Sounding the Alarm: Protein Kinase Cascades Activated by Stress and Inflammation*

Eukaryotic cells respond to extracellular stimuli by recruiting signal transduction pathways, many of which employ protein Ser/ Thr kinases of the ERK 1 family. The ubiquity of ERKs and their upstream activators, the MEKs, in signal transduction was first appreciated from studies of yeast (1, 2). Although a 54-kDa rat liver c-Jun kinase (SAPK-p54 (cid:97) 1) with properties similar to the Ras-regulated MAPKs had been characterized (3–5), the physiologic roles and regulation of this and related mammalian enzymes have emerged only recently. Molecular cloning of the SAPKs and p38s, together with the paradigms derived from the “classical” MAPKs and work in lower eukaryotes has enabled rapid elucidation of the regulation and cellular functions of these newer mammalian ERK pathways. Although architecturally homologous to the Ras/MAPK pathway, the SAPK and p38 pathways are not activated primarily by mitogens but by cellular stresses and inflammatory cytokines, which stimuli result in growth arrest, apoptosis, or activation of immune and reticuloendothelial cells. homologues yeast-osmosensing Tyr-phosphorylated Lipopolysaccharide lipopo-lysaccharide-stimulated the MEKKs SPS1-like Pyk2 couple UV osmotic shock

• Publication year

  1996

• Venue

  Journal of Biological Chemistry

• Publication date

  1996-10-04

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1074/jbc.271.40.24313PMID 8798679
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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