JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun
Open Access
- 15 July 2003
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 22 (14) , 3686-3695
- https://doi.org/10.1093/emboj/cdg364
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.Keywords
This publication has 32 references indexed in Scilit:
- Transcriptional regulation by the phosphorylation-dependent factor CREBNature Reviews Molecular Cell Biology, 2001
- AP-1 in mouse development and tumorigenesisOncogene, 2001
- Requirement of JNK for Stress- Induced Activation of the Cytochrome c-Mediated Death PathwayScience, 2000
- Diverse functions of JNK signaling and c-Jun in stress response and apoptosisOncogene, 1999
- JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domainPublished by Elsevier ,1994
- Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.Genes & Development, 1993
- The cell-type-specific activator region of c-Jun juxtaposes constitutive and negatively regulated domains.Genes & Development, 1992
- Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73Nature, 1991
- Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domainNature, 1991
- Control of c-Jun activity by interaction of a cell-specific inhibitor with regulatory domain δ: Differences between v- and c-JunCell, 1990