Sefton B M, Hunter T, Ball E H, Singer S J
Cell. 1981 Apr;24(1):165-74. doi: 10.1016/0092-8674(81)90512-2.
Vinculin, a protein associated with the cytoplasmic face of the focal adhesion plaques which anchor actin-containing microfilaments to the plasma membrane and attach a cell to the substratum, contains 8-fold more phosphotyrosine in cells transformed by Rous sarcoma virus than in uninfected cells. Because the transforming protein of RSV, p60src, is a protein kinase that modifies cellular proteins through the phosphorylation of tyrosine and because phosphotyrosine is a very rare modified amino acid, this result is a very rare modified amino acid, this result suggests that vinculin is a primary substrate of p60src. Only trace amounts of phosphotyrosine were detected in myosin heavy chains, alpha-actinin, filamin, and the intermediate filament protein vimentin. The modification of vinculin by p60src may be responsible in part for the disruption of the microfilament organization and for the changes in cell shape and adhesiveness which accompany transformation by Rous sarcoma virus.
纽蛋白是一种与粘着斑的胞质面相关的蛋白质，粘着斑将含肌动蛋白的微丝锚定到质膜上，并使细胞附着于基质。在经劳氏肉瘤病毒转化的细胞中，纽蛋白所含的磷酸酪氨酸比未感染细胞中的多8倍。由于劳氏肉瘤病毒的转化蛋白p60src是一种通过酪氨酸磷酸化来修饰细胞蛋白的蛋白激酶，且磷酸酪氨酸是一种非常罕见的修饰氨基酸，这一结果表明纽蛋白是p60src的主要底物。在肌球蛋白重链、α-辅肌动蛋白、细丝蛋白和中间丝蛋白波形蛋白中仅检测到微量的磷酸酪氨酸。p60src对纽蛋白的修饰可能部分导致了微丝组织的破坏以及伴随劳氏肉瘤病毒转化而来的细胞形状和粘附性的变化。
