메뉴 건너뛰기




Volumn 30, Issue 15, 2011, Pages 1822-1830

PAX5-PML acts as a dual dominant-negative form of both PAX5 and PML

Author keywords

apoptosis; arsenic trioxide; DNA binding; nuclear body; PAX5; PML

Indexed keywords

ARSENIC TRIOXIDE; PROMYELOCYTIC LEUKEMIA PROTEIN; TRANSCRIPTION FACTOR PAX5;

EID: 79954621829     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2010.554     Document Type: Article
Times cited : (36)

References (43)
  • 1
    • 33744522801 scopus 로고    scopus 로고
    • Histone deacetylase 3 (HDAC3) is recruited to target promoters by PML-RARα as a component of the N-CoR co-repressor complex to repress transcription in vivo
    • DOI 10.1016/j.bbrc.2006.05.047, PII S0006291X06010904
    • Atsumi A, Tomita A, Kiyoi H, Naoe T. (2006). Histone deacetylase 3 (HDAC3) is recruited to target promoters by PML-RARalpha as a component of the N-CoR co-repressor complex to repress transcription in vivo. Biochem Biophys Res Commun 345: 1471-1480. (Pubitemid 43817898)
    • (2006) Biochemical and Biophysical Research Communications , vol.345 , Issue.4 , pp. 1471-1480
    • Atsumi, A.1    Tomita, A.2    Kiyoi, H.3    Naoe, T.4
  • 2
    • 2542442633 scopus 로고    scopus 로고
    • Transcriptional control of early B cell development
    • DOI 10.1146/annurev.immunol.22.012703.104807
    • Busslinger M. (2004). Transcriptional control of early B cell development. Annu Rev Immunol 22: 55-79. (Pubitemid 38680418)
    • (2004) Annual Review of Immunology , vol.22 , pp. 55-79
    • Busslinger, M.1
  • 5
    • 0027426925 scopus 로고
    • DNA sequence recognition by Pax proteins: Bipartite structure of the paired domain and its binding site
    • Czerny T, Schaffner G, Busslinger M. (1993). DNA sequence recognition by Pax proteins: bipartite structure of the paired domain and its binding site. Genes Dev 7: 2048-2061. (Pubitemid 23312955)
    • (1993) Genes and Development , vol.7 , Issue.10 , pp. 2048-2061
    • Czerny, T.1    Schaffner, G.2    Busslinger, M.3
  • 6
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: Dynamic sensors of DNA damage and cellular stress
    • DOI 10.1002/bies.20089
    • Dellaire G, Bazett-Jones DP. (2004). PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 26: 963-977. (Pubitemid 39273070)
    • (2004) BioEssays , vol.26 , Issue.9 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 7
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • DOI 10.1016/0092-8674(94)90340-9
    • Dyck JA, Maul GG, Miller Jr WH, Chen JD, Kakizuka A, Evans RM. (1994). A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76: 333-343. (Pubitemid 24046695)
    • (1994) Cell , vol.76 , Issue.2 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller Jr., W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 8
    • 70450255241 scopus 로고    scopus 로고
    • PAX5 mutations occur frequently in adult B-cell progenitor acute lymphoblastic leukemia and PAX5 hap-loinsufficiency is associated with BCR-ABL1 and TCF3-PBX1 fusion genes: A GRAALL study
    • Familiades J, Bousquet M, Lafage-Pochitaloff M, Bene MC, Beldjord K, De Vos J et al. (2009). PAX5 mutations occur frequently in adult B-cell progenitor acute lymphoblastic leukemia and PAX5 hap-loinsufficiency is associated with BCR-ABL1 and TCF3-PBX1 fusion genes: a GRAALL study. Leukemia 23: 1989-1998.
    • (2009) Leukemia , vol.23 , pp. 1989-1998
    • Familiades, J.1    Bousquet, M.2    Lafage-Pochitaloff, M.3    Bene, M.C.4    Beldjord, K.5    De Vos, J.6
  • 9
    • 39149096620 scopus 로고    scopus 로고
    • PAX5/TEL acts as a transcriptional repressor causing down-modulation of CD19, enhances migration to CXCL12, and confers survival advantage in pre-BI cells
    • DOI 10.1158/0008-5472.CAN-07-2778
    • Fazio G, Palmi C, Rolink A, Biondi A, Cazzaniga G. (2008). PAX5/ TEL acts as a transcriptional repressor causing down-modulation of CD19, enhances migration to CXCL12, and confers survival advantage in pre-BI cells. Cancer Res 68: 181-189. (Pubitemid 351380119)
    • (2008) Cancer Research , vol.68 , Issue.1 , pp. 181-189
    • Fazio, G.1    Palmi, C.2    Rolink, A.3    Biondi, A.4    Cazzaniga, G.5
  • 10
    • 54049143319 scopus 로고    scopus 로고
    • Acetylation of PML is involved in histone deacetylase inhibitor-mediated apoptosis
    • Hayakawa F, Abe A, Kitabayashi I, Pandolfi PP, Naoe T. (2008). Acetylation of PML is involved in histone deacetylase inhibitor-mediated apoptosis. J Biol Chem 283: 24420-24425.
    • (2008) J Biol Chem , vol.283 , pp. 24420-24425
    • Hayakawa, F.1    Abe, A.2    Kitabayashi, I.3    Pandolfi, P.P.4    Naoe, T.5
  • 11
    • 1842785771 scopus 로고    scopus 로고
    • Phosphorylation of PML by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis
    • DOI 10.1016/S1535-6108(04)00082-0, PII S1535610804000820
    • Hayakawa F, Privalsky ML. (2004). Phosphorylation of PML by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis. Cancer Cell 5: 389-401. (Pubitemid 38482074)
    • (2004) Cancer Cell , vol.5 , Issue.4 , pp. 389-401
    • Hayakawa, F.1    Privalsky, M.L.2
  • 13
    • 33645850703 scopus 로고    scopus 로고
    • Repression of Flt3 by Pax5 is crucial for B-cell lineage commitment
    • Holmes ML, Carotta S, Corcoran LM, Nutt SL. (2006). Repression of Flt3 by Pax5 is crucial for B-cell lineage commitment. Genes Dev 20: 933-938.
    • (2006) Genes Dev , vol.20 , pp. 933-938
    • Holmes, M.L.1    Carotta, S.2    Corcoran, L.M.3    Nutt, S.L.4
  • 15
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1
    • Ishov AM, Sotnikov AG, Negorev D, Vladimirova OV, Neff N, Kamitani T et al. (1999). PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1. J Cell Biol 147: 221-234.
    • (1999) J Cell Biol , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3    Vladimirova, O.V.4    Neff, N.5    Kamitani, T.6
  • 17
    • 50149109824 scopus 로고    scopus 로고
    • Cloning of genes involved in chromosomal translocations by high-resolution single nucleotide polymorphism genomic microarray
    • Kawamata N, Ogawa S, Zimmermann M, Niebuhr B, Stocking C, Sanada M et al. (2008). Cloning of genes involved in chromosomal translocations by high-resolution single nucleotide polymorphism genomic microarray. Proc Natl Acad Sci USA 105: 11921-11926.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11921-11926
    • Kawamata, N.1    Ogawa, S.2    Zimmermann, M.3    Niebuhr, B.4    Stocking, C.5    Sanada, M.6
  • 20
    • 0026710736 scopus 로고
    • The promoter of the CD19 gene is a target for the B-cell-specific transcription factor BSAP
    • Kozmik Z, Wang S, Dorfler P, Adams B, Busslinger M. (1992). The promoter of the CD19 gene is a target for the B-cell-specific transcription factor BSAP. Mol Cell Biol 12: 2662-2672.
    • (1992) Mol Cell Biol , vol.12 , pp. 2662-2672
    • Kozmik, Z.1    Wang, S.2    Dorfler, P.3    Adams, B.4    Busslinger, M.5
  • 21
    • 0142009657 scopus 로고    scopus 로고
    • Requirements for selective recruitment of Ets proteins and activation of mb-1/lg-α gene transcription by Pax-5 (BSAP)
    • DOI 10.1093/nar/gkg785
    • Maier H, Ostraat R, Parenti S, Fitzsimmons D, Abraham LJ, Garvie CW et al. (2003). Requirements for selective recruitment of Ets proteins and activation of mb-1/Ig-alpha gene transcription by Pax-5 (BSAP). Nucleic Acids Res 31: 5483-5489. (Pubitemid 37441918)
    • (2003) Nucleic Acids Research , vol.31 , Issue.19 , pp. 5483-5489
    • Maier, H.1    Ostraat, R.2    Parenti, S.3    Fitzsimmons, D.4    Abraham, L.J.5    Garvie, C.W.6    Hagman, J.7
  • 22
    • 0037025198 scopus 로고    scopus 로고
    • Reversion of B cell commitment upon loss of Pax5 expression
    • DOI 10.1126/science.1067518
    • Mikkola I, Heavey B, Horcher M, Busslinger M. (2002). Reversion of B cell commitment upon loss of Pax5 expression. Science 297: 110-113. (Pubitemid 34743105)
    • (2002) Science , vol.297 , Issue.5578 , pp. 110-113
    • Mikkola, I.1    Heavey, B.2    Horcher, M.3    Busslinger, M.4
  • 24
    • 0032052378 scopus 로고    scopus 로고
    • Loss- and gain-of-function mutations reveal an important role of BSAP (Pax-5) at the start and end of B cell differentiation
    • DOI 10.1006/smim.1998.0115
    • Morrison AM, Nutt SL, Thevenin C, Rolink A, Busslinger M. (1998). Loss- and gain-of-function mutations reveal an important role of BSAP (Pax-5) at the start and end of B cell differentiation. Semin Immunol 10: 133-142. (Pubitemid 28339783)
    • (1998) Seminars in Immunology , vol.10 , Issue.2 , pp. 133-142
    • Morrison, A.M.1    Nutt, S.L.2    Thevenin, C.3    Rolink, A.4    Busslinger, M.5
  • 25
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • DOI 10.1093/emboj/17.1.61
    • Muller S, Matunis MJ, Dejean A. (1998). Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. Embo J 17: 61-70. (Pubitemid 28041048)
    • (1998) EMBO Journal , vol.17 , Issue.1 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 27
    • 58249118804 scopus 로고    scopus 로고
    • Incidence and diversity of PAX5 fusion genes in childhood acute lymphoblastic leukemia
    • Nebral K, Denk D, Attarbaschi A, Konig M, Mann G, Haas OA et al. (2009). Incidence and diversity of PAX5 fusion genes in childhood acute lymphoblastic leukemia. Leukemia 23: 134-143.
    • (2009) Leukemia , vol.23 , pp. 134-143
    • Nebral, K.1    Denk, D.2    Attarbaschi, A.3    Konig, M.4    Mann, G.5    Haas, O.A.6
  • 28
    • 34848832341 scopus 로고    scopus 로고
    • Identification of PML as novel PAX5 fusion partner in childhood acute lymphoblastic leukaemia
    • DOI 10.1111/j.1365-2141.2007.06731.x
    • Nebral K, Konig M, Harder L, Siebert R, Haas OA, Strehl S. (2007). Identification of PML as novel PAX5 fusion partner in childhood acute lymphoblastic leukaemia. Br J Haematol 139: 269-274. (Pubitemid 47493075)
    • (2007) British Journal of Haematology , vol.139 , Issue.2 , pp. 269-274
    • Nebral, K.1    Konig, M.2    Harder, L.3    Siebert, R.4    Haas, O.A.5    Strehl, S.6
  • 31
    • 0032522538 scopus 로고    scopus 로고
    • Identification of BSAP (Pax-5) target genes in early B-cell development by loss- and gain-of-function experiments
    • DOI 10.1093/emboj/17.8.2319
    • Nutt SL, Morrison AM, Dorfler P, Rolink A, Busslinger M. (1998). Identification of BSAP (Pax-5) target genes in early B-cell development by loss- and gain-of-function experiments. EMBO J 17: 2319-2333. (Pubitemid 28171916)
    • (1998) EMBO Journal , vol.17 , Issue.8 , pp. 2319-2333
    • Nutt, S.L.1    Morrison, A.M.2    Dorfler, P.3    Rolink, A.4    Busslinger, M.5
  • 32
    • 0037606048 scopus 로고    scopus 로고
    • A novel murine model of Cooley anemia and its rescue by lentiviral-mediated human β-globin gene transfer
    • DOI 10.1182/blood-2002-10-3305
    • Rivella S, May C, Chadburn A, Riviere I, Sadelain M. (2003). A novel murine model of Cooley anemia and its rescue by lentiviral-mediated human beta-globin gene transfer. Blood 101: 2932-2939. (Pubitemid 36857977)
    • (2003) Blood , vol.101 , Issue.8 , pp. 2932-2939
    • Rivella, S.1    May, C.2    Chadburn, A.3    Riviere, I.4    Sadelain, M.5
  • 33
    • 0036798665 scopus 로고    scopus 로고
    • Control of pre-BCR signaling by Pax5-dependent activation of the BLNK gene
    • DOI 10.1016/S1074-7613(02)00418-1
    • Schebesta M, Pfeffer PL, Busslinger M. (2002). Control of pre-BCR signaling by Pax5-dependent activation of the BLNK gene. Immunity 17: 473-485. (Pubitemid 35223536)
    • (2002) Immunity , vol.17 , Issue.4 , pp. 473-485
    • Schebesta, M.1    Pfeffer, P.L.2    Busslinger, M.3
  • 34
    • 0036906546 scopus 로고    scopus 로고
    • Pax5 promotes B lymphopoiesis and blocks T cell development by repressing Notch1
    • DOI 10.1016/S1074-7613(02)00472-7
    • Souabni A, Cobaleda C, Schebesta M, Busslinger M. (2002). Pax5 promotes B lymphopoiesis and blocks T cell development by repressing Notch1. Immunity 17: 781-793. (Pubitemid 35477797)
    • (2002) Immunity , vol.17 , Issue.6 , pp. 781-793
    • Souabni, A.1    Cobaleda, C.2    Schebesta, M.3    Busslinger, M.4
  • 37
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RARα in acute promyelocytic leukemia cells
    • DOI 10.1016/0092-8674(94)90341-7
    • Weis K, Rambaud S, Lavau C, Jansen J, Carvalho T, Carmo-Fonseca M et al. (1994). Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell 76: 345-356. (Pubitemid 24046696)
    • (1994) Cell , vol.76 , Issue.2 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Fonseca, M.6    Lamond, A.7    Dejeant, A.8
  • 38
    • 0035099686 scopus 로고    scopus 로고
    • The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases
    • DOI 10.1128/MCB.21.7.2259-2268.2001
    • Wu WS, Vallian S, Seto E, Yang WM, Edmondson D, Roth S et al. (2001). The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol Cell Biol 21: 2259-2268. (Pubitemid 32222080)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.7 , pp. 2259-2268
    • Wu, W.-S.1    Vallian, S.2    Seto, E.3    Yang, W.-M.4    Edmondson, D.5    Roth, S.6    Chang, K.-S.7
  • 39
    • 0036847998 scopus 로고    scopus 로고
    • PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2
    • DOI 10.1038/ncb869
    • Yang S, Kuo C, Bisi JE, Kim MK. (2002). PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/ Chk2. Nat Cell Biol 4: 865-870. (Pubitemid 35331361)
    • (2002) Nature Cell Biology , vol.4 , Issue.11 , pp. 865-870
    • Yang, S.1    Kuo, C.2    Bisi, J.E.3    Kim, M.K.4
  • 40
    • 77950826446 scopus 로고    scopus 로고
    • Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML
    • Zhang XW, Yan XJ, Zhou ZR, Yang FF, Wu ZY, Sun HB et al. (2010). Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML. Science 328: 240-243.
    • (2010) Science , vol.328 , pp. 240-243
    • Zhang, X.W.1    Yan, X.J.2    Zhou, Z.R.3    Yang, F.F.4    Wu, Z.Y.5    Sun, H.B.6
  • 42
    • 0034695883 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis
    • Zhong S, Salomoni P, Ronchetti S, Guo A, Ruggero D, Pandolfi PP. (2000b). Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. J Exp Med 191: 631-640.
    • (2000) J Exp Med , vol.191 , pp. 631-640
    • Zhong, S.1    Salomoni, P.2    Ronchetti, S.3    Guo, A.4    Ruggero, D.5    Pandolfi, P.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.