Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Daxx

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_1522-2

Synonyms

Definition

Daxx was originally identified as a protein factor that binds to a transmembrane receptor called Fas (FAS/APO-1/CD95), one member of the tumor necrosis factor receptor superfamily (Yang et al. 1997). The extracellular region of Fas is where its ligand, FasL, binds. The intracellular tail shares sequence similarity with another member of the TNF receptor family, TNF receptor I (TNFRI). The shared sequence is termed death domain for its critical role in signaling cell death upon ligand binding.

Characteristics

Since its identification in 1997, Daxx has been intensively investigated for its biological functions. However, up to date the three-dimensional crystal structure of Daxx has not been resolved. Human Daxx protein is a polypeptide of 740 amino acid residues in length. As depicted in the schematic diagram (Fig. 1), Daxx contains several putative domains and many binding sites for interacting with a...

Keywords

Nuclear Body Arsenic Trioxide Mouse Double Minute Tumor Necrosis Factor Receptor Superfamily Important Tumor Suppressor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Li Q, Wang X, Wu X et al (2007) Daxx cooperates with the Axin/HIPK2/p53 complex to induce cell death. Cancer Res 67:66–74CrossRefPubMedGoogle Scholar
  2. Salomoni P, Khelifi AF (2006) Daxx: death or survival protein. Trends Cell Biol 16:97–104CrossRefPubMedGoogle Scholar
  3. Tang J, Qu L-K, Zhang J et al (2006) Critical role for Daxx in regulating Mdm2. Nat Cell Biol 8:855–862CrossRefPubMedGoogle Scholar
  4. Yang X, Khosravi-Far R, Chang HY et al (1997) Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 89:1067–1076CrossRefPubMedPubMedCentralGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Department of Biomedical Sciences, School of Life SciencesXiamen UniversityXiamenChina