메뉴 건너뛰기




Volumn 122, Issue 11, 2013, Pages 1914-1922

MLL fusion protein–driven AML is selectively inhibited by targeted disruption of the MLL-PAFc interaction

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; MEIS1 PROTEIN; MIXED LINEAGE LEUKEMIA PROTEIN; PEPTIDES AND PROTEINS; POLYMERASE ASSOCIATED FACTOR COMPLEX; PROTEIN BCL 2; PROTEIN CDC73; UNCLASSIFIED DRUG; HOMEODOMAIN PROTEIN; HRPT2 PROTEIN, MOUSE; MLL AF9 FUSION PROTEIN, MOUSE; MLL-AF9 FUSION PROTEIN, MOUSE; MYELOID ECOTROPIC VIRAL INTEGRATION SITE 1 PROTEIN; NUCLEAR PROTEIN; ONCOPROTEIN; PAF1 PROTEIN, HUMAN; TRANSCRIPTION FACTOR HOXA9; TUMOR PROTEIN; TUMOR SUPPRESSOR PROTEIN;

EID: 84887346920     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2013-02-486977     Document Type: Article
Times cited : (15)

References (30)
  • 1
    • 84856916060 scopus 로고    scopus 로고
    • The pathogenesis of mixed-lineage leukemia
    • Muntean AG, Hess JL. 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
  • 2
    • 70350497118 scopus 로고    scopus 로고
    • Novel prognostic subgroups in childhood 11q23/ mll-rearranged acute myeloid leukemia: results of an international retrospective study
    • Balgobind BV, Raimondi SC, Harbott J, et al. Novel prognostic subgroups in childhood 11q23/ MLL-rearranged acute myeloid leukemia: results of an international retrospective study. Blood. 2009;114(12):2489-2496.
    • (2009) Blood , vol.114 , Issue.12 , pp. 2489-2496
    • Balgobind, B.V.1    Raimondi, S.C.2    Harbott, J.3
  • 3
    • 0027172909 scopus 로고
    • Molecular rearrangements on chromosome 11q23 predominate in infant acute lymphoblastic leukemia and are associated with specific biologic variables and poor outcome
    • Chen CS, Sorensen PH, Domer PH, et al. Molecular rearrangements on chromosome 11q23 predominate in infant acute lymphoblastic leukemia and are associated with specific biologic variables and poor outcome. Blood. 1993;81(9): 2386-2393.
    • (1993) Blood , vol.81 , Issue.9 , pp. 2386-2393
    • Chen, C.S.1    Sorensen, P.H.2    Domer, P.H.3
  • 4
    • 77957128551 scopus 로고    scopus 로고
    • Licensed to elongate: A molecular mechanism for mll-based leukaemogenesis
    • Mohan M, Lin C, Guest E, Shilatifard A. Licensed to elongate: a molecular mechanism for MLL-based leukaemogenesis. Nat Rev Cancer. 2010; 10(10):721-728.
    • (2010) Nat Rev Cancer , vol.10 , Issue.10 , pp. 721-728
    • Mohan, M.1    Lin, C.2    Guest, E.3    Shilatifard, A.4
  • 5
    • 77953811794 scopus 로고    scopus 로고
    • Binding of the mll phd3 finger to histone h3k4me3 is required for mll-dependent gene transcription
    • Chang PY, Hom RA, Musselman CA, et al. Binding of the MLL PHD3 finger to histone H3K4me3 is required for MLL-dependent gene transcription. J Mol Biol. 2010;400(2):137-144.
    • (2010) J Mol Biol , vol.400 , Issue.2 , pp. 137-144
    • Chang, P.Y.1    Hom, R.A.2    Musselman, C.A.3
  • 6
    • 78650205549 scopus 로고    scopus 로고
    • Mll-af9 and mll-enl alter the dynamic association of transcriptional regulators with genes critical for leukemia
    • 77-86.e71-75
    • Monroe SC, Jo SY, Sanders DS, et al. MLL-AF9 and MLL-ENL alter the dynamic association of transcriptional regulators with genes critical for leukemia. Exp Hematol. 2011;39(1):77-86.e71-75.
    • (2011) Exp Hematol , vol.39 , Issue.1
    • Monroe, S.C.1    Jo, S.Y.2    Sanders, D.S.3
  • 7
    • 39649084473 scopus 로고    scopus 로고
    • A role for the mll fusion partner enl in transcriptional elongation and chromatin modification
    • Mueller D, Bach C, Zeisig D, et al. A role for the MLL fusion partner ENL in transcriptional elongation and chromatin modification. Blood. 2007;110(13):4445-4454.
    • (2007) Blood , vol.110 , Issue.13 , pp. 4445-4454
    • Mueller, D.1    Bach, C.2    Zeisig, D.3
  • 8
    • 76349118080 scopus 로고    scopus 로고
    • A higher-order complex containing af4 and enl family proteins with p-tefb facilitates oncogenic and physiologic mll-dependent transcription
    • Yokoyama A, Lin M, Naresh A, Kitabayashi I, Cleary ML. A higher-order complex containing AF4 and ENL family proteins with P-TEFb facilitates oncogenic and physiologic MLL-dependent transcription. Cancer Cell. 2010;17(2): 198-212.
    • (2010) Cancer Cell , vol.17 , Issue.2 , pp. 198-212
    • Yokoyama, A.1    Lin, M.2    Naresh, A.3    Kitabayashi, I.4    Cleary, M.L.5
  • 9
    • 33846522525 scopus 로고    scopus 로고
    • The mixed-lineage leukemia fusion partner af4 stimulates rna polymerase ii transcriptional elongation and mediates coordinated chromatin remodeling
    • Bitoun E, Oliver PL, Davies KE. The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling. Hum Mol Genet. 2007;16(1):92-106.
    • (2007) Hum Mol Genet , vol.16 , Issue.1 , pp. 92-106
    • Bitoun, E.1    Oliver, P.L.2    Davies, K.E.3
  • 10
    • 77949409084 scopus 로고    scopus 로고
    • Linking h3k79 trimethylation to wnt signaling through a novel dot1-containing complex (dotcom)
    • Mohan M, Herz HM, Takahashi YH, et al. Linking H3K79 trimethylation to Wnt signaling through a novel Dot1-containing complex (DotCom). Genes Dev. 2010;24(6):574-589.
    • (2010) Genes Dev , vol.24 , Issue.6 , pp. 574-589
    • Mohan, M.1    Herz, H.M.2    Takahashi, Y.H.3
  • 11
    • 36849046285 scopus 로고    scopus 로고
    • Histone crosstalk between h2b monoubiquitination and h3 methylation mediated by Compass
    • Lee JS, Shukla A, Schneider J, et al. Histone crosstalk between H2B monoubiquitination and H3 methylation mediated by COMPASS. Cell. 2007;131(6):1084-1096.
    • (2007) Cell , vol.131 , Issue.6 , pp. 1084-1096
    • Lee, J.S.1    Shukla, A.2    Schneider, J.3
  • 12
    • 0037047323 scopus 로고    scopus 로고
    • Methylation of histone h3 by compass requires ubiquitination of histone h2b by rad6
    • Dover J, Schneider J, Tawiah-Boateng MA, et al. Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6. J Biol Chem. 2002;277(32):28368-28371.
    • (2002) J Biol Chem , vol.277 , Issue.32 , pp. 28368-28371
    • Dover, J.1    Schneider, J.2    Tawiah-Boateng, M.A.3
  • 13
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone h2b regulates h3 methylation and gene silencing in yeast
    • Sun ZW, Allis CD. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature. 2002;418(6893):104-108.
    • (2002) Nature , vol.418 , Issue.6893 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 14
    • 68949149115 scopus 로고    scopus 로고
    • Direct bre1-paf1 complex interactions and ring finger-independent bre1-rad6 interactions mediate histone h2b ubiquitylation in yeast
    • Kim J, Roeder RG. Direct Bre1-Paf1 complex interactions and RING finger-independent Bre1-Rad6 interactions mediate histone H2B ubiquitylation in yeast. J Biol Chem. 2009; 284(31):20582-20592.
    • (2009) J Biol Chem , vol.284 , Issue.31 , pp. 20582-20592
    • Kim, J.1    Roeder, R.G.2
  • 15
    • 0141483281 scopus 로고    scopus 로고
    • The rtf1 component of the paf1 transcriptional elongation complex is required for ubiquitination of histone H2b
    • Ng HH, Dole S, Struhl K. The Rtf1 component of the Paf1 transcriptional elongation complex is required for ubiquitination of histone H2B. J Biol Chem. 2003;278(36):33625-33628.
    • (2003) J Biol Chem , vol.278 , Issue.36 , pp. 33625-33628
    • Ng, H.H.1    Dole, S.2    Struhl, K.3
  • 16
    • 0042818412 scopus 로고    scopus 로고
    • The paf1 complex is essential for histone monoubiquitination by the rad6-bre1 complex, which signals for histone methylation by compass and dot1p
    • Wood A, Schneider J, Dover J, Johnston M, Shilatifard A. The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem. 2003; 278(37):34739-34742.
    • (2003) J Biol Chem , vol.278 , Issue.37 , pp. 34739-34742
    • Wood, A.1    Schneider, J.2    Dover, J.3    Johnston, M.4    Shilatifard, A.5
  • 17
    • 27944454433 scopus 로고    scopus 로고
    • Monoubiquitination of human histone h2b: The factors involved and their roles in hox gene regulation
    • Zhu B, Zheng Y, Pham AD, et al. Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation. Mol Cell. 2005;20(4):601-611.
    • (2005) Mol Cell , vol.20 , Issue.4 , pp. 601-611
    • Zhu, B.1    Zheng, Y.2    Pham, A.D.3
  • 18
    • 77953913196 scopus 로고    scopus 로고
    • Multiple interactions recruit mll1 and mll1 fusion proteins to the hoxa9 locus in leukemogenesis
    • Milne TA, Kim J, Wang GG, et al. Multiple interactions recruit MLL1 and MLL1 fusion proteins to the HOXA9 locus in leukemogenesis. Mol Cell. 2010;38(6):853-863.
    • (2010) Mol Cell , vol.38 , Issue.6 , pp. 853-863
    • Milne, T.A.1    Kim, J.2    Wang, G.G.3
  • 19
    • 77953246813 scopus 로고    scopus 로고
    • The paf complex synergizes with mll fusion proteins at hox loci to promote leukemogenesis
    • Muntean AG, Tan J, Sitwala K, et al. The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. Cancer Cell. 2010;17(6):609-621.
    • (2010) Cancer Cell , vol.17 , Issue.6 , pp. 609-621
    • Muntean, A.G.1    Tan, J.2    Sitwala, K.3
  • 20
    • 11844269891 scopus 로고    scopus 로고
    • The parafibromin tumor suppressor protein is part of a human paf1 complex
    • Rozenblatt-Rosen O, Hughes CM, Nannepaga SJ, et al. The parafibromin tumor suppressor protein is part of a human Paf1 complex. Mol Cell Biol. 2005;25(2):612-620.
    • (2005) Mol Cell Biol , vol.25 , Issue.2 , pp. 612-620
    • Rozenblatt-Rosen, O.1    Hughes, C.M.2    Nannepaga, S.J.3
  • 21
    • 0030221376 scopus 로고    scopus 로고
    • A novel collection of accessory factors associated with yeast rna polymerase Ii
    • Wade PA, Werel W, Fentzke RC, et al. A novel collection of accessory factors associated with yeast RNA polymerase II. Protein Expr Purif. 1996;8(1):85-90.
    • (1996) Protein Expr Purif , vol.8 , Issue.1 , pp. 85-90
    • Wade, P.A.1    Werel, W.2    Fentzke, R.C.3
  • 22
    • 42349096478 scopus 로고    scopus 로고
    • Parafibromin, a component of the human paf complex, regulates growth factors and is required for embryonic development and survival in adult mice
    • Wang P, Bowl MR, Bender S, et al. Parafibromin, a component of the human PAF complex, regulates growth factors and is required for embryonic development and survival in adult mice. Mol Cell Biol. 2008;28(9):2930-2940.
    • (2008) Mol Cell Biol , vol.28 , Issue.9 , pp. 2930-2940
    • Wang, P.1    Bowl, M.R.2    Bender, S.3
  • 23
    • 0029759926 scopus 로고    scopus 로고
    • Reversal of apoptosis by the leukaemia-associated e2a-hlf chimaeric transcription factor
    • Inaba T, Inukai T, Yoshihara T, et al. Reversal of apoptosis by the leukaemia-associated E2A-HLF chimaeric transcription factor. Nature. 1996; 382(6591):541-544.
    • (1996) Nature , vol.382 , Issue.6591 , pp. 541-544
    • Inaba, T.1    Inukai, T.2    Yoshihara, T.3
  • 24
    • 76749090562 scopus 로고    scopus 로고
    • The human paf1 complex acts in chromatin transcription elongation both independently and cooperatively with Sii/tfiis
    • Kim J, Guermah M, Roeder RG. The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS. Cell. 2010;140(4):491-503.
    • (2010) Cell , vol.140 , Issue.4 , pp. 491-503
    • Kim, J.1    Guermah, M.2    Roeder, R.G.3
  • 25
    • 2442568473 scopus 로고    scopus 로고
    • The paf1 complex has functions independent of actively transcribing rna polymerase Ii
    • Mueller CL, Porter SE, Hoffman MG, Jaehning JA. The Paf1 complex has functions independent of actively transcribing RNA polymerase II. Mol Cell. 2004;14(4):447-456.
    • (2004) Mol Cell , vol.14 , Issue.4 , pp. 447-456
    • Mueller, C.L.1    Porter, S.E.2    Hoffman, M.G.3    Jaehning, J.A.4
  • 26
    • 79751529186 scopus 로고    scopus 로고
    • The e2a-hlf oncogenic fusion protein acts through lmo2 and bcl-2 to immortalize hematopoietic progenitors
    • de Boer J, Yeung J, Ellu J, et al. The E2A-HLF oncogenic fusion protein acts through Lmo2 and Bcl-2 to immortalize hematopoietic progenitors. Leukemia. 2011;25(2):321-330.
    • (2011) Leukemia , vol.25 , Issue.2 , pp. 321-330
    • De Boer, J.1    Yeung, J.2    Ellu, J.3
  • 27
    • 35948964020 scopus 로고    scopus 로고
    • Meis1 is an essential and rate-limiting regulator of mll leukemia stem cell potential [published correction appears in genes dev. 2007;15(21):3017]
    • Wong P, Iwasaki M, Somervaille TC, So CW, Cleary ML. Meis1 is an essential and rate-limiting regulator of MLL leukemia stem cell potential [published correction appears in Genes Dev. 2007;15(21):3017]. Genes Dev. 2007;21(21): 2762-2774.
    • (2007) Genes Dev , vol.21 , Issue.21 , pp. 2762-2774
    • Wong, P.1    Iwasaki, M.2    Somervaille, T.C.3    So, C.W.4    Cleary, M.L.5
  • 29
    • 45849115106 scopus 로고    scopus 로고
    • Menin critically links mll proteins with ledgf on cancer-associated target genes
    • Yokoyama A, Cleary ML. Menin critically links MLL proteins with LEDGF on cancer-associated target genes. Cancer Cell. 2008;14(1):36-46.
    • (2008) Cancer Cell , vol.14 , Issue.1 , pp. 36-46
    • Yokoyama, A.1    Cleary, M.L.2
  • 30
    • 44949221144 scopus 로고    scopus 로고
    • Mll protects cpg clusters from methylation within the hoxa9 gene, maintaining transcript expression
    • Erfurth FE, Popovic R, Grembecka J, et al. MLL protects CpG clusters from methylation within the Hoxa9 gene, maintaining transcript expression. Proc Natl Acad Sci USA. 2008;105(21): 7517-7522.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.21 , pp. 7517-7522
    • Erfurth, F.E.1    Popovic, R.2    Grembecka, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.