Gilmore T, DeClue J E, Martin G S
Cell. 1985 Mar;40(3):609-18. doi: 10.1016/0092-8674(85)90209-0.
The v-erbB gene product of avian erythroblastosis virus (AEV) has extensive homology with the receptor for epidermal growth factor (EGF). We report here that chicken embryo fibroblasts (CEF) transformed by AEV show enhanced tyrosine phosphorylation of a number of cellular polypeptides, including the 36 kd protein, which is phosphorylated in avian sarcoma virus-transformed fibroblasts, and the 42 kd protein, which is phosphorylated in mitogen-stimulated cells. CEF infected by AEV mutants with deletions in v-erbA showed enhanced tyrosine phosphorylation, whereas CEF infected by mutants with deletions in v-erbB did not. When membranes from AEV-transformed cells were incubated with gamma-32P-ATP, both the v-erbB gene product and the 36 kd cellular protein became phosphorylated at tyrosine. These results indicate that the v-erbB protein induces tyrosine phosphorylation in vivo and in vitro, and suggest that, like the EGF receptor, it possesses tyrosine-specific protein kinase activity.
禽成红细胞增多症病毒（AEV）的v-erbB基因产物与表皮生长因子（EGF）受体具有广泛的同源性。我们在此报告，被AEV转化的鸡胚成纤维细胞（CEF）显示出多种细胞多肽酪氨酸磷酸化增强，包括在禽肉瘤病毒转化的成纤维细胞中被磷酸化的36kd蛋白，以及在有丝分裂原刺激的细胞中被磷酸化的42kd蛋白。被v-erbA缺失的AEV突变体感染的CEF显示酪氨酸磷酸化增强，而被v-erbB缺失的突变体感染的CEF则没有。当用γ-32P-ATP孵育AEV转化细胞的膜时，v-erbB基因产物和36kd细胞蛋白都在酪氨酸处被磷酸化。这些结果表明，v-erbB蛋白在体内和体外均诱导酪氨酸磷酸化，并提示它像EGF受体一样具有酪氨酸特异性蛋白激酶活性。
