Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cells, Cultured
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DNA-Binding Proteins / physiology
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Enzyme Activation
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Gene Expression Regulation, Enzymologic
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Genes, Reporter
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Humans
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Luciferases / metabolism
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Mitogen-Activated Protein Kinase 1 / genetics
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Mitogen-Activated Protein Kinase 1 / metabolism*
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Mitogen-Activated Protein Kinases / metabolism
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Nuclear Proteins / physiology
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Protein Kinase C / metabolism*
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Proto-Oncogene Proteins / physiology
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Proto-Oncogene Proteins c-raf / metabolism
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Serum Response Factor
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Transcription Factors*
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Transcription, Genetic
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Transcriptional Activation
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Transfection
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ets-Domain Protein Elk-1
Substances
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DNA-Binding Proteins
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ELK1 protein, human
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Nuclear Proteins
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Proto-Oncogene Proteins
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Serum Response Factor
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Transcription Factors
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ets-Domain Protein Elk-1
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Luciferases
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protein kinase D
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Proto-Oncogene Proteins c-raf
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Protein Kinase C
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Mitogen-Activated Protein Kinase 1
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Mitogen-Activated Protein Kinases