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

Carsten Weiss, Sandra Schneider, Erwin F. Wagner, Xiaohong Zhangs, Edward Seto, Dirk Bohmann

Research output: Contribution to journalArticlepeer-review

138 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)3686-3695
Number of pages10
JournalEMBO Journal
Volume22
Issue number14
DOIs
StatePublished - 15 Jul 2003
Externally publishedYes

Keywords

  • HDAC
  • MAP kinase
  • Phosphorylation
  • Repression of transcription
  • Signaling
  • c-Jun transcription factor

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