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Papers In Press, published online ahead of print January 6, 2005
J. Biol. Chem, 10.1074/jbc.M409161200
Submitted on August 10, 2004
Revised on January 6, 2005
Accepted on January 6, 2005

Daxx mediates the SUMO-dependent transcriptional repression of Smad4

Che-Chang Chang, Ding-Yen Lin, Hsin-I Fang, Ruey-Hwa Chen, and Hsiu-Ming Shih

Institute of Biomedical Sciences, Academia Sinica, Taipei 11529

Corresponding Author: hmshih{at}ibms.sinica.edu.tw

Daxx has been shown to function as an apoptosis regulator and transcriptional repressor via its interaction with various cytoplasmic and nuclear proteins. Here, we showed that Daxx interacts with Smad4 and represses its transcriptional activity via the COOH domain of Daxx. In vitro and in vivo interaction studies indicated that the binding of Smad4 to Daxx depends on Smad4 sumoylation. Substitution of Smad4 SUMO-conjugation residue lysine 159, but not 113, to arginine not only disrupted Smad4-Daxx interaction but also relieved Daxx-elicited repression of Smad4 transcriptional activity. Furthermore, chromatin immunoprecipitation analyses revealed the recruitment of Daxx to an endogenous, Smad4-targeted promoter through a K159 sumoylation-dependent manner. Finally, downregulation of Daxx expression by RNA interference enhanced TGF-beta-induced transcription of reporter and endogenous genes through a Smad4-, but not K159R-Smad4-, dependent manner. Together, these results indicate that Daxx suppresses Smad4-mediated transcriptional activity by direct interaction with the sumoylated Smad4 and identify a novel role of Daxx in regulating TGF-beta signaling.


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