These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun.
    Author: Weiss C, Schneider S, Wagner EF, Zhang X, Seto E, Bohmann D.
    Journal: EMBO J; 2003 Jul 15; 22(14):3686-95. PubMed ID: 12853483.
    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.
    [Abstract] [Full Text] [Related] [New Search]