ACTIVATION OF EXTRACELLULAR SIGNAL-REGULATED KINASE, ERK2, BY P21RAS ONCOPROTEIN
ACTIVATION OF EXTRACELLULAR SIGNAL-REGULATED KINASE, ERK2, BY P21RAS ONCOPROTEIN
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DOI：
10.1002/j.1460-2075.1992.tb05088.x
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发表时间：
1992-02-01
期刊：
影响因子：
11.4
通讯作者：
MARSHALL, CJ
中科院分区：
文献类型：
--
作者：
LEEVERS, SJ;MARSHALL, CJ
为了检验致癌p21ras激活的信号转导事件，我们研究了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），在对致癌p21ras的反应中，通过酪氨酸和苏氨酸的磷酸化激活，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从外部信号中解耦激酶激活。在ras转化细胞系中，这些激酶被组成性激活。我们认为这些激酶是p21ras癌蛋白激活的信号转导途径的重要组成部分。
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.