AN INSULIN-STIMULATED PROTEIN-KINASE SIMILAR TO YEAST KINASES INVOLVED IN CELL-CYCLE CONTROL
AN INSULIN-STIMULATED PROTEIN-KINASE SIMILAR TO YEAST KINASES INVOLVED IN CELL-CYCLE CONTROL
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DOI：
10.1126/science.2164259
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发表时间：
1990-07-06
期刊：
影响因子：
56.9
通讯作者：
COBB, MH
中科院分区：
文献类型：
--
作者：
BOULTON, TG;YANCOPOULOS, GD;COBB, MH
一种以磷酸化微管相关蛋白2 （MAP2）的能力为特征的蛋白激酶，被认为是胰岛素刺激磷酸化级联反应和多种其他哺乳动物细胞对细胞外信号反应的早期中间体。已经克隆出编码该蛋白丝氨酸-苏氨酸激酶的互补DNA，该蛋白设计为细胞外信号调节激酶1 （ERK1）。ERK1与酵母中的两种蛋白激酶KSS1和FUS3具有惊人的相似性。酵母激酶以拮抗的方式调节细胞周期以响应交配因子。因此，ERK1和这两种酵母激酶构成了一个进化保守的酶家族，参与调节真核细胞对细胞外信号的反应。
A protein kinase characterized by its ability to phosphorylate microtubule-associated protein-2 (MAP2), is thought to be an early intermediate in an insulin-stimulated phosphorylation cascade and in a variety of other mammalian cell responses to extracellular signals. A complementary DNA that encodes this protein serine-threonine kinase has been cloned, and the protein designed extracellular signal-regulated kinase 1 ( ERK1). ERK1 has striking similarity to two protein kinses, KSS1 and FUS3, from yeast. The yeast kinases function in an antagonistic manner to regulate the cell cycle in response to mating factors. Thus, ERK1 and the two yeast kinases constitute a family of evolutionary conserved enzymes involved in regulating the response of eukaryotic cells to extracellular signals.