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Volumn 35, Issue 6, 2010, Pages 323-332

Polycomb group protein-mediated repression of transcription

Author keywords

[No Author keywords available]

Indexed keywords

DNA; EMBRYONIC ECTODERM DEVELOPMENT PROTEIN; HISTONE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE H2A; HISTONE H3; HISTONE METHYLTRANSFERASE; HOMEODOMAIN PROTEIN; POLYCOMB GROUP PROTEIN; POLYCOMB REPRESSIVE COMPLEX 1; POLYCOMB REPRESSIVE COMPLEX 2; RING FINGER PROTEIN; TRANSCRIPTION FACTOR EZH2; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UNTRANSLATED RNA;

EID: 77954758157     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2010.02.009     Document Type: Review
Times cited : (328)

References (87)
  • 1
    • 0029416901 scopus 로고
    • The Polycomb and trithorax group proteins of Drosophila: trans-regulators of homeotic gene function
    • Kennison J.A. The Polycomb and trithorax group proteins of Drosophila: trans-regulators of homeotic gene function. Annu. Rev. Genet. 1995, 29:289-303.
    • (1995) Annu. Rev. Genet. , vol.29 , pp. 289-303
    • Kennison, J.A.1
  • 2
    • 57049141484 scopus 로고    scopus 로고
    • Dynamic regulation by polycomb group protein complexes controls pattern formation and the cell cycle in Drosophila
    • Oktaba K., et al. Dynamic regulation by polycomb group protein complexes controls pattern formation and the cell cycle in Drosophila. Dev. Cell 2008, 15:877-889.
    • (2008) Dev. Cell , vol.15 , pp. 877-889
    • Oktaba, K.1
  • 3
    • 1642633053 scopus 로고    scopus 로고
    • Bmi1 is essential for cerebellar development and is overexpressed in human medulloblastomas
    • Leung C., et al. Bmi1 is essential for cerebellar development and is overexpressed in human medulloblastomas. Nature 2004, 428:337-341.
    • (2004) Nature , vol.428 , pp. 337-341
    • Leung, C.1
  • 4
    • 0037673984 scopus 로고    scopus 로고
    • Bmi-1 determines the proliferative capacity of normal and leukaemic stem cells
    • Lessard J., Sauvageau G. Bmi-1 determines the proliferative capacity of normal and leukaemic stem cells. Nature 2003, 423:255-260.
    • (2003) Nature , vol.423 , pp. 255-260
    • Lessard, J.1    Sauvageau, G.2
  • 5
    • 33750379420 scopus 로고    scopus 로고
    • Polycomb silencers control cell fate, development and cancer
    • Sparmann A., van Lohuizen M. Polycomb silencers control cell fate, development and cancer. Nat. Rev. Cancer 2006, 6:846-856.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 846-856
    • Sparmann, A.1    van Lohuizen, M.2
  • 6
    • 33947134834 scopus 로고    scopus 로고
    • The Polycomb group proteins bind throughout the INK4A-ARF locus and are disassociated in senescent cells
    • Bracken A.P., et al. The Polycomb group proteins bind throughout the INK4A-ARF locus and are disassociated in senescent cells. Genes Dev. 2007, 21:525-530.
    • (2007) Genes Dev. , vol.21 , pp. 525-530
    • Bracken, A.P.1
  • 7
    • 0034934749 scopus 로고    scopus 로고
    • Imprinted X inactivation maintained by a mouse Polycomb group gene
    • Wang J., et al. Imprinted X inactivation maintained by a mouse Polycomb group gene. Nat. Genet. 2001, 28:371-375.
    • (2001) Nat. Genet. , vol.28 , pp. 371-375
    • Wang, J.1
  • 8
    • 7744228427 scopus 로고    scopus 로고
    • Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation
    • de Napoles M., et al. Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation. Dev. Cell 2004, 7:663-676.
    • (2004) Dev. Cell , vol.7 , pp. 663-676
    • de Napoles, M.1
  • 9
    • 34248169728 scopus 로고    scopus 로고
    • The polycomb group protein Suz12 is required for embryonic stem cell differentiation
    • Pasini D., et al. The polycomb group protein Suz12 is required for embryonic stem cell differentiation. Mol. Cell Biol. 2007, 27:3769-3779.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 3769-3779
    • Pasini, D.1
  • 10
    • 0034977239 scopus 로고    scopus 로고
    • The polycomb-group gene Ezh2 is required for early mouse development
    • O'Carroll D., et al. The polycomb-group gene Ezh2 is required for early mouse development. Mol. Cell Biol. 2001, 21:4330-4336.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 4330-4336
    • O'Carroll, D.1
  • 11
    • 8144230178 scopus 로고    scopus 로고
    • Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity
    • Pasini D., et al. Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity. EMBO J. 2004, 23:4061-4071.
    • (2004) EMBO J. , vol.23 , pp. 4061-4071
    • Pasini, D.1
  • 12
    • 0028910338 scopus 로고
    • The eed mutation disrupts anterior mesoderm production in mice
    • Faust C., et al. The eed mutation disrupts anterior mesoderm production in mice. Development 1995, 121:273-285.
    • (1995) Development , vol.121 , pp. 273-285
    • Faust, C.1
  • 13
    • 0345269795 scopus 로고    scopus 로고
    • Rnf2 (Ring1b) deficiency causes gastrulation arrest and cell cycle inhibition
    • Voncken J.W., et al. Rnf2 (Ring1b) deficiency causes gastrulation arrest and cell cycle inhibition. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:2468-2473.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2468-2473
    • Voncken, J.W.1
  • 14
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • Cao R., et al. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 2002, 298:1039-1043.
    • (2002) Science , vol.298 , pp. 1039-1043
    • Cao, R.1
  • 15
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein
    • Kuzmichev A., et al. Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev. 2002, 16:2893-2905.
    • (2002) Genes Dev. , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1
  • 16
    • 0035141264 scopus 로고    scopus 로고
    • The Drosophila Polycomb Group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3
    • Tie F., et al. The Drosophila Polycomb Group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3. Development 2001, 128:275-286.
    • (2001) Development , vol.128 , pp. 275-286
    • Tie, F.1
  • 17
    • 9444244427 scopus 로고    scopus 로고
    • Chromatin compaction by a polycomb group protein complex
    • Francis N.J., et al. Chromatin compaction by a polycomb group protein complex. Science 2004, 306:1574-1577.
    • (2004) Science , vol.306 , pp. 1574-1577
    • Francis, N.J.1
  • 18
    • 38149098408 scopus 로고    scopus 로고
    • Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation
    • Zhou W., et al. Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation. Mol. Cell 2008, 29:69-80.
    • (2008) Mol. Cell , vol.29 , pp. 69-80
    • Zhou, W.1
  • 19
    • 70349469565 scopus 로고    scopus 로고
    • Mechanisms of polycomb gene silencing: knowns and unknowns
    • Simon J.A., Kingston R.E. Mechanisms of polycomb gene silencing: knowns and unknowns. Nat. Rev. Mol. Cell Biol. 2009, 10:697-708.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 697-708
    • Simon, J.A.1    Kingston, R.E.2
  • 20
    • 29144487990 scopus 로고    scopus 로고
    • Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing
    • Cao R., et al. Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol. Cell 2005, 20:845-854.
    • (2005) Mol. Cell , vol.20 , pp. 845-854
    • Cao, R.1
  • 21
    • 33745753378 scopus 로고    scopus 로고
    • Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b
    • Buchwald G., et al. Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b. EMBO J. 2006, 25:2465-2474.
    • (2006) EMBO J. , vol.25 , pp. 2465-2474
    • Buchwald, G.1
  • 22
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 is a SUMO E3
    • Kagey M.H., et al. The polycomb protein Pc2 is a SUMO E3. Cell 2003, 113:127-137.
    • (2003) Cell , vol.113 , pp. 127-137
    • Kagey, M.H.1
  • 23
    • 34447127473 scopus 로고    scopus 로고
    • Polycomb protein Cbx4 promotes SUMO modification of de novo DNA methyltransferase Dnmt3a
    • Li B., et al. Polycomb protein Cbx4 promotes SUMO modification of de novo DNA methyltransferase Dnmt3a. Biochem. J. 2007, 405:369-378.
    • (2007) Biochem. J. , vol.405 , pp. 369-378
    • Li, B.1
  • 24
    • 33749058094 scopus 로고    scopus 로고
    • Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2
    • Roscic A., et al. Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2. Mol. Cell 2006, 24:77-89.
    • (2006) Mol. Cell , vol.24 , pp. 77-89
    • Roscic, A.1
  • 25
    • 33751027683 scopus 로고    scopus 로고
    • Human cystathionine beta-synthase is a target for sumoylation
    • Kabil O., et al. Human cystathionine beta-synthase is a target for sumoylation. Biochemistry 2006, 45:13528-13536.
    • (2006) Biochemistry , vol.45 , pp. 13528-13536
    • Kabil, O.1
  • 26
    • 27444442397 scopus 로고    scopus 로고
    • Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates transcriptional repression of E-cadherin
    • Long J., et al. Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates transcriptional repression of E-cadherin. J. Biol. Chem. 2005, 280:35477-35489.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35477-35489
    • Long, J.1
  • 27
    • 33846983276 scopus 로고    scopus 로고
    • Polycomb/Trithorax response elements and epigenetic memory of cell identity
    • Ringrose L., Paro R. Polycomb/Trithorax response elements and epigenetic memory of cell identity. Development 2007, 134:223-232.
    • (2007) Development , vol.134 , pp. 223-232
    • Ringrose, L.1    Paro, R.2
  • 28
    • 33748419671 scopus 로고    scopus 로고
    • Polycomb response elements and targeting of Polycomb group proteins in
    • Muller J., Kassis J.A. Polycomb response elements and targeting of Polycomb group proteins in. Drosophila. Curr. Opin. Genet. Dev. 2006, 16:476-484.
    • (2006) Drosophila. Curr. Opin. Genet. Dev. , vol.16 , pp. 476-484
    • Muller, J.1    Kassis, J.A.2
  • 29
    • 69449086947 scopus 로고    scopus 로고
    • A vertebrate Polycomb response element governs segmentation of the posterior hindbrain
    • Sing A., et al. A vertebrate Polycomb response element governs segmentation of the posterior hindbrain. Cell 2009, 138:885-897.
    • (2009) Cell , vol.138 , pp. 885-897
    • Sing, A.1
  • 30
    • 7544230144 scopus 로고    scopus 로고
    • The Polycomb Ezh2 methyltransferase regulates muscle gene expression and skeletal muscle differentiation
    • Caretti G., et al. The Polycomb Ezh2 methyltransferase regulates muscle gene expression and skeletal muscle differentiation. Genes Dev. 2004, 18:2627-2638.
    • (2004) Genes Dev. , vol.18 , pp. 2627-2638
    • Caretti, G.1
  • 31
    • 73149111929 scopus 로고    scopus 로고
    • A region of the human HOXD cluster that confers polycomb-group responsiveness
    • Woo, C.J. et al. A region of the human HOXD cluster that confers polycomb-group responsiveness. Cell 140, 99-110.
    • Cell , vol.140 , pp. 99-110
    • Woo, C.J.1
  • 32
    • 37249012276 scopus 로고    scopus 로고
    • Nucleosome destabilization in the epigenetic regulation of gene expression
    • Henikoff S. Nucleosome destabilization in the epigenetic regulation of gene expression. Nat. Rev. Genet. 2008, 9:15-26.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 15-26
    • Henikoff, S.1
  • 33
    • 55549141877 scopus 로고    scopus 로고
    • Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks
    • Zilberman D., et al. Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks. Nature 2008, 456:125-129.
    • (2008) Nature , vol.456 , pp. 125-129
    • Zilberman, D.1
  • 34
    • 55549148715 scopus 로고    scopus 로고
    • H2AZ is enriched at polycomb complex target genes in ES cells and is necessary for lineage commitment
    • Creyghton M.P., et al. H2AZ is enriched at polycomb complex target genes in ES cells and is necessary for lineage commitment. Cell 2008, 135:649-661.
    • (2008) Cell , vol.135 , pp. 649-661
    • Creyghton, M.P.1
  • 35
    • 34250729138 scopus 로고    scopus 로고
    • Functional demarcation of active and silent chromatin domains in human HOX loci by noncoding RNAs
    • Rinn J.L., et al. Functional demarcation of active and silent chromatin domains in human HOX loci by noncoding RNAs. Cell 2007, 129:1311-1323.
    • (2007) Cell , vol.129 , pp. 1311-1323
    • Rinn, J.L.1
  • 36
    • 55349109963 scopus 로고    scopus 로고
    • Polycomb proteins targeted by a short repeat RNA to the mouse X chromosome
    • Zhao J., et al. Polycomb proteins targeted by a short repeat RNA to the mouse X chromosome. Science 2008, 322:750-756.
    • (2008) Science , vol.322 , pp. 750-756
    • Zhao, J.1
  • 37
    • 33746407708 scopus 로고    scopus 로고
    • Recruitment of PRC1 function at the initiation of X inactivation independent of PRC2 and silencing
    • Schoeftner S., et al. Recruitment of PRC1 function at the initiation of X inactivation independent of PRC2 and silencing. EMBO J. 2006, 25:3110-3122.
    • (2006) EMBO J. , vol.25 , pp. 3110-3122
    • Schoeftner, S.1
  • 38
    • 54049138948 scopus 로고    scopus 로고
    • Kcnq1ot1 antisense noncoding RNA mediates lineage-specific transcriptional silencing through chromatin-level regulation
    • Pandey R.R., et al. Kcnq1ot1 antisense noncoding RNA mediates lineage-specific transcriptional silencing through chromatin-level regulation. Mol. Cell 2008, 32:232-246.
    • (2008) Mol. Cell , vol.32 , pp. 232-246
    • Pandey, R.R.1
  • 39
    • 62249133709 scopus 로고    scopus 로고
    • Chromatin signature reveals over a thousand highly conserved large non-coding RNAs in mammals
    • Guttman M., et al. Chromatin signature reveals over a thousand highly conserved large non-coding RNAs in mammals. Nature 2009, 458:223-227.
    • (2009) Nature , vol.458 , pp. 223-227
    • Guttman, M.1
  • 40
    • 67650921949 scopus 로고    scopus 로고
    • Many human large intergenic noncoding RNAs associate with chromatin-modifying complexes and affect gene expression
    • Khalil A.M., et al. Many human large intergenic noncoding RNAs associate with chromatin-modifying complexes and affect gene expression. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:11667-11672.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 11667-11672
    • Khalil, A.M.1
  • 41
    • 12144287606 scopus 로고    scopus 로고
    • Oculofaciocardiodental and Lenz microphthalmia syndromes result from distinct classes of mutations in BCOR
    • Ng D., et al. Oculofaciocardiodental and Lenz microphthalmia syndromes result from distinct classes of mutations in BCOR. Nat. Genet. 2004, 36:411-416.
    • (2004) Nat. Genet. , vol.36 , pp. 411-416
    • Ng, D.1
  • 42
    • 0030901289 scopus 로고    scopus 로고
    • Control of inflammation, cytokine expression, and germinal center formation by BCL-6
    • Dent A.L., et al. Control of inflammation, cytokine expression, and germinal center formation by BCL-6. Science 1997, 276:589-592.
    • (1997) Science , vol.276 , pp. 589-592
    • Dent, A.L.1
  • 43
    • 0027495491 scopus 로고
    • Alterations of a zinc finger-encoding gene, BCL-6, in diffuse large-cell lymphoma
    • Ye B.H., et al. Alterations of a zinc finger-encoding gene, BCL-6, in diffuse large-cell lymphoma. Science 1993, 262:747-750.
    • (1993) Science , vol.262 , pp. 747-750
    • Ye, B.H.1
  • 44
    • 68249129007 scopus 로고    scopus 로고
    • BCOR regulates mesenchymal stem cell function by epigenetic mechanisms
    • Fan Z., et al. BCOR regulates mesenchymal stem cell function by epigenetic mechanisms. Nat. Cell Biol. 2009, 11:1002-1009.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1002-1009
    • Fan, Z.1
  • 45
    • 33748641974 scopus 로고    scopus 로고
    • Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets
    • Gearhart M.D., et al. Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets. Mol. Cell Biol. 2006, 26:6880-6889.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 6880-6889
    • Gearhart, M.D.1
  • 46
    • 34648834735 scopus 로고    scopus 로고
    • Pcl-PRC2 is needed to generate high levels of H3-K27 trimethylation at Polycomb target genes
    • Nekrasov M., et al. Pcl-PRC2 is needed to generate high levels of H3-K27 trimethylation at Polycomb target genes. EMBO J. 2007, 26:4078-4088.
    • (2007) EMBO J. , vol.26 , pp. 4078-4088
    • Nekrasov, M.1
  • 47
    • 42149149895 scopus 로고    scopus 로고
    • Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo
    • Sarma K., et al. Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo. Mol. Cell Biol. 2008, 28:2718-2731.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 2718-2731
    • Sarma, K.1
  • 48
    • 40749126138 scopus 로고    scopus 로고
    • Role of hPHF1 in H3K27 methylation and Hox gene silencing
    • Cao R., et al. Role of hPHF1 in H3K27 methylation and Hox gene silencing. Mol. Cell Biol. 2008, 28:1862-1872.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 1862-1872
    • Cao, R.1
  • 49
    • 52649125361 scopus 로고    scopus 로고
    • MBD3, a component of the NuRD complex, facilitates chromatin alteration and deposition of epigenetic marks
    • Morey L., et al. MBD3, a component of the NuRD complex, facilitates chromatin alteration and deposition of epigenetic marks. Mol. Cell Biol. 2008, 28:5912-5923.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 5912-5923
    • Morey, L.1
  • 50
    • 34249869559 scopus 로고    scopus 로고
    • Role of the polycomb repressive complex 2 in acute promyelocytic leukemia
    • Villa R., et al. Role of the polycomb repressive complex 2 in acute promyelocytic leukemia. Cancer Cell 2007, 11:513-525.
    • (2007) Cancer Cell , vol.11 , pp. 513-525
    • Villa, R.1
  • 51
    • 66149154321 scopus 로고    scopus 로고
    • The PRC1 Polycomb group complex interacts with PLZF/RARA to mediate leukemic transformation
    • Boukarabila H., et al. The PRC1 Polycomb group complex interacts with PLZF/RARA to mediate leukemic transformation. Genes Dev. 2009, 23:1195-1206.
    • (2009) Genes Dev. , vol.23 , pp. 1195-1206
    • Boukarabila, H.1
  • 52
    • 47949125993 scopus 로고    scopus 로고
    • Polycomb complex 2 is required for E-cadherin repression by the Snail1 transcription factor
    • Herranz N., et al. Polycomb complex 2 is required for E-cadherin repression by the Snail1 transcription factor. Mol. Cell Biol. 2008, 28:4772-4781.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 4772-4781
    • Herranz, N.1
  • 53
    • 72249119297 scopus 로고    scopus 로고
    • Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target gene occupancy in pluripotent cells
    • Peng J.C., et al. Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target gene occupancy in pluripotent cells. Cell 2009, 139:1290-1302.
    • (2009) Cell , vol.139 , pp. 1290-1302
    • Peng, J.C.1
  • 54
    • 72249104107 scopus 로고    scopus 로고
    • Jumonji modulates polycomb activity and self-renewal versus differentiation of stem cells
    • Shen X., et al. Jumonji modulates polycomb activity and self-renewal versus differentiation of stem cells. Cell 2009, 139:1303-1314.
    • (2009) Cell , vol.139 , pp. 1303-1314
    • Shen, X.1
  • 55
    • 77949414371 scopus 로고    scopus 로고
    • JARID2 regulates binding of the Polycomb repressive complex 2 to target genes in ES cells
    • Pasini D., et al. JARID2 regulates binding of the Polycomb repressive complex 2 to target genes in ES cells. Nature 2010, 464:306-310.
    • (2010) Nature , vol.464 , pp. 306-310
    • Pasini, D.1
  • 56
    • 76749083433 scopus 로고    scopus 로고
    • Jarid2 and PRC2, partners in regulating gene expression
    • Li G., et al. Jarid2 and PRC2, partners in regulating gene expression. Genes Dev. 2010, 24:368-380.
    • (2010) Genes Dev. , vol.24 , pp. 368-380
    • Li, G.1
  • 57
    • 55449105221 scopus 로고    scopus 로고
    • Genomewide analysis of PRC1 and PRC2 occupancy identifies two classes of bivalent domains
    • Ku M., et al. Genomewide analysis of PRC1 and PRC2 occupancy identifies two classes of bivalent domains. PLoS Genet 2008, 4:e1000242.
    • (2008) PLoS Genet , vol.4
    • Ku, M.1
  • 58
    • 57049089995 scopus 로고    scopus 로고
    • Hedgehog signaling in development and cancer
    • Jiang J., Hui C.C. Hedgehog signaling in development and cancer. Dev. Cell 2008, 15:801-812.
    • (2008) Dev. Cell , vol.15 , pp. 801-812
    • Jiang, J.1    Hui, C.C.2
  • 59
    • 70349527902 scopus 로고    scopus 로고
    • Polyhomeotic has a tumor suppressor activity mediated by repression of Notch signaling
    • Martinez A.M., et al. Polyhomeotic has a tumor suppressor activity mediated by repression of Notch signaling. Nat. Genet. 2009, 41:1076-1082.
    • (2009) Nat. Genet. , vol.41 , pp. 1076-1082
    • Martinez, A.M.1
  • 60
    • 70349545897 scopus 로고    scopus 로고
    • A tumor suppressor activity of Drosophila Polycomb genes mediated by JAK-STAT signaling
    • Classen A.K., et al. A tumor suppressor activity of Drosophila Polycomb genes mediated by JAK-STAT signaling. Nat. Genet. 2009, 41:1150-1155.
    • (2009) Nat. Genet. , vol.41 , pp. 1150-1155
    • Classen, A.K.1
  • 61
    • 26844520965 scopus 로고    scopus 로고
    • Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3
    • Cha T.L., et al. Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3. Science 2005, 310:306-310.
    • (2005) Science , vol.310 , pp. 306-310
    • Cha, T.L.1
  • 62
    • 33751515474 scopus 로고    scopus 로고
    • The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity
    • Ben-Saadon R., et al. The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity. Mol. Cell 2006, 24:701-711.
    • (2006) Mol. Cell , vol.24 , pp. 701-711
    • Ben-Saadon, R.1
  • 63
    • 0033567291 scopus 로고    scopus 로고
    • The stress-activated protein kinase pathways
    • Tibbles L.A., Woodgett J.R. The stress-activated protein kinase pathways. Cell Mol. Life Sci. 1999, 55:1230-1254.
    • (1999) Cell Mol. Life Sci. , vol.55 , pp. 1230-1254
    • Tibbles, L.A.1    Woodgett, J.R.2
  • 64
    • 14044263532 scopus 로고    scopus 로고
    • MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1
    • Voncken J.W., et al. MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1. J. Biol. Chem. 2005, 280:5178-5187.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5178-5187
    • Voncken, J.W.1
  • 65
    • 0033398254 scopus 로고    scopus 로고
    • Chromatin-association of the Polycomb group protein BMI1 is cell cycle-regulated and correlates with its phosphorylation status
    • Voncken J.W., et al. Chromatin-association of the Polycomb group protein BMI1 is cell cycle-regulated and correlates with its phosphorylation status. J. Cell Sci. 1999, 112(pt 24):4627-4639.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 24 , pp. 4627-4639
    • Voncken, J.W.1
  • 66
    • 69449092638 scopus 로고    scopus 로고
    • Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc)
    • Sinclair D.A., et al. Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc). Proc. Natl. Acad. Sci. U. S. A. 2009, 106:13427-13432.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 13427-13432
    • Sinclair, D.A.1
  • 67
    • 67650076327 scopus 로고    scopus 로고
    • Essential role of the glycosyltransferase sxc/Ogt in polycomb repression
    • Gambetta M.C., et al. Essential role of the glycosyltransferase sxc/Ogt in polycomb repression. Science 2009, 325:93-96.
    • (2009) Science , vol.325 , pp. 93-96
    • Gambetta, M.C.1
  • 68
    • 32844459336 scopus 로고    scopus 로고
    • The Polycomb group protein EZH2 directly controls DNA methylation
    • Vire E., et al. The Polycomb group protein EZH2 directly controls DNA methylation. Nature 2006, 439:871-874.
    • (2006) Nature , vol.439 , pp. 871-874
    • Vire, E.1
  • 69
    • 33846649587 scopus 로고    scopus 로고
    • Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer
    • Schlesinger Y., et al. Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer. Nat. Genet. 2007, 39:232-236.
    • (2007) Nat. Genet. , vol.39 , pp. 232-236
    • Schlesinger, Y.1
  • 70
    • 38649126918 scopus 로고    scopus 로고
    • Promoter CpG methylation contributes to ES cell gene regulation in parallel with Oct4/Nanog, PcG complex, and histone H3 K4/K27 trimethylation
    • Fouse S.D., et al. Promoter CpG methylation contributes to ES cell gene regulation in parallel with Oct4/Nanog, PcG complex, and histone H3 K4/K27 trimethylation. Cell Stem. Cell 2008, 2:160-169.
    • (2008) Cell Stem. Cell , vol.2 , pp. 160-169
    • Fouse, S.D.1
  • 71
    • 33947245128 scopus 로고    scopus 로고
    • RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3
    • Christensen J., et al. RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3. Cell 2007, 128:1063-1076.
    • (2007) Cell , vol.128 , pp. 1063-1076
    • Christensen, J.1
  • 72
    • 33847401344 scopus 로고    scopus 로고
    • The retinoblastoma binding protein RBP2 is an H3K4 demethylase
    • Klose R.J., et al. The retinoblastoma binding protein RBP2 is an H3K4 demethylase. Cell 2007, 128:889-900.
    • (2007) Cell , vol.128 , pp. 889-900
    • Klose, R.J.1
  • 73
    • 33847383585 scopus 로고    scopus 로고
    • Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein
    • Lee M.G., et al. Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein. Cell 2007, 128:877-887.
    • (2007) Cell , vol.128 , pp. 877-887
    • Lee, M.G.1
  • 74
    • 43249116995 scopus 로고    scopus 로고
    • Coordinated regulation of transcriptional repression by the RBP2 H3K4 demethylase and Polycomb-Repressive Complex 2
    • Pasini D., et al. Coordinated regulation of transcriptional repression by the RBP2 H3K4 demethylase and Polycomb-Repressive Complex 2. Genes Dev. 2008, 22:1345-1355.
    • (2008) Genes Dev. , vol.22 , pp. 1345-1355
    • Pasini, D.1
  • 75
    • 33947244845 scopus 로고    scopus 로고
    • PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation
    • Yamane K., et al. PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation. Mol. Cell 2007, 25:801-812.
    • (2007) Mol. Cell , vol.25 , pp. 801-812
    • Yamane, K.1
  • 76
    • 66449102445 scopus 로고    scopus 로고
    • The ZNF217 oncogene is a candidate organizer of repressive histone modifiers
    • Banck M.S., et al. The ZNF217 oncogene is a candidate organizer of repressive histone modifiers. Epigenetics 2009, 4:100-106.
    • (2009) Epigenetics , vol.4 , pp. 100-106
    • Banck, M.S.1
  • 77
    • 33947302685 scopus 로고    scopus 로고
    • The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases
    • Iwase S., et al. The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases. Cell 2007, 128:1077-1088.
    • (2007) Cell , vol.128 , pp. 1077-1088
    • Iwase, S.1
  • 78
    • 34249900454 scopus 로고    scopus 로고
    • The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation
    • Tahiliani M., et al. The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation. Nature 2007, 447:601-605.
    • (2007) Nature , vol.447 , pp. 601-605
    • Tahiliani, M.1
  • 79
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • Costanzi C., Pehrson J.R. Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 1998, 393:599-601.
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 80
    • 21144446865 scopus 로고    scopus 로고
    • Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase
    • Hernandez-Munoz I., et al. Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:7635-7640.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 7635-7640
    • Hernandez-Munoz, I.1
  • 81
    • 70349804469 scopus 로고    scopus 로고
    • The histone variant macroH2A is an epigenetic regulator of key developmental genes
    • Buschbeck M., et al. The histone variant macroH2A is an epigenetic regulator of key developmental genes. Nat. Struct. Mol. Biol. 2009, 16:1074-1079.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1074-1079
    • Buschbeck, M.1
  • 82
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • Czermin B., et al. Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell 2002, 111:185-196.
    • (2002) Cell , vol.111 , pp. 185-196
    • Czermin, B.1
  • 83
    • 33645231102 scopus 로고    scopus 로고
    • Mouse polycomb proteins bind differentially to methylated histone H3 and RNA and are enriched in facultative heterochromatin
    • Bernstein E., et al. Mouse polycomb proteins bind differentially to methylated histone H3 and RNA and are enriched in facultative heterochromatin. Mol. Cell Biol. 2006, 26:2560-2569.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 2560-2569
    • Bernstein, E.1
  • 84
    • 23044476138 scopus 로고    scopus 로고
    • Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer
    • Kim C.A., et al. Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer. J. Biol. Chem. 2005, 280:27769-27775.
    • (2005) J. Biol. Chem. , vol.280 , pp. 27769-27775
    • Kim, C.A.1
  • 85
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • Wang H., et al. Role of histone H2A ubiquitination in Polycomb silencing. Nature 2004, 431:873-878.
    • (2004) Nature , vol.431 , pp. 873-878
    • Wang, H.1
  • 86
    • 35148894474 scopus 로고    scopus 로고
    • A phosphorylated form of Mel-18 targets the Ring1B histone H2A ubiquitin ligase to chromatin
    • Elderkin S., et al. A phosphorylated form of Mel-18 targets the Ring1B histone H2A ubiquitin ligase to chromatin. Mol. Cell 2007, 28:107-120.
    • (2007) Mol. Cell , vol.28 , pp. 107-120
    • Elderkin, S.1
  • 87
    • 50549091334 scopus 로고    scopus 로고
    • The polycomb repressive complex 2 is a potential target of SUMO modifications
    • Riising E.M., et al. The polycomb repressive complex 2 is a potential target of SUMO modifications. PLoS One 2008, 3:e2704.
    • (2008) PLoS One , vol.3
    • Riising, E.M.1


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