THE PRIMARY STRUCTURE OF MEK, A PROTEIN-KINASE THAT PHOSPHORYLATES THE ERK GENE-PRODUCT
THE PRIMARY STRUCTURE OF MEK, A PROTEIN-KINASE THAT PHOSPHORYLATES THE ERK GENE-PRODUCT
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DOI：
10.1126/science.1411546
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发表时间：
1992-10-16
期刊：
影响因子：
56.9
通讯作者：
ERIKSON, RL
中科院分区：
文献类型：
--
作者：
CREWS, CM;ALESSANDRINI, A;ERIKSON, RL
丝裂原活化蛋白（MAP）激酶，也被称为细胞外信号调节激酶（ERKs），被认为是多种生化信号的整合点，因为它们被多种细胞外信号激活，在苏氨酸和酪氨酸上迅速磷酸化，并且高度保守。一个关键的蛋白激酶位于MAP激酶的上游，刺激MAP激酶的酶活性。这种蛋白激酶的结构被称为MEK1，即MAP激酶或ERK激酶，从一个互补的DNA序列中被阐明，并被证明是一个由393个氨基酸（43,500道尔顿）组成的蛋白质，在大小和序列上与裂糖酵母pombe byr1基因编码的产物最密切相关。MEK基因在鼠脑中高表达，细菌中表达的产物使ERK基因产物磷酸化。
Mitogen-activated protein (MAP) kinases, also known as extracellular signal-regulated kinases (ERKs), are thought to act at an integration point for multiple biochemical signals because they are activated by a wide variety of extracellular signals, rapidly phosphorylated on threonine and tyrosine, and highly conserved. A critical protein kinase lies upstream of MAP kinase and stimulates the enzymatic activity of MAP kinase. The structure of this protein kinase, denoted MEK1, for MAP kinase or ERK kinase, was elucidated from a complementary DNA sequence an shown to be a protein of 393 amino acids (43,500 daltons) that is related most closely in size and sequence to the product encoded by the Schizosaccharomyces pombe byr1 gene. The MEK gene was highly expressed in murine brain, and the product expressed in bacteria phosphorylated the ERK gene product.