• 1
    Salomoni, P. and Khelifi, A. F., Daxx: death or survival protein? Trends Cell Biol. 2006. 16: 97104.
  • 2
    Michaelson, J. S., The Daxx enigma. Apoptosis 2000. 5: 217220.
  • 3
    Gongora, R., Stephan, R. P., Zhang, Z. and Cooper, M. D., An essential role for Daxx in the inhibition of B lymphopoiesis by type I interferons. Immunity 2001. 14: 727737.
  • 4
    Zhong, S., Salomoni, P., Ronchetti, S., Guo, A., Ruggero, D. and Pandolfi, P. P., Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. J. Exp. Med. 2000. 191: 631640.
  • 5
    Salomoni, P., Guernah, I. and Pandolfi, P. P., The PML-nuclear body associated protein Daxx regulates the cellular response to CD40. Cell Death Differ. 2006. 13: 672675.
  • 6
    Leal-Sanchez, J., Couzinet, A., Rossin, A., Abdel-Sater, F., Chakrabandhu, K., Luci, C., Anjuere, F. et al., Requirement for Daxx in mature T-cell proliferation and activation. Cell Death Differ. 2007. 14: 795806.
  • 7
    Li, R., Pei, H., Watson, D. K. and Papas, T. S., EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes. Oncogene 2000. 19: 745753.
  • 8
    Emelyanov, A. V., Kovac, C. R., Sepulveda, M. A. and Birshtein, B. K., The interaction of Pax5 (BSAP) with Daxx can result in transcriptional activation in B cells. J. Biol. Chem. 2002. 277: 1115611164.
  • 9
    Lin, D. Y., Lai, M. Z., Ann, D. K. and Shih, H. M., Promyelocytic leukemia protein (PML) functions as a glucocorticoid receptor co-activator by sequestering Daxx to the PML oncogenic domains (PODs) to enhance its transactivation potential. J. Biol. Chem. 2003. 278: 1595815965.
  • 10
    Park, J., Lee, J. H., La, M., Jang, M. J., Chae, G. W., Kim, S. B., Tak, H. et al., Inhibition of NF-kappaB acetylation and its transcriptional activity by Daxx. J. Mol. Biol. 2007. 368: 388397.
  • 11
    Croxton, R., Puto, L. A., de Belle, I., Thomas, M., Torii, S., Hanaii, F., Cuddy, M. et al., Daxx represses expression of a subset of antiapoptotic genes regulated by nuclear factor-kappaB. Cancer Res. 2006. 66: 90269035.
  • 12
    Tzeng, S. L., Cheng, Y. W., Li, C. H., Lin, Y. S., Hsu, H. C. and Kang, J. J., Physiological and functional interactions between Tcf4 and Daxx in colon cancer cells. J. Biol. Chem. 2006. 281: 1540515411.
  • 13
    Chang, C. C., Lin, D. Y., Fang, H. I., Chen, R. H. and Shih, H. M., Daxx mediates the small ubiquitin-like modifier-dependent transcriptional repression of Smad4. J. Biol. Chem. 2005. 280: 1016410173.
  • 14
    Wethkamp, N. and Klempnauer, K. H., Daxx is a transcriptional repressor of CCAAT/enhancer-binding protein beta. J. Biol. Chem. 2009. 284: 2878328794.
  • 15
    Meloni, A., Fiorillo, E., Corda, D., Incani, F., Serra, M. L., Contini, A., Cao, A. et al., DAXX is a new AIRE-interacting protein. J. Biol. Chem. 2010. 285: 1301213021.
  • 16
    Muromoto, R., Nakao, K., Watanabe, T., Sato, N., Sekine, Y., Sugiyama, K., Oritani, K. et al., Physical and functional interactions between Daxx and STAT3. Oncogene 2006. 25: 21312136.
  • 17
    Hollenbach, A. D., McPherson, C. J., Mientjes, E. J., Iyengar, R. and Grosveld, G., Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. J. Cell Sci. 2002. 115: 33193330.
  • 18
    Michaelson, J. S., Bader, D., Kuo, F., Kozak, C. and Leder, P., Loss of Daxx, a promiscuously interacting protein, results in extensive apoptosis in early mouse development. Genes Dev. 1999. 13: 19181923.
  • 19
    Puto, L. A. and Reed, J. C., Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation. Genes Dev. 2008. 22: 9981010.
  • 20
    Muromoto, R., Sugiyama, K., Takachi, A., Imoto, S., Sato, N., Yamamoto, T., Oritani, K. et al., Physical and functional interactions between Daxx and DNA methyltransferase 1-associated protein, DMAP1. J. Immunol. 2004. 172: 29852993.
  • 21
    Xue, Y., Gibbons, R., Yan, Z., Yang, D., McDowell, T. L., Sechi, S., Qin, J. et al., The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies. Proc. Natl. Acad. Sci. USA 2003. 100: 1063510640.
  • 22
    Tang, J., Wu, S., Liu, H., Stratt, R., Barak, O. G., Shiekhattar, R., Picketts, D. J. et al., A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein. J. Biol. Chem. 2004. 279: 2036920377.
  • 23
    Hirano, T., Nakajima, K. and Hibi, M., Signaling mechanisms through gp130: a model of the cytokine system. Cytokine Growth Factor Rev. 1997. 8: 241252.
  • 24
    Darnell, J. E., Jr., STATs and gene regulation. Science 1997. 277: 16301635.
  • 25
    Taga, T. and Kishimoto, T., Gp130 and the interleukin-6 family of cytokines. Annu. Rev. Immunol. 1997. 15: 797819.
  • 26
    Hankey, P. A., Regulation of hematopoietic cell development and function by Stat3. Front. Biosci. 2009. 14: 52735290.
  • 27
    Yu, H., Pardoll, D. and Jove, R., STATs in cancer inflammation and immunity: a leading role for STAT3. Nat. Rev. Cancer 2009. 9: 798809.
  • 28
    Minegishi, Y., Hyper-IgE syndrome. Curr. Opin. Immunol. 2009. 21: 487492.
  • 29
    Takeda, K., Kaisho, T., Yoshida, N., Takeda, J., Kishimoto, T. and Akira, S., Stat3 activation is responsible for IL-6-dependent T cell proliferation through preventing apoptosis: generation and characterization of T cell-specific Stat3-deficient mice. J. Immunol 1998. 161: 46524660.
  • 30
    Owaki, T., Asakawa, M., Morishima, N., Mizoguchi, I., Fukai, F., Takeda, K., Mizuguchi, J. et al., STAT3 is indispensable to IL-27-mediated cell proliferation but not to IL-27-induced Th1 differentiation and suppression of proinflammatory cytokine production. J. Immunol. 2008. 180: 29032911.
  • 31
    Chou, W. C., Levy, D. E. and Lee, C. K., STAT3 positively regulates an early step in B-cell development. Blood 2006. 108: 30053011.
  • 32
    Fukada, T., Hibi, M., Yamanaka, Y., Takahashi-Tezuka, M., Fujitani, Y., Yamaguchi, T., Nakajima, K. et al., Two signals are necessary for cell proliferation induced by a cytokine receptor gp130: involvement of STAT3 in anti-apoptosis. Immunity 1996. 5: 449460.
  • 33
    Fukada, T., Ohtani, T., Yoshida, Y., Shirogane, T., Nishida, K., Nakajima, K., Hibi, M. et al., STAT3 orchestrates contradictory signals in cytokine-induced G1 to S cell-cycle transition. EMBO J. 1998. 17: 66706677.
  • 34
    Xiang, H., Wang, J. and Boxer, L. M., Role of the cyclic AMP response element in the bcl-2 promoter in the regulation of endogenous Bcl-2 expression and apoptosis in murine B cells. Mol. Cell Biol. 2006. 26: 85998606.
  • 35
    Kuo, H. Y., Chang, C. C., Jeng, J. C., Hu, H. M., Lin, D. Y., Maul, G. G., Kwok, R. P. et al., SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx. Proc. Natl. Acad. Sci. USA 2005. 102: 1697316978.
  • 36
    Wang, J. L., Liu, D., Zhang, Z. J., Shan, S., Han, X., Srinivasula, S. M., Croce, C. M. et al., Structure-based discovery of an organic compound that binds Bcl-2 protein and induces apoptosis of tumor cells. Proc. Natl. Acad. Sci. USA 2000. 97: 71247129.
  • 37
    Hofmann, W. K., de Vos, S., Tsukasaki, K., Wachsman, W., Pinkus, G. S., Said, J. W. and Koeffler, H. P., Altered apoptosis pathways in mantle cell lymphoma detected by oligonucleotide microarray. Blood 2001. 98: 787794.
  • 38
    Boehrer, S., Nowak, D., Kukoc-Zivojnov, N., Hochmuth, S., Kim, S. Z., Hoelzer, D., Mitrou, P. S. et al., Expression of Daxx sensitizes Jurkat T-cells to the apoptosis-inducing effect of chemotherapeutic agents. Pharmacol. Res. 2005. 51: 367374.
  • 39
    Mui, A. L., Wakao, H., Kinoshita, T., Kitamura, T. and Miyajima, A., Suppression of interleukin-3-induced gene expression by a C-terminal truncated Stat5: role of Stat5 in proliferation. EMBO J. 1996. 15: 24252433.
  • 40
    Dumon, S., Santos, S. C., Debierre-Grockiego, F., Gouilleux-Gruart, V., Cocault, L., Boucheron, C., Mollat, P. et al., IL-3 dependent regulation of Bcl-xL gene expression by STAT5 in a bone marrow derived cell line. Oncogene 1999. 18: 41914199.
  • 41
    Rosa Santos, S. C., Dumon, S., Mayeux, P., Gisselbrecht, S. and Gouilleux, F., Cooperation between STAT5 and phosphatidylinositol 3-kinase in the IL-3-dependent survival of a bone marrow derived cell line. Oncogene 2000. 19: 11641172.
  • 42
    Ryo, A., Hirai, A., Nishi, M., Liou, Y. C., Perrem, K., Lin, S. C., Hirano, H. et al., A suppressive role of the prolyl isomerase Pin1 in cellular apoptosis mediated by the death-associated protein Daxx. J. Biol. Chem. 2007. 282: 3667136681.
  • 43
    Kwon, J. E., La, M., Oh, K. H., Oh, Y. M., Kim, G. R., Seol, J. H., Baek, S. H. et al., BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase. J. Biol. Chem. 2006. 281: 1266412672.
  • 44
    Tang, J., Qu, L., Pang, M. and Yang, X., Daxx is reciprocally regulated by Mdm2 and Hausp. Biochem. Biophys. Res. Commun. 2010. 393: 542545.
  • 45
    Cashen, A. F., Lazarus, H. M. and Devine, S. M., Mobilizing stem cells from normal donors: is it possible to improve upon G-CSF? Bone Marrow Transplantation 2007. 39: 577588.
  • 46
    Zhang, Y., Cheng, G., Yang, K., Fan, R., Xu, Z., Chen, L., Li, Q. et al., A novel function of granulocyte colony-stimulating factor in mobilization of human hematopoietic progenitor cells. Immunol. Cell Biol. 2009. 87: 428432.
  • 47
    Saffert, R. T., Penkert, R. R. and Kalejta, R. F., Cellular and viral control over the initial events of human cytomegalovirus experimental latency in CD34+cells. J. Virol. 2010. 84: 55945604.
  • 48
    Matsuda, T., Yamamoto, T., Muraguchi, A. and Saatcioglu, F., Cross-talk between transforming growth factor-beta and estrogen receptor signaling through Smad3. J. Biol. Chem. 2001. 276: 4290842914.
  • 49
    Muromoto, R., Ikeda, O., Okabe, K., Togi, S., Kamitani, S., Fujimuro, M., Harada, S. et al., Epstein-Barr virus-derived EBNA2 regulates STAT3 activation. Biochem. Biophys. Res. Commun. 2009. 378: 439443.
  • 50
    Ezoe, S., Matsumura, I., Gale, K., Satoh, Y., Ishikawa, J., Mizuki, M., Takahashi, S. et al., GATA transcription factors inhibit cytokine-dependent growth and survival of a hematopoietic cell line through the inhibition of STAT3 activity. J. Biol. Chem. 2005. 280: 1316313170.