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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
50
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pubmed:dateCreated |
2000-1-13
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pubmed:databankReference |
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pubmed:abstractText |
The basic region-leucine zipper transcription factor c-Jun regulates gene expression and cell function. It participates in the formation of homo- or heterodimeric complexes that specifically bind to DNA sequences called activating protein 1 (AP-1) sites. The stability and activity of c-Jun is regulated by phosphorylation within the N-terminal activation domain. Mitogen- and stress-activated c-Jun N-terminal kinases (JNKs) were previously the only described enzymes phosphorylating c-Jun at the N terminus in vivo. In this report we demonstrate a JNK-independent activation of c-Jun in vivo directed by the constitutive photomorphogenesis (COP9) signalosome. The overexpression of signalosome subunit 2 (Sgn2), a subunit of the COP9 signalosome, leads to de novo assembly of the complex with a partial incorporation of the overexpressed subunit. The de novo formation of COP9 signalosome parallels an increase of c-Jun protein resulting in elevated AP-1 transcriptional activity. The c-Jun activation caused by Sgn2 overexpression is independent of JNK and mitogen-activated protein kinase kinase 4. The data demonstrate the existence of a novel COP9 signalosome-directed c-Jun activation pathway.
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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/COPS2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/COPS5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GPS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase 4,
http://linkedlifedata.com/resource/pubmed/chemical/MAP2K4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-jun,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-1,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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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 |
10
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35297-300
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10585392-DNA-Binding Proteins,
pubmed-meshheading:10585392-Erythrocytes,
pubmed-meshheading:10585392-GTP-Binding Proteins,
pubmed-meshheading:10585392-Genes, Reporter,
pubmed-meshheading:10585392-HeLa Cells,
pubmed-meshheading:10585392-Humans,
pubmed-meshheading:10585392-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10585392-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:10585392-MAP Kinase Kinase 4,
pubmed-meshheading:10585392-Mitogen-Activated Protein Kinase Kinases,
pubmed-meshheading:10585392-Mitogen-Activated Protein Kinases,
pubmed-meshheading:10585392-Molecular Sequence Data,
pubmed-meshheading:10585392-Peptide Hydrolases,
pubmed-meshheading:10585392-Phosphorylation,
pubmed-meshheading:10585392-Protein-Tyrosine Kinases,
pubmed-meshheading:10585392-Proteins,
pubmed-meshheading:10585392-Proto-Oncogene Proteins c-jun,
pubmed-meshheading:10585392-Recombinant Fusion Proteins,
pubmed-meshheading:10585392-Recombinant Proteins,
pubmed-meshheading:10585392-Repressor Proteins,
pubmed-meshheading:10585392-Sequence Deletion,
pubmed-meshheading:10585392-Transcription Factor AP-1,
pubmed-meshheading:10585392-Transcription Factors,
pubmed-meshheading:10585392-Transcriptional Activation,
pubmed-meshheading:10585392-Transfection
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pubmed:year |
1999
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pubmed:articleTitle |
COP9 signalosome-directed c-Jun activation/stabilization is independent of JNK.
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pubmed:affiliation |
Max-Planck-Institut für Infektionsbiologie, Abteilung Molekulare Biologie, Humboldt University, 10117 Berlin, Germany. naumann@mpiib-berlin.mpg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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