Identification of Mammalian Sds3 as an Integral Component of the Sin3/Histone Deacetylase Corepressor Complex

REFERENCES

• Alland, L., R. Muhle, H. Hou, Jr., J. Potes, L. Chin, N. Schreiber-Agus, and R. A. DePinho. 1997. Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression. Nature 387: 49–55.
   PubMed Web of Science ®Google Scholar
• Ayer, D. E., C. D. Laherty, Q. A. Lawrence, A. P. Armstrong, and R. N. Eisenman. 1996. Mad proteins contain a dominant transcription repression domain. Mol. Cell. Biol. 16: 5772–5781.
   PubMedGoogle Scholar
• Ayer, D. E., Q. A. Lawrence, and R. N. Eisenman. 1995. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell 80: 767–776.
   PubMed Web of Science ®Google Scholar
• David, G., L. Alland, S. H. Hong, C. W. Wong, R. A. DePinho, and A. Dejean. 1998. Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein. Oncogene 16: 2549–2556.
   PubMed Web of Science ®Google Scholar
• Dhordain, P., O. Albagli, R. J. Lin, S. Ansieau, S. Quief, A. Leutz, J. P. Kerckaert, R. M. Evans, and D. Leprince. 1997. Corepressor SMRT binds the BTB/POZ repressing domain of the LAZ3/BCL6 oncoprotein. Proc. Natl. Acad. Sci. USA 94: 10762–10767.
   PubMed Web of Science ®Google Scholar
• Dorland, S., M. L. Deegenaars, and D. J. Stillman. 2000. Roles for the Saccharomyces cerevisiae SDS3, CBK1 and HYM1 genes in transcriptional repression by SIN3. Genetics 154: 573–586.
   PubMedGoogle Scholar
• Eagle, L. R., X. Yin, A. R. Brothman, B. J. Williams, N. B. Atkin, and E. V. Prochownik. 1995. Mutation of the MXI1 gene in prostate cancer. Nat. Genet. 9: 249–255.
   PubMed Web of Science ®Google Scholar
• Elbashir, S. M., J. Harborth, W. Lendeckel, A. Yalcin, K. Weber, and T. Tuschl. 2001. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411: 494–498.
   PubMed Web of Science ®Google Scholar
• Grignani, F., S. De Matteis, C. Nervi, L. Tomassoni, V. Gelmetti, M. Cioce, M. Fanelli, M. Ruthardt, F. F. Ferrara, I. Zamir, C. Seiser, M. A. Lazar, S. Minucci, and P. G. Pelicci. 1998. Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia. Nature 391: 815–818.
   PubMed Web of Science ®Google Scholar
• Guenther, M. G., O. Barak, and M. A. Lazar. 2001. The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3. Mol. Cell. Biol. 21: 6091–6101.
   Google Scholar
• Guidez, F., S. Ivins, J. Zhu, M. Soderstrom, S. Waxman, and A. Zelent. 1998. Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML- and PLZF-RARalpha underlie molecular pathogenesis and treatment of acute promyelocytic leukemia. Blood 91: 2634–2642.
   PubMed Web of Science ®Google Scholar
• Hassig, C. A., T. C. Fleischer, A. N. Billin, S. L. Schreiber, and D. E. Ayer. 1997. Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell 89: 341–347.
   PubMed Web of Science ®Google Scholar
• Heinzel, T., R. M. Lavinsky, T. M. Mullen, M. Soderstrom, C. D. Laherty, J. Torchia, W. M. Yang, G. Brard, S. D. Ngo, J. R. Davie, E. Seto, R. N. Eisenman, D. W. Rose, C. K. Glass, and M. G. Rosenfeld. 1997. A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 387: 43–48.
   PubMed Web of Science ®Google Scholar
• Kasten, M. M., S. Dorland, and D. J. Stillman. 1997. A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators. Mol. Cell. Biol. 17: 4852–4858.
   PubMedGoogle Scholar
• Kingston, R. E., and G. J. Narlikar. 1999. ATP-dependent remodeling and acetylation as regulators of chromatin fluidity. Genes Dev. 13: 2339–2352.
   PubMed Web of Science ®Google Scholar
• Laherty, C. D., W. M. Yang, J. M. Sun, J. R. Davie, E. Seto, and R. N. Eisenman. 1997. Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell 89: 349–356.
   PubMed Web of Science ®Google Scholar
• Lechner, T., M. J. Carrozza, Y. Yu, P. A. Grant, A. Eberharter, D. Vannier, G. Brosch, D. J. Stillman, D. Shore, and J. L. Workman. 2000. Sds3 (suppressor of defective silencing 3) is an integral component of the yeast Sin3·Rpd3 histone deacetylase complex and is required for histone deacetylase activity. J. Biol. Chem. 275: 40961–40966.
   PubMed Web of Science ®Google Scholar
• Lin, R. J., L. Nagy, S. Inoue, W. Shao, W. H. Miller, Jr., and R. M. Evans. 1998. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 391: 811–814.
   PubMed Web of Science ®Google Scholar
• Melnick, A. M., J. J. Westendorf, A. Polinger, G. W. Carlile, S. Arai, H. J. Ball, B. Lutterbach, S. W. Hiebert, and J. D. Licht. 2000. The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is a corepressor for the promyelocytic leukemia zinc finger protein. Mol. Cell. Biol. 20: 2075–2086.
   PubMed Web of Science ®Google Scholar
• Nagy, L., H. Y. Kao, D. Chakravarti, R. J. Lin, C. A. Hassig, D. E. Ayer, S. L. Schreiber, and R. M. Evans. 1997. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 89: 373–380.
   PubMed Web of Science ®Google Scholar
• Nasmyth, K., D. Stillman, and D. Kipling. 1987. Both positive and negative regulators of HO transcription are required for mother-cell-specific mating-type switching in yeast. Cell 48: 579–587.
   PubMed Web of Science ®Google Scholar
• Newmark, H. L., J. R. Lupton, and C. W. Young. 1994. Butyrate as a differentiating agent: pharmacokinetics, analogues and current status. Cancer Lett. 78: 1–5.
   PubMed Web of Science ®Google Scholar
• Pandolfi, P. P. 2001. Histone deacetylases and transcriptional therapy with their inhibitors. Cancer Chemother. Pharmacol. 48(Suppl. 1): S17–S19.
   PubMed Web of Science ®Google Scholar
• Parthun, M. R., J. Widom, and D. E. Gottschling. 1996. The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism. Cell 87: 85–94.
   PubMed Web of Science ®Google Scholar
• Prochownik, E. V., L. Eagle Grove, D. Deubler, X. L. Zhu, R. A. Stephenson, L. R. Rohr, X. Yin, and A. R. Brothman. 1998. Commonly occurring loss and mutation of the MXI1 gene in prostate cancer. Genes Chromosomes Cancer 22: 295–304.
   PubMed Web of Science ®Google Scholar
• Rao, G., L. Alland, P. Guida, N. Schreiber-Agus, K. Chen, L. Chin, J. M. Rochelle, M. F. Seldin, A. I. Skoultchi, and R. A. DePinho. 1996. Mouse Sin3A interacts with and can functionally substitute for the amino-terminal repression of the Myc antagonist Mxi1. Oncogene 12: 1165–1172.
   PubMedGoogle Scholar
• Sattler, H. P., V. Rohde, H. Bonkhoff, T. Zwergel, and B. Wullich. 1999. Comparative genomic hybridization reveals DNA copy number gains to frequently occur in human prostate cancer. Prostate 39: 79–86.
   PubMedGoogle Scholar
• Schreiber-Agus, N., L. Chin, K. Chen, R. Torres, G. Rao, P. Guida, A. I. Skoultchi, and R. A. DePinho. 1995. An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell 80: 777–786.
   PubMed Web of Science ®Google Scholar
• Schreiber-Agus, N., Y. Meng, T. Hoang, H. Hou, Jr., K. Chen, R. Greenberg, C. Cordon-Cardo, H. W. Lee, and R. A. DePinho. 1998. Role of Mxi1 in ageing organ systems and the regulation of normal and neoplastic growth. Nature 393: 483–487.
   PubMed Web of Science ®Google Scholar
• Seraj, M. J., R. S. Samant, M. F. Verderame, and D. R. Welch. 2000. Functional evidence for a novel human breast carcinoma metastasis suppressor, BRMS1, encoded at chromosome 11q13. Cancer Res. 60: 2764–2769.
   PubMedGoogle Scholar
• Smith, R. F., B. A. Wiese, M. K. Wojzynski, D. B. Davison, and K. C. Worley. 1996. BCM Search Launcher-an integrated interface to molecular biology data base search and analysis services available on the World Wide Web. Genome Res. 6: 454–462.
   PubMedGoogle Scholar
• Stillman, D. J., S. Dorland, and Y. Yu. 1994. Epistasis analysis of suppressor mutations that allow HO expression in the absence of the yeast SW15 transcriptional activator. Genetics 136: 781–788.
   PubMedGoogle Scholar
• Taunton, J., C. A. Hassig, and S. L. Schreiber. 1996. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272: 408–411.
   PubMed Web of Science ®Google Scholar
• Vannier, D., D. Balderes, and D. Shore. 1996. Evidence that the transcriptional regulators SIN3 and RPD3, and a novel gene (SDS3) with similar functions, are involved in transcriptional silencing in S. cerevisiae. Genetics 144: 1343–1353.
   Google Scholar
• Vannier, D., P. Damay, and D. Shore. 2001. A role for Sds3p, a component of the Rpd3p/Sin3p deacetylase complex, in maintaining cellular integrity in Saccharomyces cerevisiae. Mol. Genet. Genomics 265: 560–568.
   PubMedGoogle Scholar
• Verreault, A., P. D. Kaufman, R. Kobayashi, and B. Stillman. 1996. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 87: 95–104.
   PubMed Web of Science ®Google Scholar
• Vojtek, A. B., S. M. Hollenberg, and J. A. Cooper. 1993. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74: 205–214.
   PubMed Web of Science ®Google Scholar
• Yang, W. M., C. Inouye, Y. Zeng, D. Bearss, and E. Seto. 1996. Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc. Natl. Acad. Sci. USA 93: 12845–12850.
   PubMed Web of Science ®Google Scholar
• You, A., J. K. Tong, C. M. Grozinger, and S. L. Schreiber. 2001. CoREST is an integral component of the CoREST-human histone deacetylase complex. Proc. Natl. Acad. Sci. USA 98: 1454–1458.
   PubMed Web of Science ®Google Scholar
• Zhang, Y., R. Iratni, H. Erdjument-Bromage, P. Tempst, and D. Reinberg. 1997. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell 89: 357–364.
   PubMedGoogle Scholar
• Zhang, Y., H. H. Ng, H. Erdjument-Bromage, P. Tempst, A. Bird, and D. Reinberg. 1999. Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation. Genes Dev. 13: 1924–1935.
   PubMed Web of Science ®Google Scholar
• Zhang, Y., Z. W. Sun, R. Iratni, H. Erdjument-Bromage, P. Tempst, M. Hampsey, and D. Reinberg. 1998. SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex. Mol. Cell 1: 1021–1031.
   PubMedGoogle Scholar