A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells.

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ID: 281484
1994
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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.
Reference Key
han1994a Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Jiahuai Han; J.-D. Lee; L. Bibbs; R. Ulevitch
Journal Science
Year 1994
DOI
10.1126/SCIENCE.7914033
URL
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