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

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

Authors

  • Weiss C
  • Schneider S
  • Wagner EF
  • Zhang X
  • Seto E
  • Bohmann D

Journal

The EMBO journal

Publication Data

July 15, 2003

Associated Grants

None

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