The Promyelocytic Leukemia Protein Interacts with Sp1 and Inhibits Its Transactivation of the Epidermal Growth Factor Receptor Promoter

REFERENCES

• Ahn, J.-H., and G. S. Hayward 1997. The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PML-associated nuclear bodies at very early times in infected permissive cells. J. Virol. 71: 4599–4613.
   PubMed Web of Science ®Google Scholar
• Alcalay, M., L. Tomassoni, E. Colombo, S. Stoldt, F. Grignani, M. Fagioli, L. Szekely, K. Helin, and P. G. Pelicci 1998. The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol. Cell. Biol. 18: 1084–1093.
   PubMedGoogle 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
• Bannister, A. J., and T. Kouzarides 1995. CBP-induced stimulation of c-Fos activity is abrogated by E1A. EMBO J. 14: 4758–4762.
   PubMed Web of Science ®Google Scholar
• Blake, M. C., and J. C. Azizkhan 1989. Transcriptional factor E2F is required for efficient expression of the hamster dihydrofolate reductase gene in vitro and in vivo. Mol. Cell. Biol. 9: 4994–5002.
   PubMed Web of Science ®Google Scholar
• Boddy, M. N., K. Howe, L. D. Etkin, E. Solomon, and P. S. Freemont 1996. PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 13: 971–982.
   PubMed Web of Science ®Google Scholar
• Brown, D., S. Kogan, E. Lagasse, I. Weissman, M. Alcalay, P. G. Pelicci, S. Atwater, and J. M. Bishop 1997. A PMLRARalpha transgene initiates murine acute promyelocytic leukemia. Proc. Natl. Acad. Sci. USA 94: 2551–2556.
   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
• Chang, K. S., Y. H. Fan, M. Andreeff, J. X. Liu, and Z. M. Mu 1995. The PML gene encodes a phosphoprotein associated with the nuclear matrix. Blood 85: 3646–3653.
   PubMed Web of Science ®Google Scholar
• Chang, K. S., S. A. Stass, D.-T. Chu, L. L. Deaven, J. M. Trujillo, and E. J. Freireich 1992. Characterization of a fusion cDNA (RARA/myl) transcribed from the t(15;17) translocation breakpoint in acute promyelocytic leukemia. Mol. Cell. Biol. 12: 800–810.
   PubMed Web of Science ®Google Scholar
• Chen, L. I., T. Nishinaka, K. Kwan, I. Kitabayashi, K. Yokoyama, Y.-H. Fu, S. Grünwald, and R. Chiu 1994. The retinoblastoma gene product RB stimulates Sp1-mediated transcription by liberating Sp1 from a negative regulator. Mol. Cell. Biol. 14: 4380–4389.
   PubMed Web of Science ®Google Scholar
• Datta, P. K., P. Raychaudhuri, and S. Bagchi 1995. Association of p107 with Sp1: genetically separable regions of p107 are involved in regulation of E2F- and Sp1-dependent transcription. Mol. Cell. Biol. 15: 5444–5452.
   PubMedGoogle Scholar
• Ded, S. P., R. M. Munoz, D. R. Brown, M. A. Subler, and D. Sumitra 1994. Wild-type human p53 activates the human epidermal growth factor receptor promoter. Oncogene 9: 1341–1349.
   PubMedGoogle Scholar
• de The, H., C. Lavau, A. Marchio, C. Chomienne, L. Degos, and A. Dejean 1991. The PML-RARalpha 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
• Doucas, V., and R. M. Evans 1996. The PML nuclear component and cancer. Biochim. Biophys. Acta 1288: M25–M29.
   PubMedGoogle Scholar
• Dyck, J. A., G. G. Maul, W. H. Miller, 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.
   PubMed Web of Science ®Google Scholar
• Everett, R. D., and G. G. Maul 1994. HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J. 13: 5062–5069.
   PubMedGoogle Scholar
• Freemont, P. S., I. M. Hanson, and J. Trowsdale 1991. A novel cystein-rich sequence motif. Cell 64: 483–484.
   PubMed Web of Science ®Google Scholar
• Goddard, A. D., J. Borrow, P. S. Freemont, and E. Solomon 1991. Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia. Science 254: 1371–1374.
   PubMed Web of Science ®Google Scholar
• Gongora, D., G. David, L. Pintard, C. Tissot, T. D. Hua, A. Dejean, and N. Mechti 1997. Molecular cloning of a new interferon-induced PML nuclear body-associated protein. J. Biol. Chem. 272: 19457–19463.
   PubMed Web of Science ®Google Scholar
• Gregory, R. C., D. J. Taxman, D. Seshasayee, M. H. Kensinger, J. J. Bieker, and D. M. Wojchowski 1996. Functional interaction of GATA1 with erythroid Kruppel-like factor and Sp1 at defined erythroid promoters. Blood 87: 1793–1801.
   PubMedGoogle Scholar
• Grisolano, J. L., R. L. Wesselschmidt, P. G. Pelicci, and T. J. Ley 1997. Altered myeloid development and acute leukemia in transgenic mice expressing PMLRARa under control of catapsin G regulatory sequences. Blood 89: 376–387.
   PubMed Web of Science ®Google Scholar
• Gualberto, A., Baldwin, A. S.Jr. 1995. p53 and Sp1 interact and cooperate in the tumor necrosis factor-induced transcriptional activation of the HIV-1 long terminal repeat. J. Biol. Chem. 270: 19680–19683.
   PubMedGoogle Scholar
• Guiochon-Mantel, A., F. J. Savouret, F. Quignon, K. Delaber, E. Milgrom, and H. De The 1995. Effect of PML and PML-RAR on the transactivation properties and subcellular distribution of steroid hormone receptors. Mol. Endocrinol. 9: 1791–1803.
   PubMedGoogle Scholar
• He, D., Z.-M. Mu, X. Le, J.-T. Hsieh, R.-C. Pong, L. W. K. Chung, and K.-S. Chang 1997. Adenovirus-mediated expression of PML suppresses growth and tumorigenicity of prostate cancer cells. Cancer Res. 57: 1868–1872.
   PubMed Web of Science ®Google Scholar
• He, L. Z., C. Tribioli, R. Rivi, D. Peruzzi, P. G. Pelicci, V. Soares, G. Cattoretti, and P. P. Pandolphi 1997. Acute leukemia with promyelocytic features in PMLRARalpha transgenic mice. Proc. Natl. Acad. Sci. USA 94: 5302–5307.
   PubMed Web of Science ®Google Scholar
• Hudson, L. G., J. B. Santon, and G. N. Gill 1989. Regulation of epidermal growth factor receptor gene expression. Mol. Endocrinol. 3: 400–408.
   PubMedGoogle Scholar
• Ishii, S., Y.-H. Xu, R. H. Stratton, B. A. Roe, G. T. Merlino, and I. Pastan 1985. Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene. Proc. Natl. Acad. Sci. USA 82: 4920–4924.
   PubMed Web of Science ®Google Scholar
• Ishov, A. M., R. Stenberg, and G. G. Maul 1997. Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment. J. Cell Biol. 138: 5–16.
   PubMed Web of Science ®Google Scholar
• Jensen, D., A. R. Black, A. Swick, and J. C. Azizkhan 1997. Distinct role for Sp1 and E2F sites in the growth/cell cycle regulation of the DHFR promoter. J. Cell. Biochem. 67: 24–31.
   PubMed Web of Science ®Google Scholar
• Johnson, A. C., S. Ishii, Y. Jinno, I. Pastan, and G. T. Merlino 1988. Epidermal growth factor receptor gene promoter. J. Biol. Chem. 263: 5693–5699.
   PubMed Web of Science ®Google Scholar
• Johnson, D., J. Schwarz, W. Cress, and J. Nevins 1993. Expression of transcription factor E2F1 induces quiescent cells to enter S phase. Nature 365: 349–352.
   PubMed Web of Science ®Google Scholar
• Kadonaga, J. T., A. J. Courey, J. Ladika, and R. Tjian 1988. Distinct regions of Sp1 modulate DNA binding and transcriptional activation. Science 242: 1566–1570.
   PubMed Web of Science ®Google Scholar
• Kageyama, R., G. T. Merlino, and I. Pastan 1988. Epidermal growth factor (EGF) receptor gene transcription. J. Biol. Chem. 263: 6329–6336.
   PubMedGoogle Scholar
• Kakizuka, A., W. H. J. Miller, K. Umesono, R. P. J. Warrell, S. R. Frankel, V. V. V. S. Murty, E. Dmitrovsky, and R. M. Evans 1991. Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RARalpha with a novel putative transcription factor, PML. Cell 66: 663–674.
   PubMed Web of Science ®Google Scholar
• Karlseder, J., H. Rotheneder, and E. Wintersberger 1996. Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F. Mol. Cell. Biol. 16: 1659–1667.
   PubMed Web of Science ®Google Scholar
• Kastner, P., A. Perez, Y. Lutz, C. Rochette Egly, M. P. Gaub, B. Durand, M. Lanotte, R. Berger, and P. Chambon 1992. Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins. EMBO J. 11: 629–642.
   PubMed Web of Science ®Google Scholar
• Kennett, S. B., A. J. Udvadia, and J. M. Horowitz 1997. Sp3 encodes multiple proteins that differ in their capacity to stimulate or repress transcription. Nucleic Acids Res. 25: 3110–3117.
   PubMed Web of Science ®Google Scholar
• Koken, M. H. M., G. Linares Cruz, F. Quignon, A. Viron, M. K. Chelbi Alix, J. Sobczak Thepot, L. Juhlin, L. Degos, F. Calvo, and H. De Thé 1995. The PML growth-suppressor has an altered expression in human oncogenesis. Oncogene 10: 1315–1324.
   PubMed Web of Science ®Google Scholar
• Koken, M. H. M., A. Reid, F. Quignon, M. K. Chelbi-Alix, J. M. Davies, J. H. S. Kabarowski, J. Zhu, S. Dong, S.-J. Chen, Z. Chen, C. C. Tan, J. Licht, S. Waxman, H. De Thé, and A. Zelent 1997. Leukemia-associated retinoic acid receptor alpha fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies. Proc. Natl. Acad. Sci. USA 94: 10255–10260.
   PubMed Web of Science ®Google Scholar
• Kumar, A. P., and A. P. Butler 1997. Transcription factor Sp3 antagonizes activation of the ornithine decarboxylase promoter by Sp1. Nucleic Acids Res. 25: 2012–2019.
   PubMedGoogle 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
• Le, X.-F., S. Vallian, Z.-M. Mu, M.-C. Hung, and K.-S. Chang 1998. Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis. Oncogene 16: 1839–1849.
   PubMedGoogle Scholar
• Le, X. F., P. Yang, and K. S. Chang 1996. Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene, PML. J. Biol. Chem. 271: 130–135.
   PubMed Web of Science ®Google Scholar
• Lee, J.-S., K. M. Galvin, and Y. Shi 1993. Evidence for physical interaction between the zinc-finger transcription factor YY1 and Sp1. Proc. Natl. Acad. Sci. USA 90: 6145–6149.
   PubMed Web of Science ®Google Scholar
• Lin, S.-Y., A. R. Black, D. Kostic, S. Pajovic, C. N. Hoover, and J. C. Azizkhan 1996. Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction. Mol. Cell. Biol. 16: 1668–1675.
   PubMed Web of Science ®Google Scholar
• Liu, J. H., Z. M. Mu, and K. S. Chang 1995. PML suppresses oncogenic transformation of NIH/3T3 cells by activated neu. J. Exp. Med. 181: 1965–1973.
   PubMedGoogle Scholar
• Morishige, K.-I., H. Kurachi, K. Amemiya, Y. Fujita, T. Yamamoto, A. Miyake, and O. Tanizawa 1991. Evidence for the involvement of transforming growth factor alpha and epidermal growth factor receptor autocrine growth mechanism in primary human ovarian cancers in vitro. Cancer Res. 51: 5322–5328.
   PubMed Web of Science ®Google Scholar
• Mu, Z.-M., X.-F. Le, S. Vallian, A. B. Glassman, and K.-S. Chang 1997. Stable overexpression of PML alters regulation of cell cycle progression in HeLa cells. Carcinogenesis 18: 2063–2069.
   PubMedGoogle Scholar
• Mu, Z.-M., K.-V. Chin, J.-H. Liu, G. Lozano, and K.-S. Chang 1994. PML, a growth suppressor disrupted in acute promyelocytic leukemia. Mol. Cell. Biol. 14: 6858–6867.
   PubMed Web of Science ®Google Scholar
• Mukhopadhyay, D., B. Knebelmann, H. T. Cohen, S. Ananth, and V. P. Sukhatme 1997. The von Hippel-Lindau tumor suppressor gene product interacts with Sp1 to repress vascular endothelial growth factor promoter activity. Mol. Cell. Biol. 17: 5629–5639.
   PubMed Web of Science ®Google Scholar
• Noe, V., C. Chen, C. Alemany, M. Nicolas, I. Caragol, L. Chasin, and C. Ciudad 1997. Cell-growth regulation of the hamster dihydrofolate reductase gene promoter by transcription factor Sp1. Eur. J. Biochem. 249: 13–20.
   PubMedGoogle Scholar
• Szekely, L., K. Pokrovskaja, W.-Q. Jiang, H. de Thé, N. Ringertz, and G. Klein 1996. The Epstein-Barr virus-encoded nuclear antigen EBNA-5 accumulates in PML-containing bodies. J. Virol. 70: 2562–2568.
   PubMedGoogle Scholar
• Toi, M., A. Osaki, H. Yamada, and T. Toge 1991. Epidermal growth factor receptor expression as a prognostic indicator in breast cancer. Eur. J. Cancer 27: 977–980.
   PubMed Web of Science ®Google Scholar
• Udvadia, A. J., K. T. Rogers, P. D. Higgins, Y. Murata, K. H. Martin, P. A. Humphrey, and J. M. Horowitz 1993. Sp-1 binds promoter elements regulated by the RB protein and Sp-1-mediated transcription is stimulated by RB coexpression. Proc. Natl. Acad. Sci. USA 90: 3265–3269.
   PubMed Web of Science ®Google Scholar
• Udvadia, A. J., D. J. Templeton, and J. M. Horowitz 1995. Functional interactions between the retinoblastoma (Rb) protein and Sp-family members: superactivation by Rb requires amino acids necessary for growth suppression. Proc. Natl. Acad. Sci. USA 92: 3953–3957.
   PubMed Web of Science ®Google Scholar
• Vallian, S., A. J. Gaken, E. B. Gingold, T. Kouzarides, K.-S. Chang, and F. Farzaneh 1998. Modulation of Fos-mediated AP1 transcription by the promyelocytic leukemia protein. Oncogene 16: 2843–2853.
   PubMedGoogle Scholar
• Vallian, S., A. J. 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.
   PubMed Web of Science ®Google Scholar
• Wang, Z. G., L. Delva, M. Gaboli, R. Rivi, M. Giorgio, C. Cordon-Cardo, F. Grosveld, and P. P. Pandolfi 1998. Role of PML in cell growth and the retinoic acid pathway. Science 279: 1547–1551.
   PubMed Web of Science ®Google Scholar
• Weis, K., S. Rambaud, C. Lavau, J. Jansen, T. Carvalho, M. Carmo Fonseca, A. Lamond, and A. Dejean 1994. Retinoic acid regulates aberrant nuclear localization of PML-RARalpha in acute promyelocytic leukemia cells. Cell 76: 345–356.
   PubMed Web of Science ®Google Scholar
• Xu, J., K. L. Thompson, L. B. Shephard, L. G. Hudson, and G. N. Gill 1993. T3 receptor suppression of Sp1-dependent transcription from the epidermal growth factor receptor promoter via overlapping DNA-binding sites. J. Biol. Chem. 268: 16065–16073.
   PubMedGoogle Scholar