A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells

Science. 1994 Aug 5;265(5173):808-11. doi: 10.1126/science.7914033.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases / chemistry*
  • Calcium-Calmodulin-Dependent Protein Kinases / genetics
  • Cell Line
  • Endotoxins / pharmacology*
  • Genetic Complementation Test
  • Lipopolysaccharides / pharmacology
  • Macrophages, Peritoneal / enzymology
  • Mice
  • Mice, Inbred C3H
  • Mitogen-Activated Protein Kinases*
  • Molecular Sequence Data
  • Osmotic Pressure
  • Paclitaxel / pharmacology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid
  • Water-Electrolyte Balance / physiology*
  • p38 Mitogen-Activated Protein Kinases


  • Endotoxins
  • Lipopolysaccharides
  • Saccharomyces cerevisiae Proteins
  • Calcium-Calmodulin-Dependent Protein Kinases
  • HOG1 protein, S cerevisiae
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases
  • Paclitaxel

Associated data

  • GENBANK/L35253
  • GENBANK/U10871