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首页> 外文期刊>Molecular and Cellular Biology >Tyrosine phosphorylation of a 120-kilodalton pp60src substrate upon epidermal growth factor and platelet-derived growth factor receptor stimulation and in polyomavirus middle-T-antigen-transformed cells.
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Tyrosine phosphorylation of a 120-kilodalton pp60src substrate upon epidermal growth factor and platelet-derived growth factor receptor stimulation and in polyomavirus middle-T-antigen-transformed cells.

机译：在表皮生长因子和血小板衍生的生长因子受体刺激下以及在多瘤病毒中T抗原转化的细胞中，120公斤pp60src底物的酪氨酸磷酸化。

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The monoclonal antibody 2B12 is directed toward p120, a 120-kDa cellular protein originally identified as a protein tyrosine kinase substrate in cells expressing membrane-associated oncogenic variants of pp60src. In this report, we show that p120 was tyrosine phosphorylated in avian cells expressing membrane-associated, enzymatically activated variants of c-src, including variants having structural alterations in the src homology regions 2 and 3. In contrast, p120 was not tyrosine phosphorylated in cells expressing enzymatically activated, nonmyristylated pp60src. Furthermore, p120 was tyrosine phosphorylated in avian cells expressing middle T antigen, the transforming protein of polyomavirus, as well as in rodent cells stimulated with either epidermal growth factor (EGF) or platelet-derived growth factor. Analysis of the time course of p120 tyrosine phosphorylation in EGF-stimulated cells revealed a rapid onset of tyrosine phosphorylation. In addition, both the extent and duration of p120 phosphorylation increased when cells overexpressing the EGF receptor were stimulated with EGF. Biochemical analysis showed that p120 (in both normal and src-transformed cells) was membrane associated, was myristylated, and was phosphorylated on serine and threonine residues. Hence, p120 appears to be a substrate of both nonreceptor- and ligand-activated transmembrane receptor tyrosine kinases and of serine/threonine kinases and is perhaps a component of both mitogen-stimulated and tyrosine kinase oncogene-induced signaling pathways.
机译：单克隆抗体2B12针对p120，p120是一种120-kDa细胞蛋白，最初被鉴定为表达pp60src膜相关致癌变体的细胞中的蛋白酪氨酸激酶底物。在此报告中，我们显示p120在表达膜相关，酶促激活的c-src变体的禽类细胞中被酪氨酸磷酸化，包括在src同源性区域2和3中具有结构改变的变体。相反，p120在酪氨酸中没有被酪氨酸磷酸化表达酶激活的非肉豆蔻基化的pp60src的细胞。此外，p120在表达中间T抗原，多瘤病毒的转化蛋白的禽类细胞以及被表皮生长因子（EGF）或血小板衍生的生长因子刺激的啮齿类动物细胞中被酪氨酸磷酸化。对EGF刺激的细胞中p120酪氨酸磷酸化的时间过程的分析显示，酪氨酸磷酸化迅速开始。另外，当用EGF刺激过表达EGF受体的细胞时，p120磷酸化的程度和持续时间均增加。生化分析表明，p120（在正常细胞和src转化细胞中）均与膜相关，被肉豆蔻酰化，并在丝氨酸和苏氨酸残基上被磷酸化。因此，p120似乎是非受体和配体激活的跨膜受体酪氨酸激酶和丝氨酸/苏氨酸激酶的底物，并且可能是促分裂原刺激和酪氨酸激酶致癌基因诱导的信号通路的组成部分。

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