Leevers S J, Marshall C J
Section of Cell and Molecular Biology, Institute of Cancer Research, Chester Beatty Laboratories, London, UK.
EMBO J. 1992 Feb;11(2):569-74. doi: 10.1002/j.1460-2075.1992.tb05088.x.
To examine signal transduction events activated by oncogenic p21ras, we have studied kinases that are activated following the scrape loading of p21ras into quiescent cells. We observe rapid activation of 42 kDa and 46 kDa protein kinases. The 42 kDa kinase is the mitogen and extracellular-signal regulated kinase ERK2, (MAP2 kinase), which is activated by phosphorylation on tyrosine and threonine in response to oncogenic p21ras, while the 46 kDa kinase is likely to be another member of the ERK family. Stimulation of these kinases by oncogenic p21ras does not require the presence of growth factors, showing that oncogenic p21ras uncouples kinase activation from external signals. In ras transformed cell lines, these kinases are constitutively activated. We propose that the kinases are important components of the signal transduction pathway activated by p21ras oncoprotein.
为了研究致癌性p21ras激活的信号转导事件，我们研究了在将p21ras刮入静止细胞后被激活的激酶。我们观察到42 kDa和46 kDa蛋白激酶的快速激活。42 kDa激酶是丝裂原和细胞外信号调节激酶ERK2（MAP2激酶），它在致癌性p21ras作用下通过酪氨酸和苏氨酸磷酸化而被激活，而46 kDa激酶可能是ERK家族的另一个成员。致癌性p21ras对这些激酶的刺激不需要生长因子的存在，这表明致癌性p21ras使激酶激活与外部信号解偶联。在ras转化的细胞系中，这些激酶被组成性激活。我们提出这些激酶是由p21ras癌蛋白激活的信号转导途径的重要组成部分。
