A MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells

• J. Han

• J.-D. Lee

• L. Bibbs

• R. J. Ulevitch

抄録

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.

収録刊行物

• Science

  Science 265 (5173), 808-811, 1994-08-05

  American Association for the Advancement of Science (AAAS)

キーワード

• Multidisciplinary

詳細情報

• CRID: 1360574096430537728
• NII論文ID: 80007786240
• DOI: 10.1126/science.7914033
• ISSN: 10959203
• ISSN: 00368075
• ISSN: http://id.crossref.org/issn/00368075
• Web Site: https://www.science.org/doi/pdf/10.1126/science.7914033
• データソース種別:
  • Crossref
  • CiNii Articles