Pasquale E B, Maher P A, Singer S J
Proc Natl Acad Sci U S A. 1986 Aug;83(15):5507-11. doi: 10.1073/pnas.83.15.5507.
We have examined the extent of tyrosine phosphorylation of talin, a component of the cytoskeleton localized in the focal adhesions and, therefore, a potential substrate of p60v-src, the transforming protein of Rous sarcoma virus. p60v-src is a tyrosine kinase that induces high levels of phosphotyrosine and the disorganization of the cytoskeleton in transformed cells. With a polyclonal antibody utilized in a previous study [Maher, P. A., Pasquale, E. B., Wang, J. Y. J. & Singer, S. J. (1985) Proc. Natl. Acad. Sci. USA 82, 6576-6580] for the detection of tyrosine-phosphorylated proteins, we have detected phosphotyrosine residues in talin molecules immunoprecipitated from Rous sarcoma virus-transformed, but not normal, chicken embryo fibroblasts. Phospho amino acid analysis of talin from the infected cells confirmed the presence of phosphotyrosine, in addition to phosphoserine and phosphothreonine. The extent of tyrosine modification in talin was compared to that in vinculin, the other focal adhesion component previously found to contain enhanced levels of phosphotyrosine in various retrovirus-transformed cells. A considerably (3 times) larger fraction of the talin than of the vinculin molecules was found to be phosphorylated on tyrosine. The phosphorylation of talin on tyrosine may be crucial for the expression of the abnormal morphology characteristic of cells transformed by Rous sarcoma virus.
我们研究了踝蛋白的酪氨酸磷酸化程度，踝蛋白是一种细胞骨架成分，定位于粘着斑，因此是罗氏肉瘤病毒转化蛋白p60v-src的潜在底物。p60v-src是一种酪氨酸激酶，可在转化细胞中诱导高水平的磷酸酪氨酸并导致细胞骨架紊乱。利用先前研究[Maher, P. A., Pasquale, E. B., Wang, J. Y. J. & Singer, S. J. (1985) Proc. Natl. Acad. Sci. USA 82, 6576 - 6580]中用于检测酪氨酸磷酸化蛋白的多克隆抗体，我们在从罗氏肉瘤病毒转化的而非正常的鸡胚成纤维细胞免疫沉淀的踝蛋白分子中检测到了磷酸酪氨酸残基。对感染细胞中踝蛋白的磷酸氨基酸分析证实，除了磷酸丝氨酸和磷酸苏氨酸外，还存在磷酸酪氨酸。将踝蛋白中酪氨酸修饰的程度与纽蛋白中的进行了比较，纽蛋白是先前在各种逆转录病毒转化细胞中发现含有增强水平磷酸酪氨酸的另一种粘着斑成分。发现踝蛋白分子中被磷酸化的酪氨酸部分比纽蛋白分子的大得多（3倍）。踝蛋白酪氨酸磷酸化可能对于罗氏肉瘤病毒转化细胞所特有的异常形态的表达至关重要。
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