Abstract
Transcription factor AP-1 transduces environmental signals to the transcriptional machinery. To ensure a quick response yet maintain tight control over AP-1 target genes, AP-1 activity is likely to be negatively regulated in nonstimulated cells. To identify proteins that interact with the Jun subunits of AP-1 and repress its activity, we developed a novel screen for detecting protein-protein interactions that is not based on a transcriptional readout. In this system, the mammalian guanyl nucleotide exchange factor (GEF) Sos is recruited to the Saccharomyces cerevisiae plasma membrane harboring a temperature-sensitive Ras GEF, Cdc25-2, allowing growth at the nonpermissive temperature. Using the Sos recruitment system, we identified new c-Jun-interacting proteins. One of these, JDP2, heterodimerizes with c-Jun in nonstimulated cells and represses AP-1-mediated activation.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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3T3 Cells
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Amino Acid Sequence
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Animals
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Cell Cycle Proteins
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Dimerization
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Electrophoresis, Polyacrylamide Gel
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Genetic Techniques
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Mice
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Models, Molecular
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Molecular Sequence Data
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Phosphatidylinositol 3-Kinases
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Phosphoprotein Phosphatases
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Phosphotransferases (Alcohol Group Acceptor) / metabolism
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Protein Binding
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Proto-Oncogene Proteins c-fos / metabolism
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Proto-Oncogene Proteins c-jun / metabolism*
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Repressor Proteins / isolation & purification*
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Repressor Proteins / metabolism
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Transcription Factor AP-1 / metabolism*
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Transcription, Genetic / drug effects*
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ras-GRF1
Substances
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Cell Cycle Proteins
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Jundp2 protein, mouse
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Proto-Oncogene Proteins c-fos
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Proto-Oncogene Proteins c-jun
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Repressor Proteins
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Transcription Factor AP-1
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ras-GRF1
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Phosphatidylinositol 3-Kinases
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Phosphotransferases (Alcohol Group Acceptor)
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Phosphoprotein Phosphatases