메뉴 건너뛰기




Volumn 1846, Issue 2, 2014, Pages 366-379

Role of somatic cancer mutations in human protein lysine methyltransferases

Author keywords

Enzyme mechanism; Histone methylation; Lysine methylation; Protein lysine methyltransferase; Somatic cancer mutations

Indexed keywords

CELL PROTEIN; DOT1L PROTEIN; HISTONE H3; METHYLTRANSFERASE; MIXED LINEAGE LEUKEMIA PROTEIN; MLL1 PROTEIN; MLL4 PROTEIN; NSD PROTEIN; PROTEIN LYSINE METHYLTRANSFERASES; SETD2 PROTEIN; SMYD PROTEIN; TRANSCRIPTION FACTOR EZH2; UNCLASSIFIED DRUG; EZH2 PROTEIN, HUMAN; HISTONE LYSINE METHYLTRANSFERASE; POLYCOMB REPRESSIVE COMPLEX 2; SET2 PROTEIN, HUMAN;

EID: 84907646535     PISSN: 0304419X     EISSN: 18792561     Source Type: Journal    
DOI: 10.1016/j.bbcan.2014.08.002     Document Type: Review
Times cited : (42)

References (147)
  • 1
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 2007, 128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 2
    • 77949678340 scopus 로고    scopus 로고
    • Chromatin structure and the inheritance of epigenetic information
    • Margueron R., Reinberg D. Chromatin structure and the inheritance of epigenetic information. Nat. Rev. Genet. 2010, 11:285-296.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 285-296
    • Margueron, R.1    Reinberg, D.2
  • 3
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister A.J., Kouzarides T. Regulation of chromatin by histone modifications. Cell Res. 2011, 21:381-395.
    • (2011) Cell Res. , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 5
    • 78751470921 scopus 로고    scopus 로고
    • Structure and function of mammalian DNA methyltransferases
    • Jurkowska R.Z., Jurkowski T.P., Jeltsch A. Structure and function of mammalian DNA methyltransferases. Chembiochem 2011, 12:206-222.
    • (2011) Chembiochem , vol.12 , pp. 206-222
    • Jurkowska, R.Z.1    Jurkowski, T.P.2    Jeltsch, A.3
  • 7
    • 84863621527 scopus 로고    scopus 로고
    • Cancer epigenetics: from mechanism to therapy
    • Dawson M.A., Kouzarides T. Cancer epigenetics: from mechanism to therapy. Cell 2012, 150:12-27.
    • (2012) Cell , vol.150 , pp. 12-27
    • Dawson, M.A.1    Kouzarides, T.2
  • 8
    • 77953995002 scopus 로고    scopus 로고
    • Covalent histone modifications-miswritten, misinterpreted and mis-erased in human cancers
    • Chi P., Allis C.D., Wang G.G. Covalent histone modifications-miswritten, misinterpreted and mis-erased in human cancers. Nat. Rev. Cancer 2010, 10:457-469.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 457-469
    • Chi, P.1    Allis, C.D.2    Wang, G.G.3
  • 9
    • 78049402859 scopus 로고    scopus 로고
    • Molecular signals of epigenetic states
    • Bonasio R., Tu S., Reinberg D. Molecular signals of epigenetic states. Science 2010, 330:612-616.
    • (2010) Science , vol.330 , pp. 612-616
    • Bonasio, R.1    Tu, S.2    Reinberg, D.3
  • 10
    • 84904541089 scopus 로고    scopus 로고
    • Interpreting the language of histone and DNA modifications
    • Rothbart S.B., Strahl B.D. Interpreting the language of histone and DNA modifications. Biochim. Biophys. Acta 2014, 1839:627-643.
    • (2014) Biochim. Biophys. Acta , vol.1839 , pp. 627-643
    • Rothbart, S.B.1    Strahl, B.D.2
  • 11
    • 20544461679 scopus 로고    scopus 로고
    • Structural and sequence motifs of protein (histone) methylation enzymes
    • Cheng X., Collins R.E., Zhang X. Structural and sequence motifs of protein (histone) methylation enzymes. Annu. Rev. Biophys. Biomol. Struct. 2005, 34:267-294.
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 267-294
    • Cheng, X.1    Collins, R.E.2    Zhang, X.3
  • 12
    • 84914106331 scopus 로고    scopus 로고
    • Molecular basis for substrate recognition by lysine methyltransferases and demethylases
    • (in press)
    • Del Rizzo P.A., Trievel R.C. Molecular basis for substrate recognition by lysine methyltransferases and demethylases. Biochim. Biophys. Acta 2014, (in press).
    • (2014) Biochim. Biophys. Acta
    • Del Rizzo, P.A.1    Trievel, R.C.2
  • 13
    • 58049191558 scopus 로고    scopus 로고
    • Chromatin signatures in multipotent human hematopoietic stem cells indicate the fate of bivalent genes during differentiation
    • Cui K., Zang C., Roh T.Y., Schones D.E., Childs R.W., Peng W., Zhao K. Chromatin signatures in multipotent human hematopoietic stem cells indicate the fate of bivalent genes during differentiation. Cell Stem Cell 2009, 4:80-93.
    • (2009) Cell Stem Cell , vol.4 , pp. 80-93
    • Cui, K.1    Zang, C.2    Roh, T.Y.3    Schones, D.E.4    Childs, R.W.5    Peng, W.6    Zhao, K.7
  • 14
    • 84879260661 scopus 로고    scopus 로고
    • A double take on bivalent promoters
    • Voigt P., Tee W.W., Reinberg D. A double take on bivalent promoters. Genes Dev. 2013, 27:1318-1338.
    • (2013) Genes Dev. , vol.27 , pp. 1318-1338
    • Voigt, P.1    Tee, W.W.2    Reinberg, D.3
  • 15
    • 33947513027 scopus 로고    scopus 로고
    • Regulation of histone methylation by demethylimination and demethylation
    • Klose R.J., Zhang Y. Regulation of histone methylation by demethylimination and demethylation. Nat. Rev. Mol. Cell Biol. 2007, 8:307-318.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 307-318
    • Klose, R.J.1    Zhang, Y.2
  • 16
    • 84888090995 scopus 로고    scopus 로고
    • Histone lysine-specific methyltransferases and demethylases in carcinogenesis: new targets for cancer therapy and prevention
    • Tian X., Zhang S., Liu H.M., Zhang Y.B., Blair C.A., Mercola D., Sassone-Corsi P., Zi X. Histone lysine-specific methyltransferases and demethylases in carcinogenesis: new targets for cancer therapy and prevention. Curr. Cancer Drug Targets 2013, 13:558-579.
    • (2013) Curr. Cancer Drug Targets , vol.13 , pp. 558-579
    • Tian, X.1    Zhang, S.2    Liu, H.M.3    Zhang, Y.B.4    Blair, C.A.5    Mercola, D.6    Sassone-Corsi, P.7    Zi, X.8
  • 19
    • 80053144962 scopus 로고    scopus 로고
    • A decade of exploring the cancer epigenome - biological and translational implications
    • Baylin S.B., Jones P.A. A decade of exploring the cancer epigenome - biological and translational implications. Nat. Rev. Cancer 2011, 11:726-734.
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 726-734
    • Baylin, S.B.1    Jones, P.A.2
  • 20
    • 84875537133 scopus 로고    scopus 로고
    • Epigenetic reprogramming in cancer
    • Suva M.L., Riggi N., Bernstein B.E. Epigenetic reprogramming in cancer. Science 2013, 339:1567-1570.
    • (2013) Science , vol.339 , pp. 1567-1570
    • Suva, M.L.1    Riggi, N.2    Bernstein, B.E.3
  • 21
    • 84875129831 scopus 로고    scopus 로고
    • DNA methylation dynamics in health and disease
    • Bergman Y., Cedar H. DNA methylation dynamics in health and disease. Nat. Struct. Mol. Biol. 2013, 20:274-281.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 274-281
    • Bergman, Y.1    Cedar, H.2
  • 24
    • 84859893371 scopus 로고    scopus 로고
    • Histone methylation: a dynamic mark in health, disease and inheritance
    • Greer E.L., Shi Y. Histone methylation: a dynamic mark in health, disease and inheritance. Nat. Rev. Genet. 2012, 13:343-357.
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 343-357
    • Greer, E.L.1    Shi, Y.2
  • 25
    • 33644856123 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer: past, present and future
    • Yoo C.B., Jones P.A. Epigenetic therapy of cancer: past, present and future. Nat. Rev. Drug. Discov. 2006, 5:37-50.
    • (2006) Nat. Rev. Drug. Discov. , vol.5 , pp. 37-50
    • Yoo, C.B.1    Jones, P.A.2
  • 26
    • 84893437787 scopus 로고    scopus 로고
    • A DNMT3A mutation common in AML exhibits dominant-negative effects in murine ES cells
    • Kim S.J., Zhao H., Hardikar S., Singh A.K., Goodell M.A., Chen T. A DNMT3A mutation common in AML exhibits dominant-negative effects in murine ES cells. Blood 2013, 122:4086-4089.
    • (2013) Blood , vol.122 , pp. 4086-4089
    • Kim, S.J.1    Zhao, H.2    Hardikar, S.3    Singh, A.K.4    Goodell, M.A.5    Chen, T.6
  • 29
    • 70149103800 scopus 로고    scopus 로고
    • Mutation in TET2 in myeloid cancers
    • (author reply 1117-1118.)
    • Tefferi A., Lim K.H., Levine R. Mutation in TET2 in myeloid cancers. N. Engl. J. Med. 2009, 361:1117. (author reply 1117-1118.).
    • (2009) N. Engl. J. Med. , vol.361 , pp. 1117
    • Tefferi, A.1    Lim, K.H.2    Levine, R.3
  • 30
    • 84891159388 scopus 로고    scopus 로고
    • Role of DNMT3A, TET2, and IDH1/2 mutations in pre-leukemic stem cells in acute myeloid leukemia
    • Chan S.M., Majeti R. Role of DNMT3A, TET2, and IDH1/2 mutations in pre-leukemic stem cells in acute myeloid leukemia. Int. J. Hematol. 2013, 98:648-657.
    • (2013) Int. J. Hematol. , vol.98 , pp. 648-657
    • Chan, S.M.1    Majeti, R.2
  • 33
    • 77956189495 scopus 로고    scopus 로고
    • Role of TET proteins in 5mC to 5hmC conversion ES-cell self-renewal and inner cell mass specification
    • Ito S., D'Alessio A.C., Taranova O.V., Hong K., Sowers L.C., Zhang Y. Role of TET proteins in 5mC to 5hmC conversion ES-cell self-renewal and inner cell mass specification. Nature 2010, 466:1129-1133.
    • (2010) Nature , vol.466 , pp. 1129-1133
    • Ito, S.1    D'Alessio, A.C.2    Taranova, O.V.3    Hong, K.4    Sowers, L.C.5    Zhang, Y.6
  • 37
    • 84904762312 scopus 로고    scopus 로고
    • A rationale to target the SWI/SNF complex for cancer therapy
    • Hohmann A.F., Vakoc C.R. A rationale to target the SWI/SNF complex for cancer therapy. Trends Genet. 2014, 30:356-363.
    • (2014) Trends Genet. , vol.30 , pp. 356-363
    • Hohmann, A.F.1    Vakoc, C.R.2
  • 39
    • 79251590753 scopus 로고    scopus 로고
    • Specificity analysis-based identification of new methylation targets of the SET7/9 protein lysine methyltransferase
    • Dhayalan A., Kudithipudi S., Rathert P., Jeltsch A. Specificity analysis-based identification of new methylation targets of the SET7/9 protein lysine methyltransferase. Chem. Biol. 2011, 18:111-120.
    • (2011) Chem. Biol. , vol.18 , pp. 111-120
    • Dhayalan, A.1    Kudithipudi, S.2    Rathert, P.3    Jeltsch, A.4
  • 40
    • 84876735200 scopus 로고    scopus 로고
    • Protein methylation at the surface and buried deep: thinking outside the histone box
    • Clarke S.G. Protein methylation at the surface and buried deep: thinking outside the histone box. Trends Biochem. Sci. 2013, 38:243-252.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 243-252
    • Clarke, S.G.1
  • 42
    • 84914176196 scopus 로고    scopus 로고
    • An unexpected journey: lysine methylation across the proteome
    • (in press)
    • Moore K.E., Gozani O. An unexpected journey: lysine methylation across the proteome. Biochim. Biophys. Acta 2014, (in press).
    • (2014) Biochim. Biophys. Acta
    • Moore, K.E.1    Gozani, O.2
  • 43
    • 33748419671 scopus 로고    scopus 로고
    • Polycomb response elements and targeting of Polycomb group proteins in Drosophila
    • 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) Curr. Opin. Genet. Dev. , vol.16 , pp. 476-484
    • Muller, J.1    Kassis, J.A.2
  • 44
    • 78751662908 scopus 로고    scopus 로고
    • The Polycomb complex PRC2 and its mark in life
    • Margueron R., Reinberg D. The Polycomb complex PRC2 and its mark in life. Nature 2011, 469:343-349.
    • (2011) Nature , vol.469 , pp. 343-349
    • Margueron, R.1    Reinberg, D.2
  • 45
    • 1942503942 scopus 로고    scopus 로고
    • The functions of E(Z)/EZH2-mediated methylation of lysine 27 in histone H3
    • Cao R., Zhang Y. The functions of E(Z)/EZH2-mediated methylation of lysine 27 in histone H3. Curr. Opin. Genet. Dev. 2004, 14:155-164.
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 155-164
    • Cao, R.1    Zhang, Y.2
  • 47
    • 55949136562 scopus 로고    scopus 로고
    • Roles of the EZH2 histone methyltransferase in cancer epigenetics
    • Simon J.A., Lange C.A. Roles of the EZH2 histone methyltransferase in cancer epigenetics. Mutat. Res. 2008, 647:21-29.
    • (2008) Mutat. Res. , vol.647 , pp. 21-29
    • Simon, J.A.1    Lange, C.A.2
  • 54
    • 78650454078 scopus 로고    scopus 로고
    • Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas
    • Sneeringer C.J., Scott M.P., Kuntz K.W., Knutson S.K., Pollock R.M., Richon V.M., Copeland R.A. Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:20980-20985.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 20980-20985
    • Sneeringer, C.J.1    Scott, M.P.2    Kuntz, K.W.3    Knutson, S.K.4    Pollock, R.M.5    Richon, V.M.6    Copeland, R.A.7
  • 55
  • 60
    • 63849175327 scopus 로고    scopus 로고
    • MLL histone methylases in gene expression, hormone signaling and cell cycle
    • Ansari K.I., Mishra B.P., Mandal S.S. MLL histone methylases in gene expression, hormone signaling and cell cycle. Front. Biosci. (Landmark Ed) 2009, 14:3483-3495.
    • (2009) Front. Biosci. (Landmark Ed) , vol.14 , pp. 3483-3495
    • Ansari, K.I.1    Mishra, B.P.2    Mandal, S.S.3
  • 61
    • 84874018873 scopus 로고    scopus 로고
    • Skirting the pitfalls: a clear-cut nomenclature for H3K4 methyltransferases
    • Bogershausen N., Bruford E., Wollnik B. Skirting the pitfalls: a clear-cut nomenclature for H3K4 methyltransferases. Clin. Genet. 2013, 83:212-214.
    • (2013) Clin. Genet. , vol.83 , pp. 212-214
    • Bogershausen, N.1    Bruford, E.2    Wollnik, B.3
  • 62
    • 84896374738 scopus 로고    scopus 로고
    • A role for H3K4 monomethylation in gene repression and partitioning of chromatin readers
    • Cheng J., Blum R., Bowman C., Hu D., Shilatifard A., Shen S., Dynlacht B.D. A role for H3K4 monomethylation in gene repression and partitioning of chromatin readers. Mol. Cell 2014, 53:979-992.
    • (2014) Mol. Cell , vol.53 , pp. 979-992
    • Cheng, J.1    Blum, R.2    Bowman, C.3    Hu, D.4    Shilatifard, A.5    Shen, S.6    Dynlacht, B.D.7
  • 64
    • 58649110597 scopus 로고    scopus 로고
    • Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks
    • Southall S.M., Wong P.S., Odho Z., Roe S.M., Wilson J.R. Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks. Mol. Cell 2009, 33:181-191.
    • (2009) Mol. Cell , vol.33 , pp. 181-191
    • Southall, S.M.1    Wong, P.S.2    Odho, Z.3    Roe, S.M.4    Wilson, J.R.5
  • 65
    • 71949107301 scopus 로고    scopus 로고
    • Global analysis of H3K4 methylation defines MLL family member targets and points to a role for MLL1-mediated H3K4 methylation in the regulation of transcriptional initiation by RNA polymerase II
    • Wang P., Lin C., Smith E.R., Guo H., Sanderson B.W., Wu M., Gogol M., Alexander T., Seidel C., Wiedemann L.M., Ge K., Krumlauf R., Shilatifard A. Global analysis of H3K4 methylation defines MLL family member targets and points to a role for MLL1-mediated H3K4 methylation in the regulation of transcriptional initiation by RNA polymerase II. Mol. Cell. Biol. 2009, 29:6074-6085.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 6074-6085
    • Wang, P.1    Lin, C.2    Smith, E.R.3    Guo, H.4    Sanderson, B.W.5    Wu, M.6    Gogol, M.7    Alexander, T.8    Seidel, C.9    Wiedemann, L.M.10    Ge, K.11    Krumlauf, R.12    Shilatifard, A.13
  • 66
    • 17044413548 scopus 로고    scopus 로고
    • The versatile mixed lineage leukaemia gene MLL and its many associations in leukaemogenesis
    • Daser A., Rabbitts T.H. The versatile mixed lineage leukaemia gene MLL and its many associations in leukaemogenesis. Semin. Cancer Biol. 2005, 15:175-188.
    • (2005) Semin. Cancer Biol. , vol.15 , pp. 175-188
    • Daser, A.1    Rabbitts, T.H.2
  • 67
    • 35548934558 scopus 로고    scopus 로고
    • MLL translocations, histone modifications and leukaemia stem-cell development
    • Krivtsov A.V., Armstrong S.A. MLL translocations, histone modifications and leukaemia stem-cell development. Nat. Rev. Cancer 2007, 7:823-833.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 823-833
    • Krivtsov, A.V.1    Armstrong, S.A.2
  • 68
    • 84889240753 scopus 로고    scopus 로고
    • A medicinal chemistry perspective for targeting histone H3 lysine-79 methyltransferase DOT1L
    • Anglin J.L., Song Y. A medicinal chemistry perspective for targeting histone H3 lysine-79 methyltransferase DOT1L. J. Med. Chem. 2013, 56:8972-8983.
    • (2013) J. Med. Chem. , vol.56 , pp. 8972-8983
    • Anglin, J.L.1    Song, Y.2
  • 69
    • 84856916060 scopus 로고    scopus 로고
    • The pathogenesis of mixed-lineage leukemia
    • Muntean A.G., Hess J.L. The pathogenesis of mixed-lineage leukemia. Annu. Rev. Pathol. 2012, 7:283-301.
    • (2012) Annu. Rev. Pathol. , vol.7 , pp. 283-301
    • Muntean, A.G.1    Hess, J.L.2
  • 70
    • 84880283763 scopus 로고    scopus 로고
    • Histone methylase MLL1 has critical roles in tumor growth and angiogenesis and its knockdown suppresses tumor growth in vivo
    • Ansari K.I., Kasiri S., Mandal S.S. Histone methylase MLL1 has critical roles in tumor growth and angiogenesis and its knockdown suppresses tumor growth in vivo. Oncogene 2013, 32:3359-3370.
    • (2013) Oncogene , vol.32 , pp. 3359-3370
    • Ansari, K.I.1    Kasiri, S.2    Mandal, S.S.3
  • 71
    • 0037028488 scopus 로고    scopus 로고
    • MLL3, a new human member of the TRX/MLL gene family, maps to 7q36, a chromosome region frequently deleted in myeloid leukaemia
    • Ruault M., Brun M.E., Ventura M., Roizes G., De Sario A. MLL3, a new human member of the TRX/MLL gene family, maps to 7q36, a chromosome region frequently deleted in myeloid leukaemia. Gene 2002, 284:73-81.
    • (2002) Gene , vol.284 , pp. 73-81
    • Ruault, M.1    Brun, M.E.2    Ventura, M.3    Roizes, G.4    De Sario, A.5
  • 72
    • 66649120472 scopus 로고    scopus 로고
    • A tumor suppressive coactivator complex of p53 containing ASC-2 and histone H3-lysine-4 methyltransferase MLL3 or its paralogue MLL4
    • Lee J., Kim D.H., Lee S., Yang Q.H., Lee D.K., Lee S.K., Roeder R.G., Lee J.W. A tumor suppressive coactivator complex of p53 containing ASC-2 and histone H3-lysine-4 methyltransferase MLL3 or its paralogue MLL4. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:8513-8518.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8513-8518
    • Lee, J.1    Kim, D.H.2    Lee, S.3    Yang, Q.H.4    Lee, D.K.5    Lee, S.K.6    Roeder, R.G.7    Lee, J.W.8
  • 73
    • 80051665475 scopus 로고    scopus 로고
    • Somatic mutations of the mixed-lineage leukemia 3 (MLL3) gene in primary breast cancers
    • Wang X.X., Fu L., Li X., Wu X., Zhu Z., Fu L., Dong J.T. Somatic mutations of the mixed-lineage leukemia 3 (MLL3) gene in primary breast cancers. Pathol. Oncol. Res. 2011, 17:429-433.
    • (2011) Pathol. Oncol. Res. , vol.17 , pp. 429-433
    • Wang, X.X.1    Fu, L.2    Li, X.3    Wu, X.4    Zhu, Z.5    Fu, L.6    Dong, J.T.7
  • 80
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen F., Gafken P.R., Gottschling D.E. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 2002, 109:745-756.
    • (2002) Cell , vol.109 , pp. 745-756
    • van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 81
    • 0037163016 scopus 로고    scopus 로고
    • Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase
    • Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J. Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase. J. Biol. Chem. 2002, 277:30421-30424.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30421-30424
    • Lacoste, N.1    Utley, R.T.2    Hunter, J.M.3    Poirier, G.G.4    Cote, J.5
  • 82
  • 83
    • 0344837759 scopus 로고    scopus 로고
    • Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase
    • Min J., Feng Q., Li Z., Zhang Y., Xu R.M. Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell 2003, 112:711-723.
    • (2003) Cell , vol.112 , pp. 711-723
    • Min, J.1    Feng, Q.2    Li, Z.3    Zhang, Y.4    Xu, R.M.5
  • 84
  • 87
    • 79959960773 scopus 로고    scopus 로고
    • The diverse functions of Dot1 and H3K79 methylation
    • Nguyen A.T., Zhang Y. The diverse functions of Dot1 and H3K79 methylation. Genes Dev. 2011, 25:1345-1358.
    • (2011) Genes Dev. , vol.25 , pp. 1345-1358
    • Nguyen, A.T.1    Zhang, Y.2
  • 91
  • 93
    • 80052971028 scopus 로고    scopus 로고
    • Epigenetics: targeting leukemia on the DOT
    • Travers J., Blagg J., Workman P. Epigenetics: targeting leukemia on the DOT. Nat. Chem. Biol. 2011, 7:663-665.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 663-665
    • Travers, J.1    Blagg, J.2    Workman, P.3
  • 95
    • 84863115862 scopus 로고    scopus 로고
    • Deficiency of H3K79 histone methyltransferase Dot1-like protein (DOT1L) inhibits cell proliferation
    • Kim W., Kim R., Park G., Park J.W., Kim J.E. Deficiency of H3K79 histone methyltransferase Dot1-like protein (DOT1L) inhibits cell proliferation. J. Biol. Chem. 2012, 287:5588-5599.
    • (2012) J. Biol. Chem. , vol.287 , pp. 5588-5599
    • Kim, W.1    Kim, R.2    Park, G.3    Park, J.W.4    Kim, J.E.5
  • 98
    • 84856120332 scopus 로고    scopus 로고
    • Understanding the language of Lys36 methylation at histone
    • Wagner E.J., Carpenter P.B. Understanding the language of Lys36 methylation at histone. Nat. Rev. Mol. Cell Biol. 2012, 13:115-126.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 115-126
    • Wagner, E.J.1    Carpenter, P.B.2
  • 99
    • 38549139593 scopus 로고    scopus 로고
    • Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation
    • Edmunds J.W., Mahadevan L.C., Clayton A.L. Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation. EMBO J. 2008, 27:406-420.
    • (2008) EMBO J. , vol.27 , pp. 406-420
    • Edmunds, J.W.1    Mahadevan, L.C.2    Clayton, A.L.3
  • 100
    • 46849115153 scopus 로고    scopus 로고
    • Histone methyltransferase protein SETD2 interacts with p53 and selectively regulates its downstream genes
    • Xie P., Tian C., An L., Nie J., Lu K., Xing G., Zhang L., He F. Histone methyltransferase protein SETD2 interacts with p53 and selectively regulates its downstream genes. Cell. Signal. 2008, 20:1671-1678.
    • (2008) Cell. Signal. , vol.20 , pp. 1671-1678
    • Xie, P.1    Tian, C.2    An, L.3    Nie, J.4    Lu, K.5    Xing, G.6    Zhang, L.7    He, F.8
  • 101
    • 70049111751 scopus 로고    scopus 로고
    • The mRNA expression of SETD2 in human breast cancer: correlation with clinico-pathological parameters
    • Al Sarakbi W., Sasi W., Jiang W.G., Roberts T., Newbold R.F., Mokbel K. The mRNA expression of SETD2 in human breast cancer: correlation with clinico-pathological parameters. BMC Cancer 2009, 9:290.
    • (2009) BMC Cancer , vol.9 , pp. 290
    • Al Sarakbi, W.1    Sasi, W.2    Jiang, W.G.3    Roberts, T.4    Newbold, R.F.5    Mokbel, K.6
  • 102
    • 77958548631 scopus 로고    scopus 로고
    • Evidence for a tumour suppressor function of SETD2 in human breast cancer: a new hypothesis
    • Newbold R.F., Mokbel K. Evidence for a tumour suppressor function of SETD2 in human breast cancer: a new hypothesis. Anticancer Res. 2010, 30:3309-3311.
    • (2010) Anticancer Res. , vol.30 , pp. 3309-3311
    • Newbold, R.F.1    Mokbel, K.2
  • 106
    • 77953170322 scopus 로고    scopus 로고
    • Histone methyltransferase gene SETD2 is a novel tumor suppressor gene in clear cell renal cell carcinoma
    • Duns G., van den Berg E., van Duivenbode I., Osinga J., Hollema H., Hofstra R.M., Kok K. Histone methyltransferase gene SETD2 is a novel tumor suppressor gene in clear cell renal cell carcinoma. Cancer Res. 2010, 70:4287-4291.
    • (2010) Cancer Res. , vol.70 , pp. 4287-4291
    • Duns, G.1    van den Berg, E.2    van Duivenbode, I.3    Osinga, J.4    Hollema, H.5    Hofstra, R.M.6    Kok, K.7
  • 108
    • 0032569014 scopus 로고    scopus 로고
    • The PR domain of the Rb-binding zinc finger protein RIZ1 is a protein binding interface and is related to the SET domain functioning in chromatin-mediated gene expression
    • Huang S., Shao G., Liu L. The PR domain of the Rb-binding zinc finger protein RIZ1 is a protein binding interface and is related to the SET domain functioning in chromatin-mediated gene expression. J. Biol. Chem. 1998, 273:15933-15939.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15933-15939
    • Huang, S.1    Shao, G.2    Liu, L.3
  • 109
    • 78049275346 scopus 로고    scopus 로고
    • Role for the nuclear receptor-binding SET domain protein 1 (NSD1) methyltransferase in coordinating lysine 36 methylation at histone 3 with RNA polymerase II function
    • Lucio-Eterovic A.K., Singh M.M., Gardner J.E., Veerappan C.S., Rice J.C., Carpenter P.B. Role for the nuclear receptor-binding SET domain protein 1 (NSD1) methyltransferase in coordinating lysine 36 methylation at histone 3 with RNA polymerase II function. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:16952-16957.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 16952-16957
    • Lucio-Eterovic, A.K.1    Singh, M.M.2    Gardner, J.E.3    Veerappan, C.S.4    Rice, J.C.5    Carpenter, P.B.6
  • 110
    • 0031779421 scopus 로고    scopus 로고
    • WHSC1, a 90kb SET domain-containing gene, expressed in early development and homologous to a Drosophila dysmorphy gene maps in the Wolf-Hirschhorn syndrome critical region and is fused to IgH in t(4;14) multiple myeloma
    • Stec I., Wright T.J., van Ommen G.J., de Boer P.A., van Haeringen A., Moorman A.F., Altherr M.R., den Dunnen J.T. WHSC1, a 90kb SET domain-containing gene, expressed in early development and homologous to a Drosophila dysmorphy gene maps in the Wolf-Hirschhorn syndrome critical region and is fused to IgH in t(4;14) multiple myeloma. Hum. Mol. Genet. 1998, 7:1071-1082.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1071-1082
    • Stec, I.1    Wright, T.J.2    van Ommen, G.J.3    de Boer, P.A.4    van Haeringen, A.5    Moorman, A.F.6    Altherr, M.R.7    den Dunnen, J.T.8
  • 111
    • 0032212243 scopus 로고    scopus 로고
    • The t(4;14) translocation in myeloma dysregulates both FGFR3 and a novel gene MMSET, resulting in IgH/MMSET hybrid transcripts
    • Chesi M., Nardini E., Lim R.S., Smith K.D., Kuehl W.M., Bergsagel P.L. The t(4;14) translocation in myeloma dysregulates both FGFR3 and a novel gene MMSET, resulting in IgH/MMSET hybrid transcripts. Blood 1998, 92:3025-3034.
    • (1998) Blood , vol.92 , pp. 3025-3034
    • Chesi, M.1    Nardini, E.2    Lim, R.S.3    Smith, K.D.4    Kuehl, W.M.5    Bergsagel, P.L.6
  • 112
    • 0035872769 scopus 로고    scopus 로고
    • NSD3, a new SET domain-containing gene, maps to 8p12 and is amplified in human breast cancer cell lines
    • Angrand P.O., Apiou F., Stewart A.F., Dutrillaux B., Losson R., Chambon P. NSD3, a new SET domain-containing gene, maps to 8p12 and is amplified in human breast cancer cell lines. Genomics 2001, 74:79-88.
    • (2001) Genomics , vol.74 , pp. 79-88
    • Angrand, P.O.1    Apiou, F.2    Stewart, A.F.3    Dutrillaux, B.4    Losson, R.5    Chambon, P.6
  • 115
    • 67349115185 scopus 로고    scopus 로고
    • The histone methyltransferase, NSD2, enhances androgen receptor-mediated transcription
    • Kang H.B., Choi Y., Lee J.M., Choi K.C., Kim H.C., Yoo J.Y., Lee Y.H., Yoon H.G. The histone methyltransferase, NSD2, enhances androgen receptor-mediated transcription. FEBS Lett. 2009, 583:1880-1886.
    • (2009) FEBS Lett. , vol.583 , pp. 1880-1886
    • Kang, H.B.1    Choi, Y.2    Lee, J.M.3    Choi, K.C.4    Kim, H.C.5    Yoo, J.Y.6    Lee, Y.H.7    Yoon, H.G.8
  • 119
    • 84894478422 scopus 로고    scopus 로고
    • Substrate specificity analysis and novel substrates of the protein lysine methyltransferase NSD1
    • Kudithipudi S., Lungu C., Rathert P., Happel N., Jeltsch A. Substrate specificity analysis and novel substrates of the protein lysine methyltransferase NSD1. Chem. Biol. 2014, 21:226-237.
    • (2014) Chem. Biol. , vol.21 , pp. 226-237
    • Kudithipudi, S.1    Lungu, C.2    Rathert, P.3    Happel, N.4    Jeltsch, A.5
  • 121
    • 67650461956 scopus 로고    scopus 로고
    • A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf-Hirschhorn syndrome
    • Nimura K., Ura K., Shiratori H., Ikawa M., Okabe M., Schwartz R.J., Kaneda Y. A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf-Hirschhorn syndrome. Nature 2009, 460:287-291.
    • (2009) Nature , vol.460 , pp. 287-291
    • Nimura, K.1    Ura, K.2    Shiratori, H.3    Ikawa, M.4    Okabe, M.5    Schwartz, R.J.6    Kaneda, Y.7
  • 122
    • 79959272481 scopus 로고    scopus 로고
    • Cancers and the NSD family of histone lysine methyltransferases
    • Morishita M., di Luccio E. Cancers and the NSD family of histone lysine methyltransferases. Biochim. Biophys. Acta 2011, 1816:158-163.
    • (2011) Biochim. Biophys. Acta , vol.1816 , pp. 158-163
    • Morishita, M.1    di Luccio, E.2
  • 125
    • 34347392874 scopus 로고    scopus 로고
    • NUP98-NSD1 links H3K36 methylation to Hox-A gene activation and leukaemogenesis
    • Wang G.G., Cai L., Pasillas M.P., Kamps M.P. NUP98-NSD1 links H3K36 methylation to Hox-A gene activation and leukaemogenesis. Nat. Cell Biol. 2007, 9:804-812.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 804-812
    • Wang, G.G.1    Cai, L.2    Pasillas, M.P.3    Kamps, M.P.4
  • 128
    • 33644542409 scopus 로고    scopus 로고
    • SmyD1, a histone methyltransferase, is required for myofibril organization and muscle contraction in zebrafish embryos
    • Tan X., Rotllant J., Li H., De Deyne P., Du S.J. SmyD1, a histone methyltransferase, is required for myofibril organization and muscle contraction in zebrafish embryos. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:2713-2718.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2713-2718
    • Tan, X.1    Rotllant, J.2    Li, H.3    De Deyne, P.4    Du, S.J.5
  • 130
    • 33746832077 scopus 로고    scopus 로고
    • Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex
    • Brown M.A., Sims R.J., Gottlieb P.D., Tucker P.W. Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex. Mol. Cancer 2006, 5:26.
    • (2006) Mol. Cancer , vol.5 , pp. 26
    • Brown, M.A.1    Sims, R.J.2    Gottlieb, P.D.3    Tucker, P.W.4
  • 136
    • 84897114159 scopus 로고    scopus 로고
    • SMYD2 is highly expressed in pediatric acute lymphoblastic leukemia and constitutes a bad prognostic factor
    • Sakamoto L.H., Andrade R.V., Felipe M.S., Motoyama A.B., Pittella Silva F. SMYD2 is highly expressed in pediatric acute lymphoblastic leukemia and constitutes a bad prognostic factor. Leuk. Res. 2014, 38:496-502.
    • (2014) Leuk. Res. , vol.38 , pp. 496-502
    • Sakamoto, L.H.1    Andrade, R.V.2    Felipe, M.S.3    Motoyama, A.B.4    Pittella Silva, F.5
  • 138
    • 65949117245 scopus 로고    scopus 로고
    • Identification of Smyd4 as a potential tumor suppressor gene involved in breast cancer development
    • Hu L., Zhu Y.T., Qi C., Zhu Y.J. Identification of Smyd4 as a potential tumor suppressor gene involved in breast cancer development. Cancer Res. 2009, 69:4067-4072.
    • (2009) Cancer Res. , vol.69 , pp. 4067-4072
    • Hu, L.1    Zhu, Y.T.2    Qi, C.3    Zhu, Y.J.4
  • 141
    • 42549095632 scopus 로고    scopus 로고
    • Enhanced methyltransferase activity of SMYD3 by the cleavage of its N-terminal region in human cancer cells
    • Silva F.P., Hamamoto R., Kunizaki M., Tsuge M., Nakamura Y., Furukawa Y. Enhanced methyltransferase activity of SMYD3 by the cleavage of its N-terminal region in human cancer cells. Oncogene 2008, 27:2686-2692.
    • (2008) Oncogene , vol.27 , pp. 2686-2692
    • Silva, F.P.1    Hamamoto, R.2    Kunizaki, M.3    Tsuge, M.4    Nakamura, Y.5    Furukawa, Y.6
  • 147
    • 84863770814 scopus 로고    scopus 로고
    • Cancer genetics and epigenetics: two sides of the same coin?
    • You J.S., Jones P.A. Cancer genetics and epigenetics: two sides of the same coin?. Cancer Cell 2012, 22:9-20.
    • (2012) Cancer Cell , vol.22 , pp. 9-20
    • You, J.S.1    Jones, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.