Abstract

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 HOG1 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.

Keywords

MAPK7Mitogen-activated protein kinase kinaseMAP kinase kinase kinaseMAPKAPK2ASK1Mitogen-activated protein kinasep38 mitogen-activated protein kinasesMAP2K7Cell biologyBiologyProtein kinase APhosphorylationKinaseTyrosine kinaseCyclin-dependent kinase 2Molecular biologySignal transduction

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Publication Info

Year
1994
Type
article
Volume
265
Issue
5173
Pages
808-811
Citations
2651
Access
Closed

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Jiahuai Han, Jeffrey Lee, L. Bibbs et al. (1994). A MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells. Science , 265 (5173) , 808-811. https://doi.org/10.1126/science.7914033

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DOI
10.1126/science.7914033