A MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells
- 5 August 1994
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 265 (5173) , 808-811
- https://doi.org/10.1126/science.7914033
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
This publication has 20 references indexed in Scilit:
- JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domainPublished by Elsevier ,1994
- Recognition of endotoxin by cells leading to transmembrane signalingCurrent Opinion in Immunology, 1994
- Atomic structure of the MAP kinase ERK2 at 2.3 Å resolutionNature, 1994
- The MAP kinase cascade is essential for diverse signal transduction pathwaysTrends in Biochemical Sciences, 1993
- An Osmosensing Signal Transduction Pathway in YeastScience, 1993
- Heterogeneous expression of four MAP kinase isoforms in human tissuesFEBS Letters, 1992
- Internal protein sequence analysis: Enzymatic digestion for less than 10 μg of protein bound to polyvinylidene difluoride or nitrocellulose membranesAnalytical Biochemistry, 1992
- ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGFCell, 1991
- Shared Actions of Endotoxin and Taxol on TNF Receptors and TNF releaseScience, 1990
- The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic DomainsScience, 1988