메뉴 건너뛰기




Volumn 508, Issue 7495, 2014, Pages 263-268

ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H3; LYSINE; RNA POLYMERASE II; UNCLASSIFIED DRUG; VIRUS PROTEIN; ZMYND11 PROTEIN; CARRIER PROTEIN; COREPRESSOR PROTEIN; HISTONE; ZMYND11 PROTEIN, HUMAN;

EID: 84900312641     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13045     Document Type: Article
Times cited : (255)

References (49)
  • 1
    • 36448949026 scopus 로고    scopus 로고
    • Multivalent engagement of chromatin modifications by linked binding modules
    • Ruthenburg, A. J., Li, H., Patel, D. J. & Allis, C. D. Multivalent engagement of chromatin modifications by linked binding modules. Nature Rev. Mol. Cell Biol. 8, 983-994 (2007).
    • (2007) Nature Rev. Mol. Cell Biol. , vol.8 , pp. 983-994
    • Ruthenburg, A.J.1    Li, H.2    Patel, D.J.3    Allis, C.D.4
  • 2
    • 84866497062 scopus 로고    scopus 로고
    • Set2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes
    • Venkatesh, S. et al. Set2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes. Nature 489, 452-455 (2012).
    • (2012) Nature , vol.489 , pp. 452-455
    • Venkatesh, S.1
  • 3
    • 77952241644 scopus 로고    scopus 로고
    • New functions for an old variant: No substitute for histone H3.3
    • Elsaesser, S. J., Goldberg, A. D. & Allis, C. D. New functions for an old variant: no substitute for histone H3.3. Curr. Opin. Genet. Dev. 20, 110-117 (2010).
    • (2010) Curr. Opin. Genet. Dev. , vol.20 , pp. 110-117
    • Elsaesser, S.J.1    Goldberg, A.D.2    Allis, C.D.3
  • 4
    • 0029069219 scopus 로고
    • BS69, a novel adenovirus E1A-associated protein that inhibits E1A transactivation
    • Hateboer, G. et al. BS69, a novel adenovirus E1A-associated protein that inhibits E1A transactivation. EMBO J. 14, 3159-3169 (1995).
    • (1995) EMBO J. , vol.14 , pp. 3159-3169
    • Hateboer, G.1
  • 5
    • 0035804221 scopus 로고    scopus 로고
    • BS69, an adenovirus E1A-associated protein, in hibits the transcriptional activity of c-Myb
    • Ladendorff, N. E., Wu, S. & Lipsick, J. S. BS69, an adenovirus E1A-associated protein, in hibits the transcriptional activity of c-Myb. Oncogene 20, 125-132 (2001).
    • (2001) Oncogene , vol.20 , pp. 125-132
    • Ladendorff, N.E.1    Wu, S.2    Lipsick, J.S.3
  • 6
    • 0042807293 scopus 로고    scopus 로고
    • Ets-2 interacts with co-repressor BS69 to repress target gene expression
    • Wei, G., Schaffner, A. E., Baker, K. M., Mansky, K. C. & Ostrowski, M. C. Ets-2 interacts with co-repressor BS69 to repress target gene expression. Anticancer Res. 23, 2173-2178 (2003).
    • (2003) Anticancer Res. , vol.23 , pp. 2173-2178
    • Wei, G.1    Schaffner, A.E.2    Baker, K.M.3    Mansky, K.C.4    Ostrowski, M.C.5
  • 7
    • 77956193814 scopus 로고    scopus 로고
    • The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and guides DNA methylation
    • Dhayalan, A. et al. The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and guides DNA methylation. J. Biol. Chem. 285, 26114-26120 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 26114-26120
    • Dhayalan, A.1
  • 8
    • 77951977878 scopus 로고    scopus 로고
    • Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1
    • Vezzoli, A. et al. Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1. Nature Struct. Mol. Biol. 17, 617-619 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 617-619
    • Vezzoli, A.1
  • 9
    • 79959494918 scopus 로고    scopus 로고
    • Structural and histone binding ability characterizations of human PWWP domains
    • Wu, H. et al. Structural and histone binding ability characterizations of human PWWP domains. PLoS ONE 6, e18919 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e18919
    • Wu, H.1
  • 10
    • 0036176982 scopus 로고    scopus 로고
    • The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds
    • Qiu, C., Sawada, K., Zhang, X. & Cheng, X. The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds. Nature Struct. Biol. 9, 217-224 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 217-224
    • Qiu, C.1    Sawada, K.2    Zhang, X.3    Cheng, X.4
  • 11
    • 84874771985 scopus 로고    scopus 로고
    • Dynamic readers for 5-(hydroxy)methylcytosine and its oxidized derivatives
    • Spruijt, C. G. et al. Dynamic readers for 5-(hydroxy)methylcytosine and its oxidized derivatives. Cell 152, 1146-1159 (2013).
    • (2013) Cell , vol.152 , pp. 1146-1159
    • Spruijt, C.G.1
  • 12
    • 84876027348 scopus 로고    scopus 로고
    • Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes
    • Eidahl, J. O. et al. Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes. Nucleic Acids Res. 41, 3924-3936 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. 3924-3936
    • Eidahl, J.O.1
  • 13
    • 84878309032 scopus 로고    scopus 로고
    • Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain
    • van Nuland, R. et al. Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain. Epigenet. Chromatin 6, 12 (2013).
    • (2013) Epigenet. Chromatin , vol.6 , pp. 12
    • Van Nuland, R.1
  • 14
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., Laskowski, R. A. & Thornton, J. M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127-134 (1995).
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 15
    • 84555206210 scopus 로고    scopus 로고
    • Many keys to push: Diversifying the 'readership' of plant homeodomain fingers
    • Li, Y. & Li, H. Many keys to push: diversifying the 'readership' of plant homeodomain fingers. Acta Biochim. Biophys. Sin. 44, 28-39 (2012).
    • (2012) Acta Biochim. Biophys. Sin. , vol.44 , pp. 28-39
    • Li, Y.1    Li, H.2
  • 16
    • 34249026300 scopus 로고    scopus 로고
    • High-resolution profiling of histone methylations in the human genome
    • Barski, A. et al. High-resolution profiling of histone methylations in the human genome. Cell 129, 823-837 (2007).
    • (2007) Cell , vol.129 , pp. 823-837
    • Barski, A.1
  • 17
    • 77649099092 scopus 로고    scopus 로고
    • Distinct factors control histone variant H3.3 localization at specific genomic regions
    • Goldberg, A. D. et al. Distinct factors control histone variant H3.3 localization at specific genomic regions. Cell 140, 678-691 (2010).
    • (2010) Cell , vol.140 , pp. 678-691
    • Goldberg, A.D.1
  • 18
    • 68149150830 scopus 로고    scopus 로고
    • H3.3/H2A.Z double variant-containing nucleosomes mark 'nucleosome-free regions' of active promoters and other regulatory regions
    • Jin, C. et al. H3.3/H2A.Z double variant-containing nucleosomes mark 'nucleosome-free regions' of active promoters and other regulatory regions. Nature Genet. 41, 941-945 (2009).
    • (2009) Nature Genet. , vol.41 , pp. 941-945
    • Jin, C.1
  • 19
    • 84255162049 scopus 로고    scopus 로고
    • Dynamics of histone H3 deposition in vivo reveal a nucleosome gap-filling mechanism for H3.3 to maintain chromatin integrity
    • Ray-Gallet, D. et al. Dynamics of histone H3 deposition in vivo reveal a nucleosome gap-filling mechanism for H3.3 to maintain chromatin integrity. Mol. Cell 44, 928-941 (2011).
    • (2011) Mol. Cell , vol.44 , pp. 928-941
    • Ray-Gallet, D.1
  • 20
    • 38549139593 scopus 로고    scopus 로고
    • Dynamic histone H3methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation
    • Edmunds, J. W., Mahadevan, L. C. & Clayton, A. L. Dynamic histone H3methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation. EMBO J. 27, 406-420 (2008).
    • (2008) EMBO J. , vol.27 , pp. 406-420
    • Edmunds, J.W.1    Mahadevan, L.C.2    Clayton, A.L.3
  • 21
    • 81355133161 scopus 로고    scopus 로고
    • NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming
    • Kuo, A. J. et al. NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming. Mol. Cell 44, 609-620 (2011).
    • (2011) Mol. Cell , vol.44 , pp. 609-620
    • Kuo, A.J.1
  • 22
    • 77951920690 scopus 로고    scopus 로고
    • C-Myc regulates transcriptional pause release
    • Rahl, P. B. et al. c-Myc regulates transcriptional pause release. Cell 141, 432-445 (2010).
    • (2010) Cell , vol.141 , pp. 432-445
    • Rahl, P.B.1
  • 23
    • 84876842759 scopus 로고    scopus 로고
    • Signaling pathways differentially affect RNA polymerase II initiation, pausing, and elongation rate in cells
    • Danko, C. G. et al. Signaling pathways differentially affect RNA polymerase II initiation, pausing, and elongation rate in cells. Mol. Cell 50, 212-222 (2013).
    • (2013) Mol. Cell , vol.50 , pp. 212-222
    • Danko, C.G.1
  • 24
    • 5444225805 scopus 로고    scopus 로고
    • Elongation by RNA polymerase II: The short and long of it
    • Sims, R. J., III, Belotserkovskaya, R. & Reinberg, D. Elongation by RNA polymerase II: the short and long of it. Genes Dev. 18, 2437-2468 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 2437-2468
    • Sims, R.J.1    Belotserkovskaya, R.2    Reinberg, D.3
  • 25
    • 0141796267 scopus 로고    scopus 로고
    • BS69 and RACK7, a potential novel class of tumor suppressor genes
    • Ansieau, S. & Sergeant, A. BS69 and RACK7, a potential novel class of tumor suppressor genes. Pathol. Biol. (Paris) 51, 397-399 (2003).
    • (2003) Pathol. Biol. (Paris) , vol.51 , pp. 397-399
    • Ansieau, S.1    Sergeant, A.2
  • 26
    • 84862777348 scopus 로고    scopus 로고
    • Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma
    • Schwartzentruber, J. et al. Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma. Nature 482, 226-231 (2012).
    • (2012) Nature , vol.482 , pp. 226-231
    • Schwartzentruber, J.1
  • 27
    • 84867606428 scopus 로고    scopus 로고
    • Hotspot mutations in H3F3A and IDH1 define distinct epigenetic and biological subgroups of glioblastoma
    • Sturm, D. et al. Hotspot mutations in H3F3A and IDH1 define distinct epigenetic and biological subgroups of glioblastoma. Cancer Cell 22, 425-437 (2012).
    • (2012) Cancer Cell , vol.22 , pp. 425-437
    • Sturm, D.1
  • 28
    • 84877785024 scopus 로고    scopus 로고
    • Inhibition of PRC2 activity by a gain-of-function H3 mutation found in pediatric glioblastoma
    • Lewis, P. W. et al. Inhibition of PRC2 activity by a gain-of-function H3 mutation found in pediatric glioblastoma. Science 340, 857-861 (2013).
    • (2013) Science , vol.340 , pp. 857-861
    • Lewis, P.W.1
  • 29
    • 84877621282 scopus 로고    scopus 로고
    • Histone H3.3 mutations drive pediatric glioblastoma through upregulation of MYCN
    • Bjerke, L. et al. Histone H3.3 mutations drive pediatric glioblastoma through upregulation of MYCN. Cancer Discov. 3, 512-519 (2013).
    • (2013) Cancer Discov. , vol.3 , pp. 512-519
    • Bjerke, L.1
  • 30
    • 79151483638 scopus 로고    scopus 로고
    • An online survival analysis tool to rapidly assess the effect of 22,277 genes on breast cancer prognosis using microarray data of 1,809 patients
    • Gyorffy, B. et al. An online survival analysis tool to rapidly assess the effect of 22,277 genes on breast cancer prognosis using microarray data of 1,809 patients. Breast Cancer Res. Treat. 123, 725-731 (2010).
    • (2010) Breast Cancer Res. Treat. , vol.123 , pp. 725-731
    • Gyorffy, B.1
  • 31
    • 33745868054 scopus 로고    scopus 로고
    • ING2PHDdomain links histone H3 lysine 4 methylation to active gene repression
    • Shi, X. et al. ING2PHDdomain links histone H3 lysine 4 methylation to active gene repression. Nature 442, 96-99 (2006).
    • (2006) Nature , vol.442 , pp. 96-99
    • Shi, X.1
  • 32
    • 77951240318 scopus 로고    scopus 로고
    • Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation
    • Wen, H. et al. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation. J. Biol. Chem. 285, 9322-9326 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 9322-9326
    • Wen, H.1
  • 33
    • 84870046749 scopus 로고    scopus 로고
    • Identification of a chemical probe for BET bromodomain inhibition through optimization of a fragment-derived hit
    • Fish, P. et al. Identification of a chemical probe for BET bromodomain inhibition through optimization of a fragment-derived hit. J. Med. Chem. 55, 9831-9837 (2012).
    • (2012) J. Med. Chem. , vol.55 , pp. 9831-9837
    • Fish, P.1
  • 34
    • 0033756308 scopus 로고    scopus 로고
    • Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle: Assembly of prereplication complexes in late mitosis
    • Mendez, J. & Stillman, B. Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle: assembly of prereplication complexes in late mitosis. Mol. Cell. Biol. 20, 8602-8612 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8602-8612
    • Mendez, J.1    Stillman, B.2
  • 35
    • 34249099730 scopus 로고    scopus 로고
    • Combined action of PHD and chromo domains directs the Rpd3SHDAC to transcribed chromatin
    • Li, B. et al. Combined action of PHD and chromo domains directs the Rpd3SHDAC to transcribed chromatin. Science 316, 1050-1054 (2007).
    • (2007) Science , vol.316 , pp. 1050-1054
    • Li, B.1
  • 36
    • 33847386172 scopus 로고    scopus 로고
    • The site-specific installation of methyl-lysine analogs into recombinant histones
    • Simon, M. D. et al. The site-specific installation of methyl-lysine analogs into recombinant histones. Cell 128, 1003-1012 (2007).
    • (2007) Cell , vol.128 , pp. 1003-1012
    • Simon, M.D.1
  • 37
    • 36549013619 scopus 로고    scopus 로고
    • RNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryo
    • Zeitlinger, J. et al. RNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryo. Nature Genet. 39, 1512-1516 (2007).
    • (2007) Nature Genet. , vol.39 , pp. 1512-1516
    • Zeitlinger, J.1
  • 38
    • 67749106610 scopus 로고    scopus 로고
    • Synchronous and stochastic patterns of gene activation in the Drosophila embryo
    • Boettiger, A. N. & Levine, M. Synchronous and stochastic patterns of gene activation in the Drosophila embryo. Science 325, 471-473 (2009).
    • (2009) Science , vol.325 , pp. 471-473
    • Boettiger, A.N.1    Levine, M.2
  • 39
    • 45849129033 scopus 로고    scopus 로고
    • Promoter-proximal Pol II: When stalling speeds things up
    • Nechaev, S. & Adelman, K. Promoter-proximal Pol II: when stalling speeds things up. Cell Cycle 7, 1539-1544 (2008).
    • (2008) Cell Cycle , vol.7 , pp. 1539-1544
    • Nechaev, S.1    Adelman, K.2
  • 40
  • 41
    • 84865419994 scopus 로고    scopus 로고
    • The super elongation complex (SEC) family in transcriptional control
    • Luo, Z., Lin, C. & Shilatifard, A. The super elongation complex (SEC) family in transcriptional control. Nature Rev. Mol. Cell Biol. 13, 543-547 (2012).
    • (2012) Nature Rev. Mol. Cell Biol. , vol.13 , pp. 543-547
    • Luo, Z.1    Lin, C.2    Shilatifard, A.3
  • 42
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: Can low affinity systems be studied by isothermal titration calorimetry?
    • Turnbull, W. B. & Daranas, A. H. On the value of c: can low affinity systems be studied by isothermal titration calorimetry? J. Am. Chem. Soc. 125, 14859-14866 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 43
    • 0032512794 scopus 로고    scopus 로고
    • New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning
    • Lowary, P. T. & Widom, J. New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning. J. Mol. Biol. 276, 19-42 (1998).
    • (1998) J. Mol. Biol. , vol.276 , pp. 19-42
    • Lowary, P.T.1    Widom, J.2
  • 44
    • 84928761705 scopus 로고    scopus 로고
    • Preparation of nuclear and cytoplasmic extracts from mammalian cells
    • Abmayr, S. M., Yao, T., Parmely, T. & Workman, J. L. Preparation of nuclear and cytoplasmic extracts from mammalian cells. Curr. Protoc. Mol. Biol. 12.11, (2006).
    • (2006) Curr. Protoc. Mol. Biol. , vol.12 , Issue.11
    • Abmayr, S.M.1    Yao, T.2    Parmely, T.3    Workman, J.L.4
  • 45
    • 53849146020 scopus 로고    scopus 로고
    • Model-based analysis of ChIP-Seq (MACS)
    • Zhang, Y. et al. Model-based analysis of ChIP-Seq (MACS). Genome Biol. 9, R137 (2008).
    • (2008) Genome Biol. , vol.9 , pp. R137
    • Zhang, Y.1
  • 46
    • 73949158814 scopus 로고    scopus 로고
    • Structure and functional characterization of the atypical human kinase haspin
    • Eswaran, J. et al. Structure and functional characterization of the atypical human kinase haspin. Proc. Natl Acad. Sci. USA 106, 20198-20203 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 20198-20203
    • Eswaran, J.1
  • 47
    • 70350052791 scopus 로고    scopus 로고
    • Synthesis, kinase inhibitory potencies, and in vitro antiproliferative evaluation of new Pim kinase inhibitors
    • Akue-Gedu, R. et al. Synthesis, kinase inhibitory potencies, and in vitro antiproliferative evaluation of new Pim kinase inhibitors. J. Med. Chem. 52, 6369-6381 (2009).
    • (2009) J. Med. Chem. , vol.52 , pp. 6369-6381
    • Akue-Gedu, R.1
  • 48
    • 58249138122 scopus 로고    scopus 로고
    • Large-scale structural analysis of the classical human protein tyrosine phosphatome
    • Barr, A. J. et al. Large-scale structural analysis of the classical human protein tyrosine phosphatome. Cell 136, 352-363 (2009).
    • (2009) Cell , vol.136 , pp. 352-363
    • Barr, A.J.1
  • 49
    • 84856069665 scopus 로고    scopus 로고
    • A SUMOylation-dependent transcriptional subprogram is required for Myc-driven tumorigenesis
    • Kessler, J. D. et al. A SUMOylation-dependent transcriptional subprogram is required for Myc-driven tumorigenesis. Science 335, 348-353 (2012).
    • (2012) Science , vol.335 , pp. 348-353
    • Kessler, J.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.