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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
2001-3-15
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pubmed:abstractText |
Here we show that human protein kinase C mu (PKC mu) activates the mitogen-activated protein kinase (MAPK). Transient expression of constitutive active PKC mu leads to an activation of Raf-1 kinase as demonstrated by in vitro phosphorylation of MAPK. PKC mu enhances transcriptional activity of a basal thymidine kinase promotor containing serum response elements (SREs) as shown by luciferase reporter gene assays. SRE driven gene activation by PKC mu is triggered by the Elk-1 ternary complex factor. PKC mu-mediated activation of SRE driven transcription can be inhibited by the MEK1 inhibitor PD98059. In contrast to the activation of the p42/ERK1 MAPK cascade, transient expression of constitutive active PKC mu does neither affect c-jun N-terminal kinase nor p38 MAPK.
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ELK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-raf,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Response Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/ets-Domain Protein Elk-1,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase D
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
492
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39-44
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11248233-Cells, Cultured,
pubmed-meshheading:11248233-DNA-Binding Proteins,
pubmed-meshheading:11248233-Enzyme Activation,
pubmed-meshheading:11248233-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:11248233-Genes, Reporter,
pubmed-meshheading:11248233-Humans,
pubmed-meshheading:11248233-Luciferases,
pubmed-meshheading:11248233-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:11248233-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11248233-Nuclear Proteins,
pubmed-meshheading:11248233-Protein Kinase C,
pubmed-meshheading:11248233-Proto-Oncogene Proteins,
pubmed-meshheading:11248233-Proto-Oncogene Proteins c-raf,
pubmed-meshheading:11248233-Serum Response Factor,
pubmed-meshheading:11248233-Transcription, Genetic,
pubmed-meshheading:11248233-Transcription Factors,
pubmed-meshheading:11248233-Transcriptional Activation,
pubmed-meshheading:11248233-Transfection,
pubmed-meshheading:11248233-ets-Domain Protein Elk-1
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pubmed:year |
2001
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pubmed:articleTitle |
Protein kinase C mu selectively activates the mitogen-activated protein kinase (MAPK) p42 pathway.
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pubmed:affiliation |
Institute of Cell Biology and Immunology, University of Stuttgart, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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