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Volumn 11, Issue 12, 2013, Pages

Polycomb Protein SCML2 Regulates the Cell Cycle by Binding and Modulating CDK/CYCLIN/p21 Complexes

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE; CYCLINE; POLYCOMB GROUP PROTEIN; POLYCOMB GROUP PROTEIN SCML2B; PROTEIN P21; PROTEIN P27; UNCLASSIFIED DRUG;

EID: 84892760092     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001737     Document Type: Article
Times cited : (30)

References (71)
  • 1
    • 70349469565 scopus 로고    scopus 로고
    • Mechanisms of polycomb gene silencing: knowns and unknowns
    • Simon JA, Kingston RE, (2009) Mechanisms of polycomb gene silencing: knowns and unknowns. Nat Rev Mol Cell Biol 10: 697-708.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 697-708
    • Simon, J.A.1    Kingston, R.E.2
  • 2
    • 33845799903 scopus 로고    scopus 로고
    • Polycomb silencing mechanisms and the management of genomic programmes
    • Schwartz YB, Pirrotta V, (2007) Polycomb silencing mechanisms and the management of genomic programmes. Nat Rev Genet 8: 9-22.
    • (2007) Nat Rev Genet , vol.8 , pp. 9-22
    • Schwartz, Y.B.1    Pirrotta, V.2
  • 4
    • 54349083294 scopus 로고    scopus 로고
    • dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing
    • Lagarou A, Mohd-Sarip A, Moshkin YM, Chalkley GE, Bezstarosti K, et al. (2008) dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing. Genes Dev 22: 2799-2810.
    • (2008) Genes Dev , vol.22 , pp. 2799-2810
    • Lagarou, A.1    Mohd-Sarip, A.2    Moshkin, Y.M.3    Chalkley, G.E.4    Bezstarosti, K.5
  • 5
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, et al. (2002) Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298: 1039-1043.
    • (2002) Science , vol.298 , pp. 1039-1043
    • Cao, R.1    Wang, L.2    Wang, H.3    Xia, L.4    Erdjument-Bromage, H.5
  • 6
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein
    • Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D, (2002) Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev 16: 2893-2905.
    • (2002) Genes Dev , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 7
    • 0034785891 scopus 로고    scopus 로고
    • Reconstitution of a functional core polycomb repressive complex
    • Francis NJ, Saurin AJ, Shao Z, Kingston RE, (2001) Reconstitution of a functional core polycomb repressive complex. Mol Cell 8: 545-556.
    • (2001) Mol Cell , vol.8 , pp. 545-556
    • Francis, N.J.1    Saurin, A.J.2    Shao, Z.3    Kingston, R.E.4
  • 8
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, et al. (2004) Role of histone H2A ubiquitination in Polycomb silencing. Nature 431: 873-878.
    • (2004) Nature , vol.431 , pp. 873-878
    • Wang, H.1    Wang, L.2    Erdjument-Bromage, H.3    Vidal, M.4    Tempst, P.5
  • 9
    • 77952611697 scopus 로고    scopus 로고
    • Comparative analysis of chromatin binding by Sex Comb on Midleg (SCM) and other polycomb group repressors at a Drosophila Hox gene
    • Wang L, Jahren N, Miller EL, Ketel CS, Mallin DR, et al. (2010) Comparative analysis of chromatin binding by Sex Comb on Midleg (SCM) and other polycomb group repressors at a Drosophila Hox gene. Mol Cell Biol 30: 2584-2593.
    • (2010) Mol Cell Biol , vol.30 , pp. 2584-2593
    • Wang, L.1    Jahren, N.2    Miller, E.L.3    Ketel, C.S.4    Mallin, D.R.5
  • 10
    • 67650443962 scopus 로고    scopus 로고
    • Molecular recognition of histone lysine methylation by the Polycomb group repressor dSfmbt
    • Grimm C, Matos R, Ly-Hartig N, Steuerwald U, Lindner D, et al. (2009) Molecular recognition of histone lysine methylation by the Polycomb group repressor dSfmbt. EMBO J 28: 1965-1977.
    • (2009) EMBO J , vol.28 , pp. 1965-1977
    • Grimm, C.1    Matos, R.2    Ly-Hartig, N.3    Steuerwald, U.4    Lindner, D.5
  • 11
    • 0345306603 scopus 로고    scopus 로고
    • Crystal structure of the malignant brain tumor (MBT) repeats in Sex Comb on Midleg-like 2 (SCML2)
    • Sathyamurthy A, Allen MD, Murzin AG, Bycroft M, (2003) Crystal structure of the malignant brain tumor (MBT) repeats in Sex Comb on Midleg-like 2 (SCML2). J Biol Chem 278: 46968-46973.
    • (2003) J Biol Chem , vol.278 , pp. 46968-46973
    • Sathyamurthy, A.1    Allen, M.D.2    Murzin, A.G.3    Bycroft, M.4
  • 12
    • 0029896251 scopus 로고    scopus 로고
    • The Drosophila Polycomb group gene Sex comb on midleg (Scm) encodes a zinc finger protein with similarity to polyhomeotic protein
    • Bornemann D, Miller E, Simon J, (1996) The Drosophila Polycomb group gene Sex comb on midleg (Scm) encodes a zinc finger protein with similarity to polyhomeotic protein. Development 122: 1621-1630.
    • (1996) Development , vol.122 , pp. 1621-1630
    • Bornemann, D.1    Miller, E.2    Simon, J.3
  • 13
    • 0033538578 scopus 로고    scopus 로고
    • Stabilization of chromatin structure by PRC1, a Polycomb complex
    • Shao Z, Raible F, Mollaaghababa R, Guyon JR, Wu CT, et al. (1999) Stabilization of chromatin structure by PRC1, a Polycomb complex. Cell 98: 37-46.
    • (1999) Cell , vol.98 , pp. 37-46
    • Shao, Z.1    Raible, F.2    Mollaaghababa, R.3    Guyon, J.R.4    Wu, C.T.5
  • 14
    • 0030832045 scopus 로고    scopus 로고
    • A domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions
    • Peterson AJ, Kyba M, Bornemann D, Morgan K, Brock HW, et al. (1997) A domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions. Mol Cell Biol 17: 6683-6692.
    • (1997) Mol Cell Biol , vol.17 , pp. 6683-6692
    • Peterson, A.J.1    Kyba, M.2    Bornemann, D.3    Morgan, K.4    Brock, H.W.5
  • 15
    • 35748955512 scopus 로고    scopus 로고
    • Structural and functional analyses of methyl-lysine binding by the malignant brain tumour repeat protein Sex comb on midleg
    • Grimm C, de Ayala Alonso AG, Rybin V, Steuerwald U, Ly-Hartig N, et al. (2007) Structural and functional analyses of methyl-lysine binding by the malignant brain tumour repeat protein Sex comb on midleg. EMBO Rep 8: 1031-1037.
    • (2007) EMBO Rep , vol.8 , pp. 1031-1037
    • Grimm, C.1    de Ayala Alonso, A.G.2    Rybin, V.3    Steuerwald, U.4    Ly-Hartig, N.5
  • 16
    • 3843136318 scopus 로고    scopus 로고
    • Requirement for sex comb on midleg protein interactions in Drosophila polycomb group repression
    • Peterson AJ, Mallin DR, Francis NJ, Ketel CS, Stamm J, et al. (2004) Requirement for sex comb on midleg protein interactions in Drosophila polycomb group repression. Genetics 167: 1225-1239.
    • (2004) Genetics , vol.167 , pp. 1225-1239
    • Peterson, A.J.1    Mallin, D.R.2    Francis, N.J.3    Ketel, C.S.4    Stamm, J.5
  • 17
    • 41849100358 scopus 로고    scopus 로고
    • Beyond histone methyl-lysine binding: how malignant brain tumor (MBT) protein L3MBTL1 impacts chromatin structure
    • Trojer P, Reinberg D, (2008) Beyond histone methyl-lysine binding: how malignant brain tumor (MBT) protein L3MBTL1 impacts chromatin structure. Cell Cycle 7: 578-585.
    • (2008) Cell Cycle , vol.7 , pp. 578-585
    • Trojer, P.1    Reinberg, D.2
  • 18
    • 77049085236 scopus 로고    scopus 로고
    • MBT domain proteins in development and disease
    • Bonasio R, Lecona E, Reinberg D, (2010) MBT domain proteins in development and disease. Semin Cell Dev Biol 21: 221-230.
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 221-230
    • Bonasio, R.1    Lecona, E.2    Reinberg, D.3
  • 19
    • 0032053856 scopus 로고    scopus 로고
    • Characterization of SCML1, a new gene in Xp22, with homology to developmental polycomb genes
    • van de Vosse E, Walpole SM, Nicolaou A, van der Bent P, Cahn A, et al. (1998) Characterization of SCML1, a new gene in Xp22, with homology to developmental polycomb genes. Genomics 49: 96-102.
    • (1998) Genomics , vol.49 , pp. 96-102
    • van de Vosse, E.1    Walpole, S.M.2    Nicolaou, A.3    van der Bent, P.4    Cahn, A.5
  • 20
    • 0032839232 scopus 로고    scopus 로고
    • The human homolog of Sex comb on midleg (SCMH1) maps to chromosome 1p34
    • Berger J, Kurahashi H, Takihara Y, Shimada K, Brock HW, et al. (1999) The human homolog of Sex comb on midleg (SCMH1) maps to chromosome 1p34. Gene 237: 185-191.
    • (1999) Gene , vol.237 , pp. 185-191
    • Berger, J.1    Kurahashi, H.2    Takihara, Y.3    Shimada, K.4    Brock, H.W.5
  • 21
    • 0033563078 scopus 로고    scopus 로고
    • Identification of SCML2, a second human gene homologous to the Drosophila sex comb on midleg (Scm): a new gene cluster on Xp22
    • Montini E, Buchner G, Spalluto C, Andolfi G, Caruso A, et al. (1999) Identification of SCML2, a second human gene homologous to the Drosophila sex comb on midleg (Scm): a new gene cluster on Xp22. Genomics 58: 65-72.
    • (1999) Genomics , vol.58 , pp. 65-72
    • Montini, E.1    Buchner, G.2    Spalluto, C.3    Andolfi, G.4    Caruso, A.5
  • 22
    • 0033396834 scopus 로고    scopus 로고
    • A novel member of murine Polycomb-group proteins, Sex comb on midleg homolog protein, is highly conserved, and interacts with RAE28/mph1 in vitro
    • Tomotsune D, Takihara Y, Berger J, Duhl D, Joo S, et al. (1999) A novel member of murine Polycomb-group proteins, Sex comb on midleg homolog protein, is highly conserved, and interacts with RAE28/mph1 in vitro. Differentiation 65: 229-239.
    • (1999) Differentiation , vol.65 , pp. 229-239
    • Tomotsune, D.1    Takihara, Y.2    Berger, J.3    Duhl, D.4    Joo, S.5
  • 23
    • 0036340237 scopus 로고    scopus 로고
    • The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans
    • Levine SS, Weiss A, Erdjument-Bromage H, Shao Z, Tempst P, et al. (2002) The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans. Mol Cell Biol 22: 6070-6078.
    • (2002) Mol Cell Biol , vol.22 , pp. 6070-6078
    • Levine, S.S.1    Weiss, A.2    Erdjument-Bromage, H.3    Shao, Z.4    Tempst, P.5
  • 24
    • 33847377108 scopus 로고    scopus 로고
    • Mammalian Polycomb Scmh1 mediates exclusion of Polycomb complexes from the XY body in the pachytene spermatocytes
    • Takada Y, Isono K, Shinga J, Turner JM, Kitamura H, et al. (2007) Mammalian Polycomb Scmh1 mediates exclusion of Polycomb complexes from the XY body in the pachytene spermatocytes. Development 134: 579-590.
    • (2007) Development , vol.134 , pp. 579-590
    • Takada, Y.1    Isono, K.2    Shinga, J.3    Turner, J.M.4    Kitamura, H.5
  • 25
    • 1442305333 scopus 로고    scopus 로고
    • The cell-cycle regulator geminin inhibits Hox function through direct and polycomb-mediated interactions
    • Luo L, Yang X, Takihara Y, Knoetgen H, Kessel M, (2004) The cell-cycle regulator geminin inhibits Hox function through direct and polycomb-mediated interactions. Nature 427: 749-753.
    • (2004) Nature , vol.427 , pp. 749-753
    • Luo, L.1    Yang, X.2    Takihara, Y.3    Knoetgen, H.4    Kessel, M.5
  • 26
    • 63449115501 scopus 로고    scopus 로고
    • Multiple recurrent genetic events converge on control of histone lysine methylation in medulloblastoma
    • Northcott PA, Nakahara Y, Wu X, Feuk L, Ellison DW, et al. (2009) Multiple recurrent genetic events converge on control of histone lysine methylation in medulloblastoma. Nat Genet 41: 465-472.
    • (2009) Nat Genet , vol.41 , pp. 465-472
    • Northcott, P.A.1    Nakahara, Y.2    Wu, X.3    Feuk, L.4    Ellison, D.W.5
  • 27
    • 84869102655 scopus 로고    scopus 로고
    • The emerging role of Polycomb repressors in the response to DNA damage
    • Vissers JH, van Lohuizen M, Citterio E, (2012) The emerging role of Polycomb repressors in the response to DNA damage. J Cell Sci 125: 3939-3948.
    • (2012) J Cell Sci , vol.125 , pp. 3939-3948
    • Vissers, J.H.1    van Lohuizen, M.2    Citterio, E.3
  • 28
    • 78449243068 scopus 로고    scopus 로고
    • Epigenetic regulation of the INK4b-ARF-INK4a locus: in sickness and in health
    • Popov N, Gil J, (2010) Epigenetic regulation of the INK4b-ARF-INK4a locus: in sickness and in health. Epigenetics 5: 685-690.
    • (2010) Epigenetics , vol.5 , pp. 685-690
    • Popov, N.1    Gil, J.2
  • 29
    • 77954152739 scopus 로고    scopus 로고
    • Ubiquitylation and proteasomal degradation of the p21(Cip1), p27(Kip1) and p57(Kip2) CDK inhibitors
    • Lu Z, Hunter T, (2010) Ubiquitylation and proteasomal degradation of the p21(Cip1), p27(Kip1) and p57(Kip2) CDK inhibitors. Cell Cycle 9 (12):: 2342-2352.
    • (2010) Cell Cycle , vol.9 , Issue.12 , pp. 2342-2352
    • Lu, Z.1    Hunter, T.2
  • 30
    • 84873120891 scopus 로고    scopus 로고
    • RNF2/Ring1b negatively regulates p53 expression in selective cancer cell types to promote tumor development
    • Su WJ, Fang JS, Cheng F, Liu C, Zhou F, et al. (2013) RNF2/Ring1b negatively regulates p53 expression in selective cancer cell types to promote tumor development. Proc Natl Acad Sci U S A 110: 1720-1725.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 1720-1725
    • Su, W.J.1    Fang, J.S.2    Cheng, F.3    Liu, C.4    Zhou, F.5
  • 31
    • 84884595044 scopus 로고    scopus 로고
    • Knockdown of RNF2 induces apoptosis by regulating MDM2 and p53 stability
    • Wen W, Peng C, Kim MO, Ho Jeong C, Zhu F, et al. (2013) Knockdown of RNF2 induces apoptosis by regulating MDM2 and p53 stability. Oncogene.
    • (2013) Oncogene
    • Wen, W.1    Peng, C.2    Kim, M.O.3    Ho Jeong, C.4    Zhu, F.5
  • 32
    • 84860834822 scopus 로고    scopus 로고
    • Transcription-independent function of Polycomb Group Protein PSC in cell cycle control
    • Mohd-Sarip A, Lagarou A, Doyen CM, van der Knaap JA, Aslan U, et al. (2012) Transcription-independent function of Polycomb Group Protein PSC in cell cycle control. Science 336 (6082):: 744-747.
    • (2012) Science , vol.336 , Issue.6082 , pp. 744-747
    • Mohd-Sarip, A.1    Lagarou, A.2    Doyen, C.M.3    van der Knaap, J.A.4    Aslan, U.5
  • 34
    • 0032535375 scopus 로고    scopus 로고
    • Complete inhibition of Cdk/cyclin by one molecule of p21(Cip1)
    • Hengst L, Gopfert U, Lashuel HA, Reed SI, (1998) Complete inhibition of Cdk/cyclin by one molecule of p21(Cip1). Genes Dev 12: 3882-3888.
    • (1998) Genes Dev , vol.12 , pp. 3882-3888
    • Hengst, L.1    Gopfert, U.2    Lashuel, H.A.3    Reed, S.I.4
  • 35
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
    • Russo AA, Jeffrey PD, Patten AK, Massague J, Pavletich NP, (1996) Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 382: 325-331.
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massague, J.4    Pavletich, N.P.5
  • 37
    • 77951644400 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis
    • Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, et al. (2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal 3: ra3.
    • (2010) Sci Signal , vol.3
    • Olsen, J.V.1    Vermeulen, M.2    Santamaria, A.3    Kumar, C.4    Miller, M.L.5
  • 38
    • 44149105911 scopus 로고    scopus 로고
    • PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites
    • Gnad F, Ren S, Cox J, Olsen JV, Macek B, et al. (2007) PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites. Genome Biol 8: R250.
    • (2007) Genome Biol , vol.8
    • Gnad, F.1    Ren, S.2    Cox, J.3    Olsen, J.V.4    Macek, B.5
  • 39
    • 80053299231 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins
    • Liou YC, Zhou XZ, Lu KP, (2011) Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins. Trends Biochem Sci 36: 501-514.
    • (2011) Trends Biochem Sci , vol.36 , pp. 501-514
    • Liou, Y.C.1    Zhou, X.Z.2    Lu, K.P.3
  • 40
    • 84862131584 scopus 로고    scopus 로고
    • Retinoblastoma tumor-suppressor protein phosphorylation and inactivation depend on direct interaction with Pin1
    • Rizzolio F, Lucchetti C, Caligiuri I, Marchesi I, Caputo M, et al. (2012) Retinoblastoma tumor-suppressor protein phosphorylation and inactivation depend on direct interaction with Pin1. Cell Death Differ 19: 1152-1161.
    • (2012) Cell Death Differ , vol.19 , pp. 1152-1161
    • Rizzolio, F.1    Lucchetti, C.2    Caligiuri, I.3    Marchesi, I.4    Caputo, M.5
  • 41
    • 0028173667 scopus 로고
    • Acceleration of the G1/S phase transition by expression of cyclins D1 and E with an inducible system
    • Resnitzky D, Gossen M, Bujard H, Reed SI, (1994) Acceleration of the G1/S phase transition by expression of cyclins D1 and E with an inducible system. Mol Cell Biol 14: 1669-1679.
    • (1994) Mol Cell Biol , vol.14 , pp. 1669-1679
    • Resnitzky, D.1    Gossen, M.2    Bujard, H.3    Reed, S.I.4
  • 42
    • 0027193034 scopus 로고
    • Cyclin-dependent regulation of G1 in mammalian fibroblasts
    • Ohtsubo M, Roberts JM, (1993) Cyclin-dependent regulation of G1 in mammalian fibroblasts. Science 259: 1908-1912.
    • (1993) Science , vol.259 , pp. 1908-1912
    • Ohtsubo, M.1    Roberts, J.M.2
  • 43
    • 0027981476 scopus 로고
    • Cdk-interacting protein 1 directly binds with proliferating cell nuclear antigen and inhibits DNA replication catalyzed by the DNA polymerase delta holoenzyme
    • Flores-Rozas H, Kelman Z, Dean FB, Pan ZQ, Harper JW, et al. (1994) Cdk-interacting protein 1 directly binds with proliferating cell nuclear antigen and inhibits DNA replication catalyzed by the DNA polymerase delta holoenzyme. Proc Natl Acad Sci U S A 91: 8655-8659.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 8655-8659
    • Flores-Rozas, H.1    Kelman, Z.2    Dean, F.B.3    Pan, Z.Q.4    Harper, J.W.5
  • 44
    • 0028074603 scopus 로고
    • Differential effects by the p21 CDK inhibitor on PCNA-dependent DNA replication and repair
    • Li R, Waga S, Hannon GJ, Beach D, Stillman B, (1994) Differential effects by the p21 CDK inhibitor on PCNA-dependent DNA replication and repair. Nature 371: 534-537.
    • (1994) Nature , vol.371 , pp. 534-537
    • Li, R.1    Waga, S.2    Hannon, G.J.3    Beach, D.4    Stillman, B.5
  • 45
    • 0028180384 scopus 로고
    • Inducible acceleration of G1 progression through tetracycline-regulated expression of human cyclin E
    • Wimmel A, Lucibello FC, Sewing A, Adolph S, Muller R, (1994) Inducible acceleration of G1 progression through tetracycline-regulated expression of human cyclin E. Oncogene 9: 995-997.
    • (1994) Oncogene , vol.9 , pp. 995-997
    • Wimmel, A.1    Lucibello, F.C.2    Sewing, A.3    Adolph, S.4    Muller, R.5
  • 46
    • 78149423004 scopus 로고    scopus 로고
    • Regulation of the histone H4 monomethylase PR-Set7 by CRL4(Cdt2)-mediated PCNA-dependent degradation during DNA damage
    • Oda H, Hubner MR, Beck DB, Vermeulen M, Hurwitz J, et al. (2010) Regulation of the histone H4 monomethylase PR-Set7 by CRL4(Cdt2)-mediated PCNA-dependent degradation during DNA damage. Mol Cell 40: 364-376.
    • (2010) Mol Cell , vol.40 , pp. 364-376
    • Oda, H.1    Hubner, M.R.2    Beck, D.B.3    Vermeulen, M.4    Hurwitz, J.5
  • 47
    • 51649129472 scopus 로고    scopus 로고
    • Activation of p53 by nutlin leads to rapid differentiation of human embryonic stem cells
    • Maimets T, Neganova I, Armstrong L, Lako M, (2008) Activation of p53 by nutlin leads to rapid differentiation of human embryonic stem cells. Oncogene 27: 5277-5287.
    • (2008) Oncogene , vol.27 , pp. 5277-5287
    • Maimets, T.1    Neganova, I.2    Armstrong, L.3    Lako, M.4
  • 48
    • 33947301272 scopus 로고    scopus 로고
    • Epigenetic signatures of stem-cell identity
    • Spivakov M, Fisher AG, (2007) Epigenetic signatures of stem-cell identity. Nat Rev Genet 8: 263-271.
    • (2007) Nat Rev Genet , vol.8 , pp. 263-271
    • Spivakov, M.1    Fisher, A.G.2
  • 49
    • 33750379420 scopus 로고    scopus 로고
    • Polycomb silencers control cell fate, development and cancer
    • Sparmann A, van Lohuizen M, (2006) Polycomb silencers control cell fate, development and cancer. Nat Rev Cancer 6: 846-856.
    • (2006) Nat Rev Cancer , vol.6 , pp. 846-856
    • Sparmann, A.1    van Lohuizen, M.2
  • 50
    • 33744905801 scopus 로고    scopus 로고
    • The role of polycomb group proteins in cell cycle regulation during development
    • Martinez AM, Cavalli G, (2006) The role of polycomb group proteins in cell cycle regulation during development. Cell Cycle 5: 1189-1197.
    • (2006) Cell Cycle , vol.5 , pp. 1189-1197
    • Martinez, A.M.1    Cavalli, G.2
  • 52
    • 0033552813 scopus 로고    scopus 로고
    • The oncogene and Polycomb-group gene bmi-1 regulates cell proliferation and senescence through the ink4a locus
    • Jacobs JJ, Kieboom K, Marino S, DePinho RA, van Lohuizen M, (1999) The oncogene and Polycomb-group gene bmi-1 regulates cell proliferation and senescence through the ink4a locus. Nature 397: 164-168.
    • (1999) Nature , vol.397 , pp. 164-168
    • Jacobs, J.J.1    Kieboom, K.2    Marino, S.3    DePinho, R.A.4    van Lohuizen, M.5
  • 53
    • 33947576177 scopus 로고    scopus 로고
    • Bypass of senescence by the polycomb group protein CBX8 through direct binding to the INK4A-ARF locus
    • Dietrich N, Bracken AP, Trinh E, Schjerling CK, Koseki H, et al. (2007) Bypass of senescence by the polycomb group protein CBX8 through direct binding to the INK4A-ARF locus. EMBO J 26: 1637-1648.
    • (2007) EMBO J , vol.26 , pp. 1637-1648
    • Dietrich, N.1    Bracken, A.P.2    Trinh, E.3    Schjerling, C.K.4    Koseki, H.5
  • 54
    • 68149171468 scopus 로고    scopus 로고
    • Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus
    • doi:10.1371/journal.pone.0006380
    • Maertens GN, El Messaoudi-Aubert S, Racek T, Stock JK, Nicholls J, et al. (2009) Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus. PLoS One 4: e6380 doi:10.1371/journal.pone.0006380.
    • (2009) PLoS One , vol.4
    • Maertens, G.N.1    El Messaoudi-Aubert, S.2    Racek, T.3    Stock, J.K.4    Nicholls, J.5
  • 56
    • 0030927929 scopus 로고    scopus 로고
    • Estrogen-dependent cyclin E-cdk2 activation through p21 redistribution
    • Planas-Silva MD, Weinberg RA, (1997) Estrogen-dependent cyclin E-cdk2 activation through p21 redistribution. Mol Cell Biol 17: 4059-4069.
    • (1997) Mol Cell Biol , vol.17 , pp. 4059-4069
    • Planas-Silva, M.D.1    Weinberg, R.A.2
  • 57
    • 0032482437 scopus 로고    scopus 로고
    • Lack of relationship between CDK activity and G1 cyclin expression in breast cancer cells
    • Sweeney KJ, Swarbrick A, Sutherland RL, Musgrove EA, (1998) Lack of relationship between CDK activity and G1 cyclin expression in breast cancer cells. Oncogene 16: 2865-2878.
    • (1998) Oncogene , vol.16 , pp. 2865-2878
    • Sweeney, K.J.1    Swarbrick, A.2    Sutherland, R.L.3    Musgrove, E.A.4
  • 58
    • 81055137194 scopus 로고    scopus 로고
    • A quantitative model for cyclin-dependent kinase control of the cell cycle: revisited
    • Uhlmann F, Bouchoux C, Lopez-Aviles S, (2011) A quantitative model for cyclin-dependent kinase control of the cell cycle: revisited. Philos Trans R Soc Lond B Biol Sci 366: 3572-3583.
    • (2011) Philos Trans R Soc Lond B Biol Sci , vol.366 , pp. 3572-3583
    • Uhlmann, F.1    Bouchoux, C.2    Lopez-Aviles, S.3
  • 60
    • 79151470981 scopus 로고    scopus 로고
    • A high proliferation rate is required for cell reprogramming and maintenance of human embryonic stem cell identity
    • Ruiz S, Panopoulos AD, Herrerias A, Bissig KD, Lutz M, et al. (2011) A high proliferation rate is required for cell reprogramming and maintenance of human embryonic stem cell identity. Curr Biol 21: 45-52.
    • (2011) Curr Biol , vol.21 , pp. 45-52
    • Ruiz, S.1    Panopoulos, A.D.2    Herrerias, A.3    Bissig, K.D.4    Lutz, M.5
  • 61
    • 78649807567 scopus 로고    scopus 로고
    • Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA
    • Kaneko S, Li G, Son J, Xu CF, Margueron R, et al. (2010) Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA. Genes Dev 24: 2615-2620.
    • (2010) Genes Dev , vol.24 , pp. 2615-2620
    • Kaneko, S.1    Li, G.2    Son, J.3    Xu, C.F.4    Margueron, R.5
  • 62
    • 78650511231 scopus 로고    scopus 로고
    • CDK1-dependent phosphorylation of EZH2 suppresses methylation of H3K27 and promotes osteogenic differentiation of human mesenchymal stem cells
    • Wei Y, Chen YH, Li LY, Lang J, Yeh SP, et al. (2011) CDK1-dependent phosphorylation of EZH2 suppresses methylation of H3K27 and promotes osteogenic differentiation of human mesenchymal stem cells. Nat Cell Biol 13: 87-94.
    • (2011) Nat Cell Biol , vol.13 , pp. 87-94
    • Wei, Y.1    Chen, Y.H.2    Li, L.Y.3    Lang, J.4    Yeh, S.P.5
  • 63
    • 80051496158 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 1 (CDK1)-mediated phosphorylation of enhancer of zeste 2 (Ezh2) regulates its stability
    • Wu SC, Zhang Y, (2011) Cyclin-dependent kinase 1 (CDK1)-mediated phosphorylation of enhancer of zeste 2 (Ezh2) regulates its stability. J Biol Chem 286: 28511-28519.
    • (2011) J Biol Chem , vol.286 , pp. 28511-28519
    • Wu, S.C.1    Zhang, Y.2
  • 64
    • 78149285100 scopus 로고    scopus 로고
    • Cyclin-dependent kinases regulate epigenetic gene silencing through phosphorylation of EZH2
    • Chen S, Bohrer LR, Rai AN, Pan Y, Gan L, et al. (2010) Cyclin-dependent kinases regulate epigenetic gene silencing through phosphorylation of EZH2. Nat Cell Biol 12: 1108-1114.
    • (2010) Nat Cell Biol , vol.12 , pp. 1108-1114
    • Chen, S.1    Bohrer, L.R.2    Rai, A.N.3    Pan, Y.4    Gan, L.5
  • 65
    • 70349545897 scopus 로고    scopus 로고
    • A tumor suppressor activity of Drosophila Polycomb genes mediated by JAK-STAT signaling
    • Classen AK, Bunker BD, Harvey KF, Vaccari T, Bilder D, (2009) A tumor suppressor activity of Drosophila Polycomb genes mediated by JAK-STAT signaling. Nat Genet 41: 1150-1155.
    • (2009) Nat Genet , vol.41 , pp. 1150-1155
    • Classen, A.K.1    Bunker, B.D.2    Harvey, K.F.3    Vaccari, T.4    Bilder, D.5
  • 66
    • 70349527902 scopus 로고    scopus 로고
    • Polyhomeotic has a tumor suppressor activity mediated by repression of Notch signaling
    • Martinez AM, Schuettengruber B, Sakr S, Janic A, Gonzalez C, et al. (2009) Polyhomeotic has a tumor suppressor activity mediated by repression of Notch signaling. Nat Genet 41: 1076-1082.
    • (2009) Nat Genet , vol.41 , pp. 1076-1082
    • Martinez, A.M.1    Schuettengruber, B.2    Sakr, S.3    Janic, A.4    Gonzalez, C.5
  • 67
    • 72449192414 scopus 로고    scopus 로고
    • The novel tumor-suppressor Mel-18 in prostate cancer: its functional polymorphism, expression and clinical significance
    • Wang W, Yuasa T, Tsuchiya N, Ma Z, Maita S, et al. (2009) The novel tumor-suppressor Mel-18 in prostate cancer: its functional polymorphism, expression and clinical significance. Int J Cancer 125: 2836-2843.
    • (2009) Int J Cancer , vol.125 , pp. 2836-2843
    • Wang, W.1    Yuasa, T.2    Tsuchiya, N.3    Ma, Z.4    Maita, S.5
  • 68
    • 47349131797 scopus 로고    scopus 로고
    • Gene expression profiling of Polycomb, Hox and Meis genes in patients with acute myeloid leukaemia
    • Grubach L, Juhl-Christensen C, Rethmeier A, Olesen LH, Aggerholm A, et al. (2008) Gene expression profiling of Polycomb, Hox and Meis genes in patients with acute myeloid leukaemia. Eur J Haematol 81: 112-122.
    • (2008) Eur J Haematol , vol.81 , pp. 112-122
    • Grubach, L.1    Juhl-Christensen, C.2    Rethmeier, A.3    Olesen, L.H.4    Aggerholm, A.5
  • 70
    • 47949131755 scopus 로고    scopus 로고
    • Upregulation of annexin A1 expression by butyrate in human colon adenocarcinoma cells: role of p53, NF-Y, and p38 mitogen-activated protein kinase
    • Lecona E, Barrasa JI, Olmo N, Llorente B, Turnay J, et al. (2008) Upregulation of annexin A1 expression by butyrate in human colon adenocarcinoma cells: role of p53, NF-Y, and p38 mitogen-activated protein kinase. Mol Cell Biol 28: 4665-4674.
    • (2008) Mol Cell Biol , vol.28 , pp. 4665-4674
    • Lecona, E.1    Barrasa, J.I.2    Olmo, N.3    Llorente, B.4    Turnay, J.5
  • 71
    • 84863011309 scopus 로고    scopus 로고
    • PCGF homologs, CBX proteins, and RYBP define functionally distinct PRC1 family complexes
    • Gao Z, Zhang J, Bonasio R, Strino F, Sawai A, et al. (2012) PCGF homologs, CBX proteins, and RYBP define functionally distinct PRC1 family complexes. Mol Cell 45: 344-356.
    • (2012) Mol Cell , vol.45 , pp. 344-356
    • Gao, Z.1    Zhang, J.2    Bonasio, R.3    Strino, F.4    Sawai, A.5


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