A MAP KINASE TARGETED BY ENDOTOXIN AND HYPEROSMOLARITY IN MAMMALIAN-CELLS
A MAP KINASE TARGETED BY ENDOTOXIN AND HYPEROSMOLARITY IN MAMMALIAN-CELLS
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DOI：
10.1126/science.7914033
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发表时间：
1994-08-05
期刊：
影响因子：
56.9
通讯作者：
ULEVITCH, RJ
中科院分区：
文献类型：
--
作者：
HAN, J;LEE, JD;ULEVITCH, RJ
哺乳动物细胞通过激活蛋白激酶级联反应来响应内毒素脂多糖（LPS），从而导致新的基因表达。一种蛋白激酶，p38，这是酪氨酸磷酸化的LPS，被克隆。p38酶和酿酒酵母HOG 1基因的产物都是促分裂原活化蛋白（MAP）激酶家族的成员，它们在关键磷酸化位点处和附近具有将这些蛋白质与大多数其他MAP激酶家族成员区分开的序列。HOG1和p38在细胞外渗透压变化后都被酪氨酸磷酸化。这些发现将哺乳动物细胞中的信号通路与酵母中对生理应激反应的通路联系起来。
Mammalian cells respond to endotoxic lipopolysaccharide (LPS) by activation of protein kinase cascades that lead to new gene expression. A protein kinase, p38, that was tyrosine phosphorylated in response to LPS, was cloned. The p38 enzyme and the product of the Saccharomyces cerevisiae HOG 1 gene, which are both members of the mitogen-activated protein (MAP) kinase family, have sequences at and adjacent to critical phosphorylation sites that distinguish these proteins from most other MAP kinase family members. Both HOG1 and p38 are tyrosine phosphorylated after extracellular changes in osmolarity. These findings link a signaling pathway in mammalian cells with a pathway in yeast that is responsive to physiological stress.