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Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation

J Han1, Y Jiang, Z Li

  • 1Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA. jhan@scripps.edu

Nature
|March 20, 1997
PubMed

Insights

Lipopolysaccharide (LPS) triggers innate immune cells via MAP kinase (MAPK) pathways. This study reveals p38-mediated phosphorylation activates MEF2C transcription, increasing c-jun gene expression for host defense.

Area of Science:

  • Immunology
  • Cellular Biology
  • Molecular Signaling

Background:

  • Innate immune cells recognize microbial products like lipopolysaccharide (LPS) to initiate host defense.
  • Intracellular signaling pathways, including mitogen-activated protein kinase (MAPK) pathways, are crucial for cellular responses to infection.
  • The MAPK p38 is implicated in regulating cellular responses and pro-inflammatory molecule expression during infection.

Purpose of the Study:

  • To investigate the role of p38 in innate immune responses.
  • To identify proteins whose functions are regulated by p38-catalyzed phosphorylation.
  • To elucidate the link between the p38 pathway and transcription factors involved in host defense.

Main Methods:

  • Investigated the effect of LPS on monocytic cells.
  • Analyzed the activation of MEF2C transcription factor.
  • Examined p38-catalyzed phosphorylation of MEF2C.
  • Measured c-jun gene transcription levels.

Main Results:

  • Lipopolysaccharide (LPS) stimulation increases the transactivation activity of MEF2C in monocytic cells.
  • MEF2C activation is mediated by p38-catalyzed phosphorylation.
  • MEF2C activation leads to increased transcription of the c-jun gene.
  • The p38 pathway influences c-Jun protein levels during infection.

Conclusions:

  • The p38 pathway plays a significant role in regulating host defense and inflammation.
  • p38-mediated phosphorylation of MEF2C is a key mechanism linking LPS recognition to inflammatory gene expression.
  • This pathway contributes to maintaining the balance of c-Jun protein during infection, impacting cellular defense.

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