Axin bridges Daxx to p53
The death domain-associated protein Daxx exerts many reported functions that include mediating the signaling from FasL to apoptosis via activating the c-Jun N-terminal kinase (JNK), induction and inhibition of apoptosis, and regulation of chromatin remodeling. It was originally cloned from a yeast t...
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Veröffentlicht in: | Cell research 2007-04, Vol.17 (4), p.301-302 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The death domain-associated protein Daxx exerts many reported functions that include mediating the signaling from FasL to apoptosis via activating the c-Jun N-terminal kinase (JNK), induction and inhibition of apoptosis, and regulation of chromatin remodeling. It was originally cloned from a yeast two-hybrid screen using the intracellular tail of the Fas receptor as the bait. Whereas many of the initial reports remain controversial, it is clear that Daxx plays important roles in the regulation of apoptosis triggered by a series of stress signals including UV irradiation, hydrogen peroxide treatment and TGF- beta treatment. In this Commentary, we focus on Axin being a tethering factor linking Daxx to p53. |
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ISSN: | 1001-0602 1748-7838 |
DOI: | 10.1038/cr.2007.16 |