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JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun.

The EMBO journal | Jul 15, 2003

http://www.ncbi.nlm.nih.gov/pubmed/12853483

The AP-1 transcription factor c-Jun is a prototypical nuclear effector of the JNK signal transduction pathway. The integrity of JNK phosphorylation sites at serines 63/73 and at threonines 91/93 in c-Jun is essential for signal-dependent target gene activation. We show that c-Jun phosphorylation mediates dissociation of an inhibitory complex, which is associated with histone deacetylase 3 (HDAC3). The subsequent events that ultimately cause increased mRNA synthesis are independent of c-Jun phosphorylation and its interaction with JNK. These findings provide an 'activation by de-repression' model as an explanation for the stimulatory function of JNK on c-Jun.

Pubmed ID: 12853483 RIS Download

Mesh terms: 3T3 Cells | Animals | Cell Line | Genes, Reporter | Histone Deacetylases | Humans | JNK Mitogen-Activated Protein Kinases | MAP Kinase Kinase 4 | Mice | Mitogen-Activated Protein Kinase Kinases | Mutagenesis, Site-Directed | Mutation | Phosphorylation | Protein Binding | Protein Structure, Tertiary | Proto-Oncogene Proteins c-jun | RNA, Messenger | Recombinant Fusion Proteins | Sequence Deletion | Serine | Suppression, Genetic | Threonine | Transcription, Genetic | Transcriptional Activation

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