medicine, New York, 10016.
Science. 1993 Sep 24;261(5129):1736-9. doi: 10.1126/science.8378775.
Interferons induce transcriptional activation through tyrosine phosphorylation of the latent, cytoplasmic transcription factor interferon-stimulated gene factor-3 (ISGF-3). Growth factors and cytokines were found to use a similar pathway: The 91-kilodalton subunit of ISGF-3 was activated and tyrosine phosphorylated in response to epidermal growth factor (EGF), platelet-derived growth factor, and colony stimulating factor-1. The tyrosine phosphorylated factor acquired DNA binding activity and accumulated in nuclei. Activation required the major sites for autophosphorylation on the EGF receptor that bind Src homology region 2 domain-containing proteins implicated in Ras activation. However, activation of this factor was independent of the normal functioning of Ras.
干扰素通过潜伏的细胞质转录因子干扰素刺激基因因子3（ISGF-3）的酪氨酸磷酸化诱导转录激活。发现生长因子和细胞因子使用类似的途径：ISGF-3的91千道尔顿亚基响应表皮生长因子（EGF）、血小板衍生生长因子和集落刺激因子-1而被激活并酪氨酸磷酸化。酪氨酸磷酸化因子获得DNA结合活性并在细胞核中积累。激活需要表皮生长因子受体上与参与Ras激活的含Src同源区2结构域的蛋白质结合的自磷酸化主要位点。然而，该因子的激活与Ras的正常功能无关。
