1. Daxx is reciprocally regulated by Mdm2 and Hausp.
- Author
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Tang J, Qu L, Pang M, and Yang X
- Subjects
- Cell Line, Tumor, Co-Repressor Proteins, Humans, Molecular Chaperones, Ubiquitin-Specific Peptidase 7, Adaptor Proteins, Signal Transducing metabolism, Nuclear Proteins metabolism, Proto-Oncogene Proteins c-mdm2 metabolism, Ubiquitin Thiolesterase metabolism, Ubiquitination
- Abstract
Daxx is a multifunctional protein, regulating a wide range of important functions including apoptosis and transcription. However, the way Daxx is regulated is poorly understood. In our previous studies, we have found that Daxx forms a complex with the E3 ubiquitin ligase Mdm2 and the de-ubiquitinase Hausp. In the present work, we show that Daxx is ubiquitinated by Mdm2 in both in vitro and in vivo systems and Mdm2 reduces Daxx expression upon over-expression. We further demonstrate that Hausp critically controls the cellular level of Daxx most likely by inducing Daxx de-ubiquitination. These results reveal Mdm2 and Hausp as important regulators for Daxx functions by controlling Daxx ubiquitination and stability., (2010 Elsevier Inc. All rights reserved.)
- Published
- 2010
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