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Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine.

Protein kinases activated by dual phosphorylation on Tyr and Thr (MAP kinases) can be grouped into two major classes: ERK and JNK. The ERK group regulates multiple targets in response to growth factors via a Ras-dependent mechanism. In contrast, JNK activates the transcription factor c-Jun in response to pro-inflammatory cytokines and exposure of cells to several forms of environmental stress. Recently, a novel mammalian protein kinase (p38) that shares sequence similarity with mitogen-activated protein (MAP) kinases was identified. Here, we demonstrate that p38, like JNK, is activated by treatment of cells with pro-inflammatory cytokines and environmental stress. The mechanism of p38 activation is mediated by dual phosphorylation on Thr-180 and Tyr-182. Immunofluorescence microscopy demonstrated that p38 MAP kinase is present in both the nucleus and cytoplasm of activated cells. Together, these data establish that p38 is a member of the mammalian MAP kinase group.

Pubmed ID: 7535770


  • Raingeaud J
  • Gupta S
  • Rogers JS
  • Dickens M
  • Han J
  • Ulevitch RJ
  • Davis RJ


The Journal of biological chemistry

Publication Data

March 31, 1995

Associated Grants

  • Agency: NCI NIH HHS, Id: CA58396

Mesh Terms

  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cell Line
  • Cercopithecus aethiops
  • Enzyme Activation
  • HeLa Cells
  • Humans
  • Inflammation
  • Interleukin-1
  • JNK Mitogen-Activated Protein Kinases
  • Lipopolysaccharides
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases
  • Molecular Weight
  • Osmolar Concentration
  • Phosphorylation
  • Phosphothreonine
  • Phosphotyrosine
  • Recombinant Proteins
  • Sequence Deletion
  • Stress, Physiological
  • Subcellular Fractions
  • Substrate Specificity
  • Threonine
  • Transfection
  • Tumor Necrosis Factor-alpha
  • Tyrosine