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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 RIS Download

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

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Associated grants

  • Agency: NCI NIH HHS, Id: CA58396

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