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Article

Transcriptional Regulation Is Affected by Subnuclear Targeting of Reporter Plasmids to PML Nuclear Bodies

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Pages 8814-8825 | Received 12 Apr 2006, Accepted 30 Aug 2006, Published online: 27 Mar 2023

REFERENCES

  • Bailey, D., and P. O'Hare. 2002. Herpes simplex virus 1 ICP0 co-localizes with a SUMO-specific protease. J. Gen. Virol. 83:2951–2964.
  • Beech, S. J., K. J. Lethbridge, N. Killick, N. McGlincy, and K. N. Leppard. 2005. Isoforms of the promyelocytic leukemia protein differ in their effects on ND10 organization. Exp. Cell Res. 307:109–117.
  • Bischof, O., O. Kirsh, M. Pearson, K. Itahana, P. G. Pelicci, and A. Dejean. 2002. Deconstructing PML-induced premature senescence. EMBO J. 21:3358–3369.
  • Boisvert, F. M., M. J. Hendzel, and D. P. Bazett-Jones. 2000. Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J. Cell Biol. 148:283–292.
  • Boisvert, F. M., M. J. Kruhlak, A. K. Box, M. J. Hendzel, and D. P. Bazett-Jones. 2001. The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J. Cell Biol. 152:1099–1106.
  • Ching, R. W., G. Dellaire, C. H. Eskiw, and D. P. Bazett-Jones. 2005. PML bodies: a meeting place for genomic loci? J. Cell Sci. 118:847–854.
  • Condemine, W., Y. Takahashi, J. Zhu, F. Puvion-Dutilleul, S. Guegan, A. Janin, and H. de The. 2006. Characterization of endogenous human promyelocytic leukemia isoforms. Cancer Res. 66:6192–6198.
  • Dehghani, H., G. Dellaire, and D. P. Bazett-Jones. 2005. Organization of chromatin in the interphase mammalian cell. Micron 36:95–108.
  • Dellaire, G., and D. P. Bazett-Jones. 2004. PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 26:963–977.
  • Dellaire, G., R. Farrall, and W. A. Bickmore. 2003. The Nuclear Protein Database (NPD): sub-nuclear localisation and functional annotation of the nuclear proteome. Nucleic Acids Res. 31:328–330.
  • Dellaire, G., R. Nisman, C. H. Eskiw, and D. P. Bazett-Jones. 2004. In situ imaging and isolation of proteins using dsDNA oligonucleotides. Nucleic Acids Res. 32:e165.
  • de The, H., C. Lavau, A. Marchio, C. Chomienne, L. Degos, and A. Dejean. 1991. The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66:675–684.
  • Dyck, J. A., G. G. Maul, W. H. Miller, Jr., J. D. Chen, A. Kakizuka, and R. M. Evans. 1994. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76:333–343.
  • Eskiw, C. H., G. Dellaire, and D. P. Bazett-Jones. 2004. Chromatin contributes to structural integrity of promyelocytic leukemia bodies through a SUMO-1-independent mechanism. J. Biol. Chem. 279:9577–9585.
  • Eskiw, C. H., G. Dellaire, J. S. Mymryk, and D. P. Bazett-Jones. 2003. Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly. J. Cell Sci. 116:4455–4466.
  • Hagglund, R., and B. Roizman. 2004. Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1. J. Virol. 78:2169–2178.
  • Hiller, Y., E. A. Bayer, and M. Wilchek. 1991. Studies on the biotin-binding site of avidin. Minimized fragments that bind biotin. Biochem J. 278:573–585.
  • Hofmann, T. G., A. Moller, H. Sirma, H. Zentgraf, Y. Taya, W. Droge, H. Will, and M. L. Schmitz. 2002. Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. Nat. Cell Biol. 4:1–10.
  • Ishov, A. M., A. G. Sotnikov, D. Negorev, O. V. Vladimirova, N. Neff, T. Kamitani, E. T. Yeh, J. F. Strauss III, and G. G. Maul. 1999. PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147:221–234.
  • Jensen, K., C. Shiels, and P. S. Freemont. 2001. PML protein isoforms and the RBCC/TRIM motif. Oncogene 20:7223–7233.
  • Kastner, P., A. Perez, Y. Lutz, C. Rochette-Egly, M. P. Gaub, and P. Chambon. 1991. [Fusion proteins between PML and alpha-RAR in acute promyelocytic leukemia]. C. R. Seances Soc. Biol. Fil. 185:391–401. (In French.)
  • LaMorte, V. J., J. A. Dyck, R. L. Ochs, and R. M. Evans. 1998. Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc. Natl. Acad. Sci. USA 95:4991–4996.
  • Li, H., C. Leo, J. Zhu, X. Wu, J. O'Neil, E. J. Park, and J. D. Chen. 2000. Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol. Cell. Biol. 20:1784–1796.
  • Lin, D. Y., M. Z. Lai, D. K. Ann, and H. M. Shih. 2003. 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. 278:15958–15965.
  • Lopez, P., R. J. Jacob, and B. Roizman. 2002. Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effect on accumulation of infectious herpes simplex virus 1 or its proteins. J. Virol. 76:9355–9367.
  • Melnick, A., and J. D. Licht. 1999. Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia. Blood 93:3167–3215.
  • Moller, A., H. Sirma, T. G. Hofmann, S. Rueffer, E. Klimczak, W. Droge, H. Will, and M. L. Schmitz. 2003. PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains. Cancer Res. 63:4310–4314.
  • Muller, S., and A. Dejean. 1999. Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J. Virol. 73:5137–5143.
  • Nefkens, I., D. G. Negorev, A. M. Ishov, J. S. Michaelson, E. T. Yeh, R. M.Tanguay, W. E. Muller, and G. G. Maul. 2003. Heat shock and Cd2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 and 25 differently. J. Cell Sci. 116:513–524.
  • Rotem-Yehudar, R., M. Groettrup, A. Soza, P. M. Kloetzel, and R. Ehrlich. 1996. LMP-associated proteolytic activities and TAP-dependent peptide transport for class 1 MHC molecules are suppressed in cell lines transformed by the highly oncogenic adenovirus 12. J. Exp. Med. 183:499–514.
  • Sapetschnig, A., G. Rischitor, H. Braun, A. Doll, M. Schergaut, F. Melchior, and G. Suske. 2002. Transcription factor Sp3 is silenced through SUMO modification by PIAS1. EMBO J. 21:5206–5215.
  • Shiels, C., S. A. Islam, R. Vatcheva, P. Sasieni, M. J. Sternberg, P. S. Freemont, and D. Sheer. 2001. PML bodies associate specifically with the MHC gene cluster in interphase nuclei. J. Cell Sci. 114:3705–3716.
  • Spengler, M. L., and M. G. Brattain. 2006. Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory domain and inhibits Sp1-dependent transcription. J. Biol. Chem. 281:5567–5574.
  • Sternsdorf, T., K. Jensen, B. Reich, and H. Will. 1999. The nuclear dot protein Sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J. Biol. Chem. 274:12555–12566.
  • Vallian, S., K. V. Chin, and K. S. Chang. 1998. The promyelocytic leukemia protein interacts with Sp1 and inhibits its transactivation of the epidermal growth factor receptor promoter. Mol. Cell. Biol. 18:7147–7156.
  • Vallian, S., J. A. Gaken, E. B. Gingold, T. Kouzarides, K. S. Chang, and F. Farzaneh. 1998. Modulation of Fos-mediated AP-1 transcription by the promyelocytic leukemia protein. Oncogene 16:2843–2853.
  • Vallian, S., J. A. Gaken, I. D. Trayner, E. B. Gingold, T. Kouzarides, K. S. Chang, and F. Farzaneh. 1997. Transcriptional repression by the promyelocytic leukemia protein, PML. Exp. Cell Res. 237:371–382.
  • Wu, W. S., S. Vallian, E. Seto, W. M. Yang, D. Edmondson, S. Roth, and K. S. Chang. 2001. The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol. Cell. Biol. 21:2259–2268.
  • Zheng, P., Y. Guo, Q. Niu, D. E. Levy, J. A. Dyck, S. Lu, L. A. Sheiman, and Y. Liu. 1998. Proto-oncogene PML controls genes devoted to MHC class I antigen presentation. Nature 396:373–376.
  • Zhong, S., P. Salomoni, and P. P. Pandolfi. 2000. The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2:E85–E90.

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