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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
1995-5-10
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphothreonine,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7420-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7535770-Animals,
pubmed-meshheading:7535770-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:7535770-Cell Line,
pubmed-meshheading:7535770-Cercopithecus aethiops,
pubmed-meshheading:7535770-Enzyme Activation,
pubmed-meshheading:7535770-HeLa Cells,
pubmed-meshheading:7535770-Humans,
pubmed-meshheading:7535770-Inflammation,
pubmed-meshheading:7535770-Interleukin-1,
pubmed-meshheading:7535770-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:7535770-Lipopolysaccharides,
pubmed-meshheading:7535770-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:7535770-Mitogen-Activated Protein Kinases,
pubmed-meshheading:7535770-Molecular Weight,
pubmed-meshheading:7535770-Osmolar Concentration,
pubmed-meshheading:7535770-Phosphorylation,
pubmed-meshheading:7535770-Phosphothreonine,
pubmed-meshheading:7535770-Phosphotyrosine,
pubmed-meshheading:7535770-Recombinant Proteins,
pubmed-meshheading:7535770-Sequence Deletion,
pubmed-meshheading:7535770-Stress, Physiological,
pubmed-meshheading:7535770-Subcellular Fractions,
pubmed-meshheading:7535770-Substrate Specificity,
pubmed-meshheading:7535770-Threonine,
pubmed-meshheading:7535770-Transfection,
pubmed-meshheading:7535770-Tumor Necrosis Factor-alpha,
pubmed-meshheading:7535770-Tyrosine
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pubmed:year |
1995
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pubmed:articleTitle |
Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01605, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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