Common Properties of Nuclear Body Protein SP100 and TIF1α Chromatin Factor: Role of SUMO Modification

REFERENCES

• Aasland, R., T. Gibson, and A. Stewart. 1995. The PHD finger: implications for chromatin-mediated transcriptional regulation. Trends Biochem. Sci 20:56–59.
   PubMed Web of Science ®Google Scholar
• Ascoli, C. A., and G. G. Maul. 1991. Identification of a novel nuclear domain. J. Cell Biol. 112:785–795.
   PubMed Web of Science ®Google Scholar
• Bhaskar, V., S. A. Valentine, and A. J. Courey. 2000. A functional interaction between dorsal and components of the smt3 conjugation machinery. J. Biol. Chem. 275:4033–4040.
   PubMedGoogle Scholar
• Bloch, D. B., S. M. de la Monte, P. Guigaouri, A. Filippov, and K. D. Bloch. 1996. Identification and characterization of a leukocyte-specific component of the nuclear body. J. Biol. Chem. 271:29198–29204.
   PubMedGoogle Scholar
• Bloch, D. B., A. Nakajima, T. Gulick, J. D. Chiche, D. Orth, S. M. de La Monte, and K. D. Bloch. 2000. Sp110 localizes to the PML-Sp100 nuclear body and may function as a nuclear hormone receptor transcriptional coactivator. Mol. Cell. Biol. 20:6138–6146.
   PubMed Web of Science ®Google Scholar
• Boisvert, F., M. Hendzel, and D. Bazett-Jones. 2000. Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J. Cell Biol. 148:283–292.
   PubMed Web of Science ®Google Scholar
• Carvalho, T., J. S. Seeler, K. Ohman, P. Jordan, U. Pettersson, G. Akusjarvi, M. Carmo-Fonseca, and A. Dejean. 1995. Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies. J. Cell Biol. 131:45–56.
   PubMed Web of Science ®Google Scholar
• Chen, G. Q., J. Zhu, X. G. Shi, J. H. Ni, H. J. Zhong, G. Y. Si, X. L. Jin, W. Tang, X. S. Li, S. M. Xong, Z. X. Shen, G. L. Sun, J. Ma, P. Zhang, T. D. Zhang, C. Gazin, T. Naoe, S. J. Chen, Z. Y. Wang, and Z. Chen. 1996. In vitro studies on cellular and molecular mechanisms of arsenic trioxide (As2O3) in the treatment of acute promyelocytic leukemia: As2O3 induces NB4 cell apoptosis with downregulation of Bcl-2 expression and modulation of PML-RAR alpha/PML proteins. Blood 88:1052–1061.
   PubMed Web of Science ®Google Scholar
• Dent, A. L., J. Yewdell, F. Puvion-Dutilleul, M. H. Koken, H. de The, and L. M. Staudt. 1996. LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies. Blood 88:1423–1426.
   PubMed Web of Science ®Google Scholar
• Desterro, J. M., M. S. Rodriguez, and R. T. Hay. 1998. SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol. Cell 2:233–239.
   PubMed Web of Science ®Google Scholar
• de The, H., C. Lavau, A. Marchio, C. Chomienne, L. Degos, and A. Dejean. 1991. The PML-RAR-α fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66:675–684.
   PubMed Web of Science ®Google Scholar
• Everett, R. D., W. C. Earnshaw, A. F. Pluta, T. Sternsdorf, A. M. Ainsztein, M. Carmena, S. Ruchaud, W. L. Hsu, and A. Orr. 1999. A dynamic connection between centromeres and ND10 proteins. J. Cell Sci. 112:3443–3454.
   PubMedGoogle Scholar
• Fraser, R. A., D. J. Heard, S. Adam, A. C. Lavigne, B. Le Douarin, L. Tora, R. Losson, C. Rochette-Egly, and P. Chambon. 1998. The putative cofactor TIF1alpha is a protein kinase that is hyperphosphorylated upon interaction with liganded nuclear receptors. J. Biol. Chem. 273:16199–16204.
   PubMedGoogle Scholar
• Friedman, J. R., W. J. Fredericks, D. E. Jensen, D. W. Speicher, X. P. Huang, E. G. Neilson, and F. J. Rauscher. 1996. KAP-1, a novel corepressor for the highly conserved KRAB repression domain. Genes Dev. 10:2067–2078.
   PubMed Web of Science ®Google Scholar
• Gibson, T., C. Ramu, C. Gemünd, and R. Aasland. 1998. The APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor. Trends Biochem. Sci. 23:242–244.
   PubMed Web of Science ®Google Scholar
• Gostissa, M., A. Hengstermann, V. Fogal, P. Sandy, S. E. Schwarz, M. Scheffner, and G. Del Sal. 1999. Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1. EMBO J. 18:6462–6471.
   PubMed Web of Science ®Google Scholar
• Guldner, H. H., C. Szostecki, T. Grotzinger, and H. Will. 1992. IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis. J. Immunol. 149:4067–4073.
   PubMed Web of Science ®Google Scholar
• Guldner, H. H., C. Szostecki, P. Schroder, U. Matschl, K. Jensen, C. Luders, H. Will, and T. Sternsdorf. 1999. Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif. J. Cell Sci. 112:733–747.
   PubMedGoogle Scholar
• Hollenbach, A. D., J. E. Sublett, C. J. McPherson, and G. Grosveld. 1999. The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx. EMBO J. 18:3702–3711.
   PubMedGoogle Scholar
• Ishov, A. M., A. G. Sotnikov, D. Negorev, O. V. Vladimirova, N. Neff, T. Kamitani, E. T. Yeh, J. F. Strauss, 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.
   PubMed Web of Science ®Google Scholar
• Jeanmougin, F., J. M. Wurtz, B. Le Douarin, P. Chambon, and R. Losson. 1997. The bromodomain revisited. Trends Biochem. Sci. 22:151–153.
   PubMed Web of Science ®Google Scholar
• Johnson, P. R., and M. Hochstrasser. 1997. SUMO-1: ubiquitin gains weight. Trends Cell Biol. 7:408–413.
   PubMedGoogle Scholar
• Kim, S. S., Y. M. Chen, E. O'Leary, R. Witzgall, M. Vidal, and J. V. Bonventre. 1996. A novel member of the RING finger family, KRIP-1, associates with the KRAB-A transcriptional repressor domain of zinc finger proteins. Proc. Natl. Acad. Sci. USA 93:15299–15304.
   PubMed Web of Science ®Google Scholar
• Kim, Y. H., C. Y. Choi, and Y. Kim. 1999. Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1. Proc. Natl. Acad. Sci. USA 96:12350–12355.
   PubMedGoogle Scholar
• Klugbauer, S., and H. Rabes. 1999. The transcription coactivator HTIF1 and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas. Oncogene 18:4388–4393.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Lavau, C., A. Marchio, M. Fagioli, J. Jansen, B. Falini, P. Lebon, F. Grosveld, P. P. Pandolfi, P. G. Pelicci, and A. Dejean. 1995. The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene 11:871–876.
   PubMed Web of Science ®Google Scholar
• LeDouarin, B., A. L. Nielsen, J. M. Garnier, H. Ichinose, F. Jeanmougin, R. Losson, and P. Chambon. 1996. A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors. EMBO J. 15:6701–6715.
   PubMedGoogle Scholar
• LeDouarin, B., C. Zechel, J. M. Garnier, Y. Lutz, L. Tora, P. Pierrat, D. Heery, H. Gronemeyer, P. Chambon, and R. Losson. 1995. The N-terminal part of TIF1, a putative mediator of the ligand- dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. EMBO J. 14:2020–2033.
   PubMedGoogle Scholar
• Lehembre, F., P. Badenhorst, S. Muller, A. Travers, F. Schweisguth, and A. Dejean. 2000. Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies. Mol. Cell. Biol. 20:1072–1082.
   PubMedGoogle Scholar
• Lehming, N., S. A. Le, J. Schüller, and M. Ptashne. 1998. Chromatin components as part of a putative transcriptional repressing complex. Proc. Natl. Acad. Sci. USA 95:7322–7326.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Lin, R., D. Egan, and R. Evans. 1999. Molecular genetics of acute promyelocytic leukemia. Trends Genet. 15:179–184.
   PubMed Web of Science ®Google Scholar
• Mahajan, R., C. Delphin, T. Guan, L. Gerace, and F. Melchior. 1997. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88:97–107.
   PubMed Web of Science ®Google Scholar
• Matunis, M. J., J. Wu, and G. Blobel. 1998. SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex. J. Cell Biol. 140:499–509.
   PubMed Web of Science ®Google Scholar
• Maul, G. G.. 1998. Nuclear domain 10, the site of DNA virus transcription and replication. Bioessays 20:660–667.
   PubMed Web of Science ®Google Scholar
• Miki, T., T. P. Fleming, M. Crescenzi, C. J. Molloy, S. B. Blam, S. H. Reynolds, and S. A. Aaronson. 1991. Development of a highly efficient expression cDNA cloning system: application to oncogene isolation. Proc. Natl. Acad. Sci. USA 88:5167–5171.
   PubMed Web of Science ®Google Scholar
• Moosmann, P., O. Georgiev, B. Le Douarin, J. P. Bourquin, and W. Schaffner. 1996. Transcriptional repression by RING finger protein TIF1 beta that interacts with the KRAB repressor domain of KOX1. Nucleic Acids Res. 24:4859–4867.
   PubMed Web of Science ®Google Scholar
• Müller, S., M. Berger, F. Lehembre, J. Seeler, Y. Haupt, and A. Dejean. 2000. SUMO-1 modification of c-jun and p53 is co-regulated with ubiquitination in a phosphorylation-dependent manner. J. Biol. Chem. 275:13321–13329.
   PubMed Web of Science ®Google Scholar
• Müller, S., M. J. Matunis, and A. Dejean. 1998. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17:61–70.
   PubMed Web of Science ®Google Scholar
• Negorev, D., A. M. Ishov, and G. G. Maul. 2001. Evidence for separate ND10-binding and homo-oligomerization domains of Sp100. J. Cell Sci. 114:59–68.
   PubMedGoogle Scholar
• Nielsen, A., J. A. Ortiz, J. You, M. Oulad-Abdelghani, R. Khechumian, A. Gansmuller, P. Chambon, and R. Losson. 1999. Interaction with the members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in the transcriptional silencing by members of the TIF1 family. EMBO J. 18:6385–6395.
   PubMed Web of Science ®Google Scholar
• Pearson, M., R. Carbone, C. Sebastiani, M. Cioce, M. Fagioli, S. Saito, Y. Higashimoto, E. Appella, S. Minucci, P. P. Pandolfi, and P. G. Pelicci. 2000. PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406:207–210.
   PubMed Web of Science ®Google Scholar
• Pluta, A. F., W. C. Earnshaw, and I. G. Goldberg. 1998. Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death. J. Cell Sci. 111:2029–2041.
   PubMed Web of Science ®Google Scholar
• Rodriguez, M. S., J. M. Desterro, S. Lain, C. A. Midgley, D. P. Lane, and R. T. Hay. 1999. SUMO-1 modification activates the transcriptional response of p53. EMBO J. 18:6455–6461.
   PubMed Web of Science ®Google Scholar
• Ryan, R. F., D. C. Schultz, K. Ayyanathan, P. B. Singh, J. R. Friedman, W. J. Fredericks, and F. J. Rauscher. 1999. KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HP1 proteins: a potential role for Kruppel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing. Mol. Cell. Biol. 19:4366–4378.
   PubMed Web of Science ®Google Scholar
• Seeler, J.-S., and A. Dejean. 1999. The PML nuclear bodies: actors or extras?. Curr. Opin. Genet. Dev. 9:362–367.
   PubMedGoogle Scholar
• Seeler, J.-S., A. Marchio, D. Sitterlin, C. Transy, and A. Dejean. 1998. Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc. Natl. Acad. Sci. USA 95:7316–7321.
   PubMed Web of Science ®Google Scholar
• Stadler, M., M. K. Chelbi-Alix, M. H. Koken, L. Venturini, C. Lee, A. Saib, F. Quignon, L. Pelicano, M. C. Guillemin, C. Schindler, and H. de The. 1995. Transcriptional induction of the PML growth suppressor gene by interferons is mediated through an ISRE and a GAS element. Oncogene 11:2565–2573.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Sternsdorf, T., K. Jensen, and H. Will. 1997. Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 139:1621–1634.
   PubMedGoogle Scholar
• Szostecki, C., H. H. Guldner, H. J. Netter, and H. Will. 1990. Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis. J. Immunol. 145:4338–4347.
   PubMed Web of Science ®Google Scholar
• Tanaka, K., J. Nishide, K. Okazaki, H. Kato, O. Niwa, T. Nakagawa, H. Matsuda, M. Kawamukai, and Y. Murakami. 1999. Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation. Mol. Cell. Biol. 19:8660–8672.
   PubMed Web of Science ®Google Scholar
• Thenot, S., C. Henriquet, H. Rochefort, and V. Cavailles. 1997. Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1. J. Biol. Chem. 272:12062–12068.
   PubMed Web of Science ®Google Scholar
• Torii, S., D. A. Egan, R. A. Evans, and J. C. Reed. 1999. Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs). EMBO J. 18:6037–6049.
   PubMedGoogle Scholar
• Venturini, L., J. You, M. Stadler, R. Galien, V. Lallemand, M. H. Koken, M. G. Mattei, A. Ganser, P. Chambon, R. Losson, and H. de Thé. 1999. TIF1gamma, a novel member of the transcriptional intermediary factor 1 family. Oncogene 18:1209–1217.
   PubMed Web of Science ®Google Scholar
• Winston, F., and C. Allis. 1999. The bromodomain: a chromatin-targeting module?. Nat. Struct. Biol. 6:601–604.
   PubMedGoogle Scholar
• Xie, K., E. J. Lambie, and M. Snyder. 1993. Nuclear dot antigens may specify transcriptional domains in the nucleus. Mol. Cell. Biol. 13:6170–6179.
   PubMed Web of Science ®Google Scholar
• Zhong, S., L. Delva, C. Rachez, C. Cenciarelli, D. Gandini, H. Zhang, S. Kalantry, L. P. Freedman, and P. P. Pandolfi. 1999. A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins. Nat. Genet. 23:287–295.
   PubMed Web of Science ®Google Scholar
• Zhong, S., S. Müller, S. Ronchetti, P. Freemont, A. Dejean, and P. Pandolfi. 2000. A role of SUMO-1-modified PML in nuclear body formation. Blood 95:2748–2753.
   PubMed Web of Science ®Google Scholar
• Zhu, J., M. H. Koken, F. Quignon, M. K. Chelbi-Alix, L. Degos, Z. Y. Wang, Z. Chen, and H. de Thé. 1997. Arsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemia. Proc. Natl. Acad. Sci. USA 94:3978–3983.
   PubMed Web of Science ®Google Scholar