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JNK phosphorylation relieves HDAC3‐dependent suppression of the transcriptional activity of c‐Jun
Author(s) -
Weiss Carsten,
Schneider Sandra,
Wagner Erwin F.,
Zhang Xiaohong,
Seto Edward,
Bohmann Dirk
Publication year - 2003
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdg364
Subject(s) - biology , phosphorylation , hdac3 , microbiology and biotechnology , c jun , transcriptional activity , transcription factor , biochemistry , gene , histone , histone deacetylase
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.