Kamata T, Kung H F
Program Resources, Inc., National Cancer Institute-Frederick Cancer Research Facility, Maryland 21701.
Mol Cell Biol. 1990 Mar;10(3):880-6. doi: 10.1128/mcb.10.3.880-886.1990.
Using Xenopus oocytes as a model system, we investigated the possible involvement of ras proteins in the pathway leading to phosphorylation of ribosomal protein S6. Our results indicate that microinjection of oncogenic T24 H-ras protein (which contains valine at position 12) markedly stimulated S6 phosphorylation on serine residues in oocytes, whereas normal ras protein (which contains glycine at position 12) was without effect. The S6 phosphorylation activity in the cell extract from T24 ras protein-injected oocytes was increased significantly. In addition, injection of protein kinase C potentiated the induction of maturation and S6 phosphorylation by the oncogenic ras protein. A similar potentiation was detected when T24 ras protein-injected oocytes were incubated with active phorbol ester. These findings suggest that ras proteins activate the pathway linked to S6 phosphorylation and that protein kinase C has a synergistic effect on the ras-mediated pathway.
我们以非洲爪蟾卵母细胞作为模型系统,研究了Ras蛋白在导致核糖体蛋白S6磷酸化的信号通路中可能发挥的作用。我们的结果表明,显微注射致癌性T24 H-Ras蛋白(第12位氨基酸为缬氨酸)可显著刺激卵母细胞中丝氨酸残基上的S6磷酸化,而正常Ras蛋白(第12位氨基酸为甘氨酸)则无此作用。注射T24 Ras蛋白的卵母细胞的细胞提取物中的S6磷酸化活性显著增加。此外,注射蛋白激酶C可增强致癌性Ras蛋白诱导的成熟和S6磷酸化。当将注射了T24 Ras蛋白的卵母细胞与活性佛波酯一起孵育时,也检测到了类似的增强作用。这些发现表明,Ras蛋白激活了与S6磷酸化相关的信号通路,并且蛋白激酶C对Ras介导的信号通路具有协同作用。