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Gene Review

Daxx  -  Fas death domain-associated protein

Mus musculus

Synonyms: Death domain-associated protein 6
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Disease relevance of Daxx


High impact information on Daxx

  • Other proteins, notably Daxx, also bind Fas and presumably mediate a FADD-independent apoptotic pathway [2].
  • These findings implicate the gene repressor function of Daxx in interferon-induced apoptosis of lymphoid progenitors [3].
  • Gene expression profile analysis of interferon-beta-treated progenitor B cells revealed enhanced Daxx expression, with concomitant Daxx protein increase and nuclear body translocation [3].
  • An essential role for Daxx in the inhibition of B lymphopoiesis by type I interferons [3].
  • On DNA damage, Daxx dissociates from Mdm2, which correlates with Mdm2 self-degradation [4].

Biological context of Daxx

  • CONCLUSIONS: Limitin suppresses B-cell growth through activation of Tyk2, resulting in the up-regulation and nuclear translocation of Daxx [5].
  • Daxx has been shown to play an essential role in type I IFN-mediated suppression of B cell development and apoptosis [6].
  • Sumoylation of Daxx regulates IFN-induced growth suppression of B lymphocytes and the hormone receptor-mediated transactivation [6].
  • Notably, a Daxx-small ubiquitin-related modifier fusion protein exhibited increased nuclear localization and ability to suppress cell growth in Ba/F3 cells [6].
  • Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX [7].

Anatomical context of Daxx

  • Limitin also induces the expression and nuclear translocation of Daxx, which is essential for IFN-alpha-induced inhibition of B-lymphocyte development [5].
  • Murine pro-B cell line Ba/F3 expressing Daxx KA revealed a resistance to the IFN-induced growth suppression [6].
  • We have generated transgenic mice expressing a dominant-negative form of Daxx (Daxx-DN) in the T-cell lineage [8].
  • We found that Daxx represses the expression of several antiapoptotic genes regulated by nuclear factor-kappaB, including cIAP2, in human tumor cell lines [9].

Associations of Daxx with chemical compounds

  • It is noteworthy that treatment with an exportin inhibitor, leptomycin B, resulted in nuclear localization of Daxx KA and recovery of the IFN-induced growth suppression in Ba/F3 cells [6].

Physical interactions of Daxx


Co-localisations of Daxx

  • Daxx partially co-localizes with Skip in vivo and changes the cellular distribution of Skip [10].

Regulatory relationships of Daxx


Other interactions of Daxx

  • The absence of Tyk2 abrogates this induction of Daxx expression and nuclear translocation [5].
  • Moreover, FasL up-regulation is reduced in the presence of transgenic dominant-negative Daxx [12].
  • In mutant SOD1(G93A) and SOD1(G85R), but not in control motoneurons, this up-regulation results in activation of Fas, leading through Daxx to phosphorylation of p38 and further NO synthesis [12].
  • Here, we show that the transcription repressor Daxx and the SWI/SNF protein ATRX are both associated with two intranuclear domains: ND10/PML bodies and heterochromatin [7].
  • These results imply that our novel suicide switch system may provide a powerful tool to delineate or identify the signaling molecules for Daxx-mediated apoptotic machinery in B lymphocyte progenitors through JNK activation [11].

Analytical, diagnostic and therapeutic context of Daxx


  1. Genetic characterization of new Dobrava hantavirus isolate from Greece. Nemirov, K., Vapalahti, O., Papa, A., Plyusnina, A., Lundkvist, A., Antoniadis, A., Vaheri, A., Plyusnin, A. J. Med. Virol. (2003) [Pubmed]
  2. Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Zhang, J., Cado, D., Chen, A., Kabra, N.H., Winoto, A. Nature (1998) [Pubmed]
  3. An essential role for Daxx in the inhibition of B lymphopoiesis by type I interferons. Gongora, R., Stephan, R.P., Zhang, Z., Cooper, M.D. Immunity (2001) [Pubmed]
  4. Critical role for Daxx in regulating Mdm2. Tang, J., Qu, L.K., Zhang, J., Wang, W., Michaelson, J.S., Degenhardt, Y.Y., El-Deiry, W.S., Yang, X. Nat. Cell Biol. (2006) [Pubmed]
  5. Limitin, an interferon-like cytokine, transduces inhibitory signals on B-cell growth through activation of Tyk2, but not Stat1, followed by induction and nuclear translocation of Daxx. Aoki, K., Shimoda, K., Oritani, K., Matsuda, T., Kamezaki, K., Muromoto, R., Numata, A., Tamiya, S., Haro, T., Ishikawa, F., Takase, K., Yamamoto, T., Yumioka, T., Miyamoto, T., Nagafuji, K., Gondo, H., Nagafuchi, S., Nakayama, K., Harada, M. Exp. Hematol. (2003) [Pubmed]
  6. Sumoylation of Daxx regulates IFN-induced growth suppression of B lymphocytes and the hormone receptor-mediated transactivation. Muromoto, R., Ishida, M., Sugiyama, K., Sekine, Y., Oritani, K., Shimoda, K., Matsuda, T. J. Immunol. (2006) [Pubmed]
  7. Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX. Ishov, A.M., Vladimirova, O.V., Maul, G.G. J. Cell. Sci. (2004) [Pubmed]
  8. Requirement for Daxx in mature T-cell proliferation and activation. Leal-Sanchez, J., Couzinet, A., Rossin, A., Abdel-Sater, F., Chakrabandhu, K., Luci, C., Anjuere, F., Stebe, E., Hancock, D., Hueber, A.O. Cell Death Differ. (2007) [Pubmed]
  9. Daxx Represses Expression of a Subset of Antiapoptotic Genes Regulated by Nuclear Factor-{kappa}B. Croxton, R., Puto, L.A., de Belle, I., Thomas, M., Torii, S., Hanaii, F., Cuddy, M., Reed, J.C. Cancer Res. (2006) [Pubmed]
  10. The death domain-associated protein modulates activity of the transcription co-factor Skip/NcoA62. Tang, J., Chang, H.Y., Yang, X. FEBS Lett. (2005) [Pubmed]
  11. Daxx enhances Fas-mediated apoptosis in a murine pro-B cell line, BAF3. Muromoto, R., Yamamoto, T., Yumioka, T., Sekine, Y., Sugiyama, K., Shimoda, K., Oritani, K., Matsuda, T. FEBS Lett. (2003) [Pubmed]
  12. Chronic activation in presymptomatic amyotrophic lateral sclerosis (ALS) mice of a feedback loop involving Fas, Daxx, and FasL. Raoul, C., Buhler, E., Sadeghi, C., Jacquier, A., Aebischer, P., Pettmann, B., Henderson, C.E., Haase, G. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  13. Mouse cytomegalovirus immediate-early protein 1 binds with host cell repressors to relieve suppressive effects on viral transcription and replication during lytic infection. Tang, Q., Maul, G.G. J. Virol. (2003) [Pubmed]
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