Gacon G, Gisselbrecht S, Piau J P, Fiszman M Y, Fischer S
Eur J Biochem. 1982 Jul;125(2):453-6. doi: 10.1111/j.1432-1033.1982.tb06704.x.
The transforming protein of Rous' sarcoma virus (RSV) is a phosphoprotein of Mr 60 000 (pp60src) which displays protein kinase activity specific for tyrosine residues; pp60src is associated with the plasma membrane and is recovered in the detergent-insoluble material which represents the subcellular matrix of the cell. After phosphorylation of this material of RSV-transformed cells with [gamma-32P]ATP, five phosphoproteins have been detected which are not seen in normal cells. These proteins (Mr = 135 000, 125 000, 75 000, 70 000, 60 000) contain phosphotyrosine. Their phosphorylation is strongly inhibited by anti-pp60src antibodies. In cells transformed by a temperature-sensitive mutant of RSV, these phosphoproteins, present at the permissive temperature, are no longer detected at the non-permissive temperature. It is concluded that these phosphorylations are mediated by pp60src protein kinase activity. This supports a possible role of the phosphorylation of cytoskeletal proteins in the transformation process.
劳氏肉瘤病毒（RSV）的转化蛋白是一种分子量为60000的磷蛋白（pp60src），它具有对酪氨酸残基特异的蛋白激酶活性；pp60src与质膜相关，并存在于代表细胞亚细胞基质的去污剂不溶性物质中。用[γ-32P]ATP对RSV转化细胞的这种物质进行磷酸化后，检测到了五种在正常细胞中未见的磷蛋白。这些蛋白（分子量分别为135000、125000、75000、70000、60000）含有磷酸酪氨酸。它们的磷酸化受到抗pp60src抗体的强烈抑制。在由RSV的温度敏感突变体转化的细胞中，这些在允许温度下存在的磷蛋白，在非允许温度下不再被检测到。结论是这些磷酸化是由pp60src蛋白激酶活性介导的。这支持了细胞骨架蛋白磷酸化在转化过程中可能发挥的作用。
