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Volumn 17, Issue 5, 2005, Pages 721-732

A role for PML3 in centrosome duplication and genome stability

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; CYCLIN DEPENDENT KINASE 2; PROMYELOCYTIC LEUKEMIA PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN 3; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

EID: 14644394332     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.02.014     Document Type: Article
Times cited : (43)

References (49)
  • 1
    • 4644259577 scopus 로고    scopus 로고
    • Induction of centrosome amplification and chromosome instability in p53-null cells by transient exposure to subtoxic levels of S-phase-targeting anticancer drugs
    • R.A. Bennett, H. Izumi, and K. Fukasawa Induction of centrosome amplification and chromosome instability in p53-null cells by transient exposure to subtoxic levels of S-phase-targeting anticancer drugs Oncogene 23 2004 6823 6829
    • (2004) Oncogene , vol.23 , pp. 6823-6829
    • Bennett, R.A.1    Izumi, H.2    Fukasawa, K.3
  • 2
    • 0035897415 scopus 로고    scopus 로고
    • Regulation and localization of the Bloom syndrome protein in response to DNA damage
    • O. Bischof, S.H. Kim, J. Irving, S. Beresten, N.A. Ellis, and J. Campisi Regulation and localization of the Bloom syndrome protein in response to DNA damage J. Cell Biol. 153 2001 367 380
    • (2001) J. Cell Biol. , vol.153 , pp. 367-380
    • Bischof, O.1    Kim, S.H.2    Irving, J.3    Beresten, S.4    Ellis, N.A.5    Campisi, J.6
  • 4
    • 0037034829 scopus 로고    scopus 로고
    • PML NBs associate with hMre11 complex and p53 at sites of irradiation induced DNA damage
    • R. Carbone, M. Pearson, S. Minucci, and P.P. Pelicci PML NBs associate with hMre11 complex and p53 at sites of irradiation induced DNA damage Oncogene 21 2002 1633 1640
    • (2002) Oncogene , vol.21 , pp. 1633-1640
    • Carbone, R.1    Pearson, M.2    Minucci, S.3    Pelicci, P.P.4
  • 5
    • 0036745763 scopus 로고    scopus 로고
    • CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells
    • Z. Chen, V.B. Indjeian, M. McManus, L. Wang, and B.D. Dynlacht CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells Dev. Cell 3 2002 339 350
    • (2002) Dev. Cell , vol.3 , pp. 339-350
    • Chen, Z.1    Indjeian, V.B.2    McManus, M.3    Wang, L.4    Dynlacht, B.D.5
  • 6
    • 0037048280 scopus 로고    scopus 로고
    • Centrosome amplification and the development of cancer
    • A.B. D'Assoro, W.L. Lingle, and J.L. Salisbury Centrosome amplification and the development of cancer Oncogene 21 2002 6146 6153
    • (2002) Oncogene , vol.21 , pp. 6146-6153
    • D'Assoro, A.B.1    Lingle, W.L.2    Salisbury, J.L.3
  • 7
    • 0029814277 scopus 로고    scopus 로고
    • Molecular genetics of Bloom's syndrome
    • N.A. Ellis, and J. German Molecular genetics of Bloom's syndrome Hum. Mol. Genet. 5 1996 1457 1463
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1457-1463
    • Ellis, N.A.1    German, J.2
  • 10
    • 0035854383 scopus 로고    scopus 로고
    • The mouse Mps1p-like kinase regulates centrosome duplication
    • H.A. Fisk, and M. Winey The mouse Mps1p-like kinase regulates centrosome duplication Cell 106 2001 95 104
    • (2001) Cell , vol.106 , pp. 95-104
    • Fisk, H.A.1    Winey, M.2
  • 12
    • 0033989262 scopus 로고    scopus 로고
    • Centrosome amplification and instability occurs exclusively in aneuploid, but not in diploid colorectal cancer cell lines, and correlates with numerical chromosomal aberrations
    • B.M. Ghadimi, D.L. Sackett, M.J. Difillippantonio, E. Schrock, T. Neumann, A. Jauho, G. Auer, and T. Ried Centrosome amplification and instability occurs exclusively in aneuploid, but not in diploid colorectal cancer cell lines, and correlates with numerical chromosomal aberrations Genes Chromosomes Cancer 27 2000 183 190
    • (2000) Genes Chromosomes Cancer , vol.27 , pp. 183-190
    • Ghadimi, B.M.1    Sackett, D.L.2    Difillippantonio, M.J.3    Schrock, E.4    Neumann, T.5    Jauho, A.6    Auer, G.7    Ried, T.8
  • 13
    • 0037017398 scopus 로고    scopus 로고
    • Drosophila Aurora a kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules
    • R. Giet, D. McLean, S. Descamps, M.J. Lee, J.W. Raff, C. Prigent, and D.M. Glover Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules J. Cell Biol. 156 2002 437 451
    • (2002) J. Cell Biol. , vol.156 , pp. 437-451
    • Giet, R.1    McLean, D.2    Descamps, S.3    Lee, M.J.4    Raff, J.W.5    Prigent, C.6    Glover, D.M.7
  • 14
    • 0032535244 scopus 로고    scopus 로고
    • Polo-like kinases: A team that plays through mitosis
    • D.M. Glover, I.M. Hagan, and A.A. Tavares Polo-like kinases: a team that plays through mitosis Genes Dev. 12 1998 3777 3787
    • (1998) Genes Dev. , vol.12 , pp. 3777-3787
    • Glover, D.M.1    Hagan, I.M.2    Tavares, A.A.3
  • 15
    • 0034564214 scopus 로고    scopus 로고
    • The centrosome-associated Aurora/Ip1-like kinase family
    • T.M. Goepfert, and B.R. Brinkley The centrosome-associated Aurora/Ip1-like kinase family Curr. Top. Dev. Biol. 49 2000 331 342
    • (2000) Curr. Top. Dev. Biol. , vol.49 , pp. 331-342
    • Goepfert, T.M.1    Brinkley, B.R.2
  • 17
    • 0035945342 scopus 로고    scopus 로고
    • Aurora-A kinase is required for centrosome maturation in Caenorhabditis elegans
    • E. Hannak, M. Kirkham, A.A. Hyman, and K. Oegema Aurora-A kinase is required for centrosome maturation in Caenorhabditis elegans J. Cell Biol. 155 2001 1109 1116
    • (2001) J. Cell Biol. , vol.155 , pp. 1109-1116
    • Hannak, E.1    Kirkham, M.2    Hyman, A.A.3    Oegema, K.4
  • 18
    • 0037048277 scopus 로고    scopus 로고
    • Two for two: Cdk2 and its role in centrosome doubling
    • E.H. Hinchcliffe, and G. Sluder Two for two: Cdk2 and its role in centrosome doubling Oncogene 21 2002 6154 6160
    • (2002) Oncogene , vol.21 , pp. 6154-6160
    • Hinchcliffe, E.H.1    Sluder, G.2
  • 19
    • 0141429171 scopus 로고    scopus 로고
    • Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells
    • T. Hirota, N. Kunitoku, T. Sasayama, T. Marumoto, D. Zhang, M. Nitta, K. Hatakeyama, and H. Saya Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells Cell 114 2003 585 598
    • (2003) Cell , vol.114 , pp. 585-598
    • Hirota, T.1    Kunitoku, N.2    Sasayama, T.3    Marumoto, T.4    Zhang, D.5    Nitta, M.6    Hatakeyama, K.7    Saya, H.8
  • 20
    • 13944270252 scopus 로고    scopus 로고
    • Playing polo in G1 - A novel function of polo-like kinase-2 in centriole duplication
    • I. Hoffmann Playing polo in G1 - a novel function of polo-like kinase-2 in centriole duplication Cell Cycle 3 2004 e76 e77
    • (2004) Cell Cycle , vol.3
    • Hoffmann, I.1
  • 21
    • 0032573068 scopus 로고    scopus 로고
    • BRCA1 is associated with the centrosome during mitosis
    • L.-C. Hsu, and R.L. White BRCA1 is associated with the centrosome during mitosis Proc. Natl. Acad. Sci. USA 95 1998 12983 12988
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12983-12988
    • Hsu, L.-C.1    White, R.L.2
  • 22
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • K. Jensen, C. Shiels, and P.S. Freemont PML protein isoforms and the RBCC/TRIM motif Oncogene 20 2001 7223 7233
    • (2001) Oncogene , vol.20 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 24
    • 0032499256 scopus 로고    scopus 로고
    • Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis
    • X.F. Le, S. Vallian, Z.M. Mu, M.C. Hung, and K.S. Chang Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis Oncogene 16 1998 1839 1849
    • (1998) Oncogene , vol.16 , pp. 1839-1849
    • Le X., F.1    Vallian, S.2    Mu, Z.M.3    Hung, M.C.4    Chang, K.S.5
  • 25
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-β signalling
    • H.K. Lin, S. Bergmann, and P.P. Pandolfi Cytoplasmic PML function in TGF-β signalling Nature 431 2004 205 211
    • (2004) Nature , vol.431 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 26
    • 0035969097 scopus 로고    scopus 로고
    • Transcriptional regulation in acute promyelocytic leukemia
    • R.J. Lin, T. Sternsdorf, M. Tini, and R.M. Evans Transcriptional regulation in acute promyelocytic leukemia Oncogene 20 2001 7204 7215
    • (2001) Oncogene , vol.20 , pp. 7204-7215
    • Lin, R.J.1    Sternsdorf, T.2    Tini, M.3    Evans, R.M.4
  • 28
    • 0041856232 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation
    • I. Louria-Hayon, T. Grossman, R.V. Sionov, O. Alsheich, P.P. Pandolfi, and Y. Haupt The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation J. Biol. Chem. 278 2003 33134 33141
    • (2003) J. Biol. Chem. , vol.278 , pp. 33134-33141
    • Louria-Hayon, I.1    Grossman, T.2    Sionov, R.V.3    Alsheich, O.4    Pandolfi, P.P.5    Haupt, Y.6
  • 29
    • 0033557572 scopus 로고    scopus 로고
    • cip-1/waf-1-deficiency causes deformed nuclear architecture, centriole overduplication, polyploidy, and relaxed microtubule damage checkpoints in human hematopoietic cells
    • cip-1/waf-1-deficiency causes deformed nuclear architecture, centriole overduplication, polyploidy, and relaxed microtubule damage checkpoints in human hematopoietic cells Blood 93 1999 1390 1398
    • (1999) Blood , vol.93 , pp. 1390-1398
    • Mantel, C.1    Braun, S.E.2    Reid, S.3    Henegariu, O.4    Liu, L.5    Hangoc, G.6    Broxmeyer, H.E.7
  • 30
    • 0033594469 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 2 (Cdk2) is required for centrosome duplication in mammalian cells
    • Y. Matsumoto, K. Hayashi, and J.L. Maller Cyclin-dependent kinase 2 (Cdk2) is required for centrosome duplication in mammalian cells Curr. Biol. 9 1999 429 432
    • (1999) Curr. Biol. , vol.9 , pp. 429-432
    • Matsumoto, Y.1    Hayashi, K.2    Maller, J.L.3
  • 31
    • 0033561797 scopus 로고    scopus 로고
    • Deconstructing a disease: RARα, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia
    • A. Melnick, and J.D. Licht Deconstructing a disease: RARα, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia Blood 93 1999 3167 3215
    • (1999) Blood , vol.93 , pp. 3167-3215
    • Melnick, A.1    Licht, J.D.2
  • 32
    • 0034749425 scopus 로고    scopus 로고
    • DNA damage-dependent nuclear dynamics of the Mre11 complex
    • O.K. Mirzoeva, and J.H.J. Petrini DNA damage-dependent nuclear dynamics of the Mre11 complex Mol. Cell. Biol. 21 2001 281 288
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 281-288
    • Mirzoeva, O.K.1    Petrini, J.H.J.2
  • 33
    • 0028095410 scopus 로고
    • PML, a growth suppressor disrupted in acute promyelocytic leukemia
    • Z.M. Mu, K.V. Chin, J.H. Liu, G. Lozano, and K.S. Chang PML, a growth suppressor disrupted in acute promyelocytic leukemia Mol. Cell. Biol. 14 1994 6858 6867
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6858-6867
    • Mu, Z.M.1    Chin, K.V.2    Liu, J.H.3    Lozano, G.4    Chang, K.S.5
  • 34
    • 11144219997 scopus 로고    scopus 로고
    • Physical and functional link of the leukemia-associated factors AML1 and PML
    • L.A. Nguyen, P.P. Pandolfi, Y. Aikawa, Y. Tagata, M. Ohki, and I. Kitabayashi Physical and functional link of the leukemia-associated factors AML1 and PML Blood 105 2004 292 300
    • (2004) Blood , vol.105 , pp. 292-300
    • Nguyen, L.A.1    Pandolfi, P.P.2    Aikawa, Y.3    Tagata, Y.4    Ohki, M.5    Kitabayashi, I.6
  • 35
    • 0036831681 scopus 로고    scopus 로고
    • Centrosome aberrations: Cause or consequence of cancer progression?
    • E.A. Nigg Centrosome aberrations: cause or consequence of cancer progression? Nat. Rev. Cancer 2 2002 1 11
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 1-11
    • Nigg, E.A.1
  • 37
    • 1642511792 scopus 로고    scopus 로고
    • TopBP1 localises to centrosomes in mitosis and to chromosome cores in meiosis
    • K. Reini, L. Uitto, D. Perera, P.B. Moens, R. Freire, and J.E. Syvaoja TopBP1 localises to centrosomes in mitosis and to chromosome cores in meiosis Chromosoma 112 2004 323 330
    • (2004) Chromosoma , vol.112 , pp. 323-330
    • Reini, K.1    Uitto, L.2    Perera, D.3    Moens, P.B.4    Freire, R.5    Syvaoja, J.E.6
  • 38
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • P. Salomoni, and P.P. Pandolfi The role of PML in tumor suppression Cell 108 2002 165 170
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 39
    • 0035969102 scopus 로고    scopus 로고
    • SUMO: Of branched proteins and nuclear bodies
    • J.-S. Seeler, and A. Dejean SUMO: of branched proteins and nuclear bodies Oncogene 20 2001 7243 7249
    • (2001) Oncogene , vol.20 , pp. 7243-7249
    • Seeler, J.-S.1    Dejean, A.2
  • 40
    • 0037048323 scopus 로고    scopus 로고
    • Loss of p53 and centrosome hyperamplification
    • T. Tarapore, and K. Fukasawa Loss of p53 and centrosome hyperamplification Oncogene 21 2002 6234 6240
    • (2002) Oncogene , vol.21 , pp. 6234-6240
    • Tarapore, T.1    Fukasawa, K.2
  • 41
    • 0034609753 scopus 로고    scopus 로고
    • The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation
    • A.O. Walter, W. Seghezzi, W. Korver, J. Sheung, and E. Lees The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation Oncogene 19 2000 4906 4916
    • (2000) Oncogene , vol.19 , pp. 4906-4916
    • Walter, A.O.1    Seghezzi, W.2    Korver, W.3    Sheung, J.4    Lees, E.5
  • 43
    • 0030091256 scopus 로고    scopus 로고
    • Failure to unwind causes cancer. Genome stability
    • P.M. Watt, and I.D. Hickson Failure to unwind causes cancer. Genome stability Curr. Biol. 6 1996 265 267
    • (1996) Curr. Biol. , vol.6 , pp. 265-267
    • Watt, P.M.1    Hickson, I.D.2
  • 44
    • 0038146926 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein sensitizes tumor necrosis factor α-induced apoptosis by inhibiting the NF-κB survival pathway
    • W.S. Wu, Z.X. Xu, W.N. Hittelman, P. Salomoni, P.P. Pandolfi, and K.S. Chang Promyelocytic leukemia protein sensitizes tumor necrosis factor α-induced apoptosis by inhibiting the NF-κB survival pathway J. Biol. Chem. 278 2003 12294 12304
    • (2003) J. Biol. Chem. , vol.278 , pp. 12294-12304
    • Wu, W.S.1    Xu, Z.X.2    Hittelman, W.N.3    Salomoni, P.4    Pandolfi, P.P.5    Chang, K.S.6
  • 45
    • 0037979238 scopus 로고    scopus 로고
    • PML colocalizes with and stabilizes the DNA damage response protein TopBP1
    • Z.X. Xu, A. Timanava-Atanasova, R.X. Zhao, and K.S. Chang PML colocalizes with and stabilizes the DNA damage response protein TopBP1 Mol. Cell. Biol. 23 2003 4247 4256
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4247-4256
    • Xu, Z.X.1    Timanava-Atanasova, A.2    Zhao, R.X.3    Chang, K.S.4
  • 46
    • 0345826116 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein 4 induces apoptosis by inhibition of Survivin expression
    • Z.X. Xu, R.X. Zhao, T. Ding, T.T. Tran, W. Zhang, P.P. Pandolfi, and K.S. Chang Promyelocytic leukemia protein 4 induces apoptosis by inhibition of Survivin expression J. Biol. Chem. 279 2004 1838 1844
    • (2004) J. Biol. Chem. , vol.279 , pp. 1838-1844
    • Xu, Z.X.1    Zhao, R.X.2    Ding, T.3    Tran, T.T.4    Zhang, W.5    Pandolfi, P.P.6    Chang, K.S.7
  • 47
    • 0033598931 scopus 로고    scopus 로고
    • A role for PML and the nuclear body in genomic stability
    • S. Zhong, T.Z. Ye, R. Stan, N.A. Ellis, and P.P. Pandolfi A role for PML and the nuclear body in genomic stability Oncogene 18 1999 7841 7847
    • (1999) Oncogene , vol.18 , pp. 7841-7847
    • Zhong, S.1    Ye, T.Z.2    Stan, R.3    Ellis, N.A.4    Pandolfi, P.P.5
  • 48
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • S. Zhong, P. Solomoni, and P.P. Pandolfi The transcriptional role of PML and the nuclear body Nat. Cell Biol. 2 2000 E85 E90
    • (2000) Nat. Cell Biol. , vol.2
    • Zhong, S.1    Solomoni, P.2    Pandolfi, P.P.3
  • 49
    • 0031714080 scopus 로고    scopus 로고
    • Tumor amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation
    • H. Zhou, J. Kuang, L. Zhong, W.L. Kuo, J.W. Gray, A. Sahin, B.R. Brinkley, and S. Sen Tumor amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation Nat. Genet. 20 1998 189 193
    • (1998) Nat. Genet. , vol.20 , pp. 189-193
    • Zhou, H.1    Kuang, J.2    Zhong, L.3    Kuo, W.L.4    Gray, J.W.5    Sahin, A.6    Brinkley, B.R.7    Sen, S.8


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