메뉴 건너뛰기




Volumn 8, Issue 12, 2007, Pages 1006-1016

Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies

Author keywords

[No Author keywords available]

Indexed keywords

ATR PROTEIN; CASEIN KINASE II; CHAPERONE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; DAXX PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MAMMALIAN TARGET OF RAPAMYCIN INHIBITOR; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN KINASE B; STAT PROTEIN; SUMO PROTEIN;

EID: 36448975490     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2277     Document Type: Review
Times cited : (766)

References (123)
  • 1
    • 0033561797 scopus 로고    scopus 로고
    • Melnick, A. & Licht, J. D. Deconstructing a disease: RARα, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia. Blood 93, 3167-3215 (1999). This review on the molecular pathogenesis of APL is a classic. Although some aspects are perhaps outdated, it still provides a broad and detailed description of the functions of the fusion partners of RARα.
    • Melnick, A. & Licht, J. D. Deconstructing a disease: RARα, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia. Blood 93, 3167-3215 (1999). This review on the molecular pathogenesis of APL is a classic. Although some aspects are perhaps outdated, it still provides a broad and detailed description of the functions of the fusion partners of RARα.
  • 2
    • 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, A. M. et al. 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).
    • (1999) J. Cell Biol , vol.147 , pp. 221-234
    • Ishov, A.M.1
  • 3
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni, P. & Pandolfi, P. P. The role of PML in tumor suppression. Cell 108, 165-170 (2002).
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 4
    • 4644351274 scopus 로고    scopus 로고
    • Dellaire, G. & Bazett-Jones, D. P. PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 26, 963-977 (2004). An important review on the structure of PML-NBs and their properties and dynamics in cells exposed to DNA damage.
    • Dellaire, G. & Bazett-Jones, D. P. PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 26, 963-977 (2004). An important review on the structure of PML-NBs and their properties and dynamics in cells exposed to DNA damage.
  • 5
    • 33745316089 scopus 로고    scopus 로고
    • Identification of a tumour suppressor network opposing nuclear Akt function
    • Trotman, L. C. et al. Identification of a tumour suppressor network opposing nuclear Akt function. Nature 441, 523-527 (2006).
    • (2006) Nature , vol.441 , pp. 523-527
    • Trotman, L.C.1
  • 6
    • 33747488399 scopus 로고    scopus 로고
    • PML inhibits HIF-1α translation and neoangiogenesis through repression of mTOR
    • Bernardi, R. et al. PML inhibits HIF-1α translation and neoangiogenesis through repression of mTOR. Nature 442, 779-785 (2006).
    • (2006) Nature , vol.442 , pp. 779-785
    • Bernardi, R.1
  • 7
    • 0026532516 scopus 로고
    • A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies
    • Stuurman, N. et al. A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies. J. Cell Sci. 101, 773-784 (1992).
    • (1992) J. Cell Sci , vol.101 , pp. 773-784
    • Stuurman, N.1
  • 8
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • Boisvert, F. M., Hendzel, M. J. & Bazett-Jones, D. P. Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J. Cell Biol. 148, 283-292 (2000).
    • (2000) J. Cell Biol , vol.148 , pp. 283-292
    • Boisvert, F.M.1    Hendzel, M.J.2    Bazett-Jones, D.P.3
  • 9
    • 1542304599 scopus 로고    scopus 로고
    • Eskiw, C. H., Dellaire, G. & Bazett-Jones, D. P. Chromatin contributes to structural integrity of promyelocytic leukemia bodies through a SUMO-1-independent mechanism. J. Biol. Chem. 279, 9577-9585 (2004). The authors of this report used a combination of correlative fluorescence microscopy and electron spectroscopic imaging to demonstrate that the integrity of PML-NBs is maintained through contacts with surrounding chromatin fibres.
    • Eskiw, C. H., Dellaire, G. & Bazett-Jones, D. P. Chromatin contributes to structural integrity of promyelocytic leukemia bodies through a SUMO-1-independent mechanism. J. Biol. Chem. 279, 9577-9585 (2004). The authors of this report used a combination of correlative fluorescence microscopy and electron spectroscopic imaging to demonstrate that the integrity of PML-NBs is maintained through contacts with surrounding chromatin fibres.
  • 11
    • 0036318221 scopus 로고    scopus 로고
    • Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions for PML nuclear bodies
    • Borden, K. L. Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies. Mol. Cell. Biol. 22, 5259-5269 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 5259-5269
    • Borden, K.L.1
  • 12
    • 0029805916 scopus 로고    scopus 로고
    • PML-containing nuclear bodies: Their spatial distribution in relation to other nuclear components
    • Grande, M. A. et al. PML-containing nuclear bodies: their spatial distribution in relation to other nuclear components. J. Cell. Biochem. 63, 280-291 (1996).
    • (1996) J. Cell. Biochem , vol.63 , pp. 280-291
    • Grande, M.A.1
  • 13
    • 1242329998 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies associate with transcriptionally active genomic regions
    • Wang, J. et al. Promyelocytic leukemia nuclear bodies associate with transcriptionally active genomic regions. J. Cell Biol. 164, 515-526 (2004).
    • (2004) J. Cell Biol , vol.164 , pp. 515-526
    • Wang, J.1
  • 14
    • 0034759620 scopus 로고    scopus 로고
    • PML bodies associate specifically with the MHC gene cluster in interphase nuclei
    • Shiels, C. et al. PML bodies associate specifically with the MHC gene cluster in interphase nuclei. J. Cell Sci. 114, 3705-3716 (2001).
    • (2001) J. Cell Sci , vol.114 , pp. 3705-3716
    • Shiels, C.1
  • 15
    • 33845871732 scopus 로고    scopus 로고
    • Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus
    • Kumar, P. P. et al. Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus. Nature Cell Biol. 9, 45-56 (2007).
    • (2007) Nature Cell Biol , vol.9 , pp. 45-56
    • Kumar, P.P.1
  • 16
    • 0038386615 scopus 로고    scopus 로고
    • Specific interaction of PML bodies with the TP53 locus in Jurkat interphase nuclei
    • Sun, Y., Durrin, L. K. & Krontiris, T. G. Specific interaction of PML bodies with the TP53 locus in Jurkat interphase nuclei. Genomics 82, 250-252 (2003).
    • (2003) Genomics , vol.82 , pp. 250-252
    • Sun, Y.1    Durrin, L.K.2    Krontiris, T.G.3
  • 17
    • 33749157645 scopus 로고    scopus 로고
    • Nuclear and chromatin reorganization in the MHCOct3/ 4 locus at developmental phases of embryonic stem cell differentiation
    • Aoto, T., Saitoh, N., Ichimura, T., Niwa, H. & Nakao, M. Nuclear and chromatin reorganization in the MHCOct3/ 4 locus at developmental phases of embryonic stem cell differentiation. Dev. Biol. 298, 354-367 (2006).
    • (2006) Dev. Biol , vol.298 , pp. 354-367
    • Aoto, T.1    Saitoh, N.2    Ichimura, T.3    Niwa, H.4    Nakao, M.5
  • 18
    • 0037206267 scopus 로고    scopus 로고
    • Proto-oncogene PML enhances antigen presentation by MHC class I molecules in human lung cancer cells
    • Chang, S. K. et al. Proto-oncogene PML enhances antigen presentation by MHC class I molecules in human lung cancer cells. Mol. Cells 14, 130-135 (2002).
    • (2002) Mol. Cells , vol.14 , pp. 130-135
    • Chang, S.K.1
  • 19
    • 0037866466 scopus 로고    scopus 로고
    • The PML gene is not involved in the regulation of MHC class I expression in human cell lines
    • Bruno, S. et al. The PML gene is not involved in the regulation of MHC class I expression in human cell lines. Blood 101, 3514-3519 (2003).
    • (2003) Blood , vol.101 , pp. 3514-3519
    • Bruno, S.1
  • 20
    • 0032844040 scopus 로고    scopus 로고
    • Alteration of the PML protooncogene in leukemic cells does not abrogate expression of MHC class I antigens
    • Larghero, J. et al. Alteration of the PML protooncogene in leukemic cells does not abrogate expression of MHC class I antigens. Leukemia 13, 1295-1296 (1999).
    • (1999) Leukemia , vol.13 , pp. 1295-1296
    • Larghero, J.1
  • 21
    • 3042701410 scopus 로고    scopus 로고
    • Concordant down-regulation of protooncogene PML and major histocompatibility antigen HLA class I expression in high-grade prostate cancer
    • Zhang, H. et al. Concordant down-regulation of protooncogene PML and major histocompatibility antigen HLA class I expression in high-grade prostate cancer. Cancer Immun. 3, 2 (2003).
    • (2003) Cancer Immun , vol.3 , pp. 2
    • Zhang, H.1
  • 22
    • 2442568547 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are disorganized in colorectal tumors with total loss of major histocompatibility complex class I expression and LMP7 downregulation
    • Cabrera, C. M., Jimenez, P., Concha, A., Garrido, F. & Ruiz-Cabello, F. Promyelocytic leukemia (PML) nuclear bodies are disorganized in colorectal tumors with total loss of major histocompatibility complex class I expression and LMP7 downregulation. Tissue Antigens 63, 446-452 (2004).
    • (2004) Tissue Antigens , vol.63 , pp. 446-452
    • Cabrera, C.M.1    Jimenez, P.2    Concha, A.3    Garrido, F.4    Ruiz-Cabello, F.5
  • 23
    • 1342291118 scopus 로고    scopus 로고
    • Gurrieri, C. et al. Loss of the tumor suppressor PML in human cancers of multiple histologic origins. J. Natl Cancer Inst. 96, 269-279 (2004). A systematic analysis of PML expression in various tumours of different histological origin allowed the authors to affirm that PML and PML-NBs are lost in some tumours and that, in some cases, this correlates with disease progression.
    • Gurrieri, C. et al. Loss of the tumor suppressor PML in human cancers of multiple histologic origins. J. Natl Cancer Inst. 96, 269-279 (2004). A systematic analysis of PML expression in various tumours of different histological origin allowed the authors to affirm that PML and PML-NBs are lost in some tumours and that, in some cases, this correlates with disease progression.
  • 24
    • 0028916423 scopus 로고
    • The PML growth-suppressor has an altered expression in human oncogenesis
    • Koken, M. H. et al. The PML growth-suppressor has an altered expression in human oncogenesis. Oncogene 10, 1315-1324 (1995).
    • (1995) Oncogene , vol.10 , pp. 1315-1324
    • Koken, M.H.1
  • 25
    • 10544236906 scopus 로고    scopus 로고
    • Heterogeneous nuclear expression of the promyelocytic leukemia (PML) protein in normal and neoplastic human tissues
    • Gambacorta, M. et al. Heterogeneous nuclear expression of the promyelocytic leukemia (PML) protein in normal and neoplastic human tissues. Am. J. Pathol. 149, 2023-2035 (1996).
    • (1996) Am. J. Pathol , vol.149 , pp. 2023-2035
    • Gambacorta, M.1
  • 26
    • 0028966628 scopus 로고
    • Characterization of a new monoclonal antibody (PG-M3) directed against the aminoterminal portion of the PML gene product: Immunocytochemical evidence for high expression of PML proteins on activated macrophages, endothelial cells, and epithelia
    • Flenghi, L. et al. Characterization of a new monoclonal antibody (PG-M3) directed against the aminoterminal portion of the PML gene product: immunocytochemical evidence for high expression of PML proteins on activated macrophages, endothelial cells, and epithelia. Blood 85, 1871-1880 (1995).
    • (1995) Blood , vol.85 , pp. 1871-1880
    • Flenghi, L.1
  • 27
    • 0032035436 scopus 로고    scopus 로고
    • A novel nuclear substructure, ND10: Distribution in normal and neoplastic human tissues
    • Cho, Y., Lee, I., Maul, G. G. & Yu, E. A novel nuclear substructure, ND10: distribution in normal and neoplastic human tissues. Int. J. Mol. Med. 1, 717-724 (1998).
    • (1998) Int. J. Mol. Med , vol.1 , pp. 717-724
    • Cho, Y.1    Lee, I.2    Maul, G.G.3    Yu, E.4
  • 28
    • 0028951531 scopus 로고
    • PML nuclear bodies are general targets for inflammation and cell proliferation
    • Terris, B. et al. PML nuclear bodies are general targets for inflammation and cell proliferation. Cancer Res. 55, 1590-1597 (1995).
    • (1995) Cancer Res , vol.55 , pp. 1590-1597
    • Terris, B.1
  • 29
    • 27244444559 scopus 로고    scopus 로고
    • TRIM family proteins: Retroviral restriction and antiviral defence
    • Nisole, S., Stoye, J. P. & Saib, A. TRIM family proteins: retroviral restriction and antiviral defence. Nature Rev. Microbiol. 3, 799-808 (2005).
    • (2005) Nature Rev. Microbiol , vol.3 , pp. 799-808
    • Nisole, S.1    Stoye, J.P.2    Saib, A.3
  • 30
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: Implications in antiviral defence
    • Everett, R. D. & Chelbi-Alix, M. K. PML and PML nuclear bodies: Implications in antiviral defence. Biochimie 89, 819-830 (2007).
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 31
    • 33845473249 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein functions as a negative regulator of IFN-γ signaling
    • Choi, Y. H., Bernardi, R., Pandolfi, P. P. & Benveniste, E. N. The promyelocytic leukemia protein functions as a negative regulator of IFN-γ signaling. Proc. Natl Acad. Sci. USA 103, 18715-18720 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 18715-18720
    • Choi, Y.H.1    Bernardi, R.2    Pandolfi, P.P.3    Benveniste, E.N.4
  • 32
    • 0029560027 scopus 로고
    • Transcriptional induction of the PML growth suppressor gene by interferons is mediated through an ISRE and a GAS element
    • Stadler, M. et al. Transcriptional induction of the PML growth suppressor gene by interferons is mediated through an ISRE and a GAS element. Oncogene 11, 2565-2573 (1995).
    • (1995) Oncogene , vol.11 , pp. 2565-2573
    • Stadler, M.1
  • 33
    • 34247174887 scopus 로고    scopus 로고
    • Dror, N. et al. Interferon regulatory factor-8 is indispensable for the expression of promyelocytic leukemia and the formation of nuclear bodies in myeloid cells. J. Biol. Chem. 282, 5633-5640 (2007). This paper shows that a loss of expression of IRF8 in human CML correlates with a loss of expression of PML. This is also the first report to demonstrate that loss of expression of PML can be detected in leukaemias in addition to solid tumours.
    • Dror, N. et al. Interferon regulatory factor-8 is indispensable for the expression of promyelocytic leukemia and the formation of nuclear bodies in myeloid cells. J. Biol. Chem. 282, 5633-5640 (2007). This paper shows that a loss of expression of IRF8 in human CML correlates with a loss of expression of PML. This is also the first report to demonstrate that loss of expression of PML can be detected in leukaemias in addition to solid tumours.
  • 34
    • 0030917324 scopus 로고    scopus 로고
    • Altered distribution of the promyelocytic leukemia-associated protein is associated with cellular senescence
    • Jiang, W. Q. & Ringertz, N. Altered distribution of the promyelocytic leukemia-associated protein is associated with cellular senescence. Cell Growth Differ. 8, 513-522 (1997).
    • (1997) Cell Growth Differ , vol.8 , pp. 513-522
    • Jiang, W.Q.1    Ringertz, N.2
  • 35
    • 0034644274 scopus 로고    scopus 로고
    • PML regulates p53 acetylation and premature senescence induced by oncogenic Ras
    • Pearson, M. et al. PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406, 207-210 (2000).
    • (2000) Nature , vol.406 , pp. 207-210
    • Pearson, M.1
  • 36
    • 0034663873 scopus 로고    scopus 로고
    • Ferbeyre, G. et al. PML is induced by oncogenic ras and promotes premature senescence. Genes Dev. 14, 2015-2027 (2000). References 35 and 36 are the first reports that implicate PML-NBs in the regulation of cellular senescence. They show that PML-NBs increase in size and number following the induction of senescence and that PML regulates p53 acetylation and activation.
    • Ferbeyre, G. et al. PML is induced by oncogenic ras and promotes premature senescence. Genes Dev. 14, 2015-2027 (2000). References 35 and 36 are the first reports that implicate PML-NBs in the regulation of cellular senescence. They show that PML-NBs increase in size and number following the induction of senescence and that PML regulates p53 acetylation and activation.
  • 37
    • 1542285168 scopus 로고    scopus 로고
    • PML is a direct p53 target that modulates p53 effector functions
    • de Stanchina, E. et al. PML is a direct p53 target that modulates p53 effector functions. Mol. Cell 13, 523-535 (2004).
    • (2004) Mol. Cell , vol.13 , pp. 523-535
    • de Stanchina, E.1
  • 38
    • 0029010740 scopus 로고
    • The PML gene encodes a phosphoprotein associated with the nuclear matrix
    • Chang, K. S., Fan, Y. H., Andreeff, M., Liu, J. & Mu, Z. M. The PML gene encodes a phosphoprotein associated with the nuclear matrix. Blood 85, 3646-3653 (1995).
    • (1995) Blood , vol.85 , pp. 3646-3653
    • Chang, K.S.1    Fan, Y.H.2    Andreeff, M.3    Liu, J.4    Mu, Z.M.5
  • 39
    • 1842785771 scopus 로고    scopus 로고
    • Phosphorylation of PML by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis
    • Hayakawa, F. & Privalsky, M. L. Phosphorylation of PML by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis. Cancer Cell 5, 389-401 (2004).
    • (2004) Cancer Cell , vol.5 , pp. 389-401
    • Hayakawa, F.1    Privalsky, M.L.2
  • 40
    • 3242726103 scopus 로고    scopus 로고
    • PML regulates p53 stability by sequestering Mdm2 to the nucleolus
    • Bernardi, R. et al. PML regulates p53 stability by sequestering Mdm2 to the nucleolus. Nature Cell Biol. 6, 665-672 (2004).
    • (2004) Nature Cell Biol , vol.6 , pp. 665-672
    • Bernardi, R.1
  • 41
    • 0036847998 scopus 로고    scopus 로고
    • PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2
    • Yang, S., Kuo, C., Bisi, J. E. & Kim, M. K. PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2. Nature Cell Biol. 4, 865-870 (2002).
    • (2002) Nature Cell Biol , vol.4 , pp. 865-870
    • Yang, S.1    Kuo, C.2    Bisi, J.E.3    Kim, M.K.4
  • 42
    • 33746208870 scopus 로고    scopus 로고
    • A CK2-dependent mechanism for degradation of the PML tumor suppressor
    • Scaglioni, P. P. et al. A CK2-dependent mechanism for degradation of the PML tumor suppressor. Cell 126, 269-283 (2006).
    • (2006) Cell , vol.126 , pp. 269-283
    • Scaglioni, P.P.1
  • 43
    • 0033034749 scopus 로고    scopus 로고
    • SUMO-1 modification of the acute promyelocytic leukaemia protein PML: Implications for nuclear localisation
    • Duprez, E. et al. SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation. J. Cell Sci. 112, 381-393 (1999).
    • (1999) J. Cell Sci , vol.112 , pp. 381-393
    • Duprez, E.1
  • 44
    • 0343776952 scopus 로고    scopus 로고
    • Role of SUMO-1-modified PML in nuclear body formation
    • Zhong, S. et al. Role of SUMO-1-modified PML in nuclear body formation. Blood 95, 2748-2752 (2000).
    • (2000) Blood , vol.95 , pp. 2748-2752
    • Zhong, S.1
  • 45
    • 0036809116 scopus 로고    scopus 로고
    • SUMO-1 protease-1 regulates gene transcription through PML
    • Best, J. L. et al. SUMO-1 protease-1 regulates gene transcription through PML. Mol. Cell 10, 843-855 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 843-855
    • Best, J.L.1
  • 46
    • 0037327059 scopus 로고    scopus 로고
    • 2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 and 25 differently
    • 2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 and 25 differently. J. Cell Sci. 116, 513-524 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 513-524
    • Nefkens, I.1
  • 47
    • 15644368249 scopus 로고    scopus 로고
    • Covalent modification of PML by the sentrin family of ubiquitin-like proteins
    • Kamitani, T., Nguyen, H. P., Kito, K., Fukuda-Kamitani, T. & Yeh, E. T. Covalent modification of PML by the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273, 3117-3120 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 3117-3120
    • Kamitani, T.1    Nguyen, H.P.2    Kito, K.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 48
    • 9444260454 scopus 로고    scopus 로고
    • Distinct in vivo dynamics of vertebrate SUMO paralogues
    • Ayaydin, F. & Dasso, M. Distinct in vivo dynamics of vertebrate SUMO paralogues. Mol. Biol. Cell 15, 5208-5218 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5208-5218
    • Ayaydin, F.1    Dasso, M.2
  • 49
    • 24644522876 scopus 로고    scopus 로고
    • Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3
    • Fu, C. et al. Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3. Oncogene 24, 5401-5413 (2005).
    • (2005) Oncogene , vol.24 , pp. 5401-5413
    • Fu, C.1
  • 50
    • 33748990136 scopus 로고    scopus 로고
    • SUSP1 antagonizes formation of highly SUMO2/3-conjugated species
    • Mukhopadhyay, D. et al. SUSP1 antagonizes formation of highly SUMO2/3-conjugated species. J. Cell Biol. 174, 939-949 (2006).
    • (2006) J. Cell Biol , vol.174 , pp. 939-949
    • Mukhopadhyay, D.1
  • 51
    • 28444448039 scopus 로고    scopus 로고
    • Nacerddine, K. et al. The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice. Dev. Cell 9, 769-779 (2005). Describes the generation of mice that are deficient for the SUMO E2-conjugating enzyme UBC9. Loss of UBC9 leads to early embryonic lethality and major defects in chromosome condensation and segregation. Moreover, PML-NBs are disrupted along with other nuclear structures.
    • Nacerddine, K. et al. The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice. Dev. Cell 9, 769-779 (2005). Describes the generation of mice that are deficient for the SUMO E2-conjugating enzyme UBC9. Loss of UBC9 leads to early embryonic lethality and major defects in chromosome condensation and segregation. Moreover, PML-NBs are disrupted along with other nuclear structures.
  • 52
    • 33750447586 scopus 로고    scopus 로고
    • Shen, T. H., Lin, H. K., Scaglioni, P. P., Yung, T. M. & Pandolfi, P. P. The mechanisms of PML-nuclear body formation. Mol. Cell 24, 331-339 (2006). PML is shown to have a SUMO-binding domain that is necessary for PML-NB formation. A model for the nucleation of PML-NBs is presented.
    • Shen, T. H., Lin, H. K., Scaglioni, P. P., Yung, T. M. & Pandolfi, P. P. The mechanisms of PML-nuclear body formation. Mol. Cell 24, 331-339 (2006). PML is shown to have a SUMO-binding domain that is necessary for PML-NB formation. A model for the nucleation of PML-NBs is presented.
  • 53
    • 33646031179 scopus 로고    scopus 로고
    • In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies
    • Saitoh, N. et al. In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies. Exp. Cell Res. 312, 1418-1430 (2006).
    • (2006) Exp. Cell Res , vol.312 , pp. 1418-1430
    • Saitoh, N.1
  • 54
    • 33646859205 scopus 로고    scopus 로고
    • Quimby, B. B., Yong-Gonzalez, V., Anan, T., Strunnikov, A. V. & Dasso, M. The promyelocytic leukemia protein stimulates SUMO conjugation in yeast. Oncogene 25, 2999-3005 (2006). So far, this is the only report to show that the expression of PML in yeast can promote sumoylation activity in vivo and in vitro and that this activity depends on the RING domain of PML.
    • Quimby, B. B., Yong-Gonzalez, V., Anan, T., Strunnikov, A. V. & Dasso, M. The promyelocytic leukemia protein stimulates SUMO conjugation in yeast. Oncogene 25, 2999-3005 (2006). So far, this is the only report to show that the expression of PML in yeast can promote sumoylation activity in vivo and in vitro and that this activity depends on the RING domain of PML.
  • 56
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
    • Sternsdorf, T., Jensen, K. & Will, H. Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 139, 1621-1634 (1997).
    • (1997) J. Cell Biol , vol.139 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 57
    • 33645749156 scopus 로고    scopus 로고
    • Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in G1
    • Dellaire, G., Eskiw, C. H., Dehghani, H., Ching, R. W. & Bazett-Jones, D. P. Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in G1. J. Cell Sci. 119, 1034-1042 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 1034-1042
    • Dellaire, G.1    Eskiw, C.H.2    Dehghani, H.3    Ching, R.W.4    Bazett-Jones, D.P.5
  • 58
    • 34250214907 scopus 로고    scopus 로고
    • SUMOrganization of the nucleus
    • Heun, P. SUMOrganization of the nucleus. Curr. Opin. Cell Biol. 19, 350-355 (2007).
    • (2007) Curr. Opin. Cell Biol , vol.19 , pp. 350-355
    • Heun, P.1
  • 59
    • 33750491062 scopus 로고    scopus 로고
    • Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors
    • Lin, D. Y. et al. Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol. Cell 24, 341-354 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 341-354
    • Lin, D.Y.1
  • 60
    • 0036170782 scopus 로고    scopus 로고
    • Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus
    • Muratani, M. et al. Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus. Nature Cell Biol. 4, 106-110 (2002).
    • (2002) Nature Cell Biol , vol.4 , pp. 106-110
    • Muratani, M.1
  • 61
    • 0242550970 scopus 로고    scopus 로고
    • Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly
    • Eskiw, C. H., Dellaire, G., Mymryk, J. & Bazett-Jones, D. P. Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly. J. Cell Sci. 116, 4455-4466 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 4455-4466
    • Eskiw, C.H.1    Dellaire, G.2    Mymryk, J.3    Bazett-Jones, D.P.4
  • 62
    • 0036966365 scopus 로고    scopus 로고
    • Mobile foci of Sp100 do not contain PML: PML bodies are immobile but PML and Sp100 proteins are not
    • Wiesmeijer, K., Molenaar, C., Bekeer, I. M., Tanke, H. J. & Dirks, R. W. Mobile foci of Sp100 do not contain PML: PML bodies are immobile but PML and Sp100 proteins are not. J. Struct. Biol. 140, 180-188 (2002).
    • (2002) J. Struct. Biol , vol.140 , pp. 180-188
    • Wiesmeijer, K.1    Molenaar, C.2    Bekeer, I.M.3    Tanke, H.J.4    Dirks, R.W.5
  • 63
    • 0035908032 scopus 로고    scopus 로고
    • 3-induced PML or PML/retinoic acid receptor α degradation
    • 3-induced PML or PML/retinoic acid receptor α degradation. J. Exp. Med. 193, 1361-1371 (2001).
    • (2001) J. Exp. Med , vol.193 , pp. 1361-1371
    • Lallemand-Breitenbach, V.1
  • 64
    • 0033549496 scopus 로고    scopus 로고
    • Intracellular localization of proteasomal degradation of a viral antigen
    • Anton, L. C. et al. Intracellular localization of proteasomal degradation of a viral antigen. J. Cell Biol. 146, 113-124 (1999).
    • (1999) J. Cell Biol , vol.146 , pp. 113-124
    • Anton, L.C.1
  • 65
    • 0036968725 scopus 로고    scopus 로고
    • Proteasome-dependent processing of nuclear proteins is correlated with their subnuclear localization
    • Dino Rockel, T. & von Mikecz, A. Proteasome-dependent processing of nuclear proteins is correlated with their subnuclear localization. J. Struct. Biol. 140, 189-199 (2002).
    • (2002) J. Struct. Biol , vol.140 , pp. 189-199
    • Dino Rockel, T.1    von Mikecz, A.2
  • 66
    • 0033672197 scopus 로고    scopus 로고
    • Visualization of gene activity in living cells
    • Tsukamoto, T. et al. Visualization of gene activity in living cells. Nature Cell Biol. 2, 871-878 (2000).
    • (2000) Nature Cell Biol , vol.2 , pp. 871-878
    • Tsukamoto, T.1
  • 67
    • 33645731002 scopus 로고    scopus 로고
    • The number of PML nuclear bodies increases in early S phase by a fission mechanism
    • Dellaire, G., Ching, R. W., Dehghani, H., Ren, Y. & Bazett-Jones, D. P. The number of PML nuclear bodies increases in early S phase by a fission mechanism. J. Cell Sci. 119, 1026-1033 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 1026-1033
    • Dellaire, G.1    Ching, R.W.2    Dehghani, H.3    Ren, Y.4    Bazett-Jones, D.P.5
  • 68
    • 0033598931 scopus 로고    scopus 로고
    • A role for PML and the nuclear body in genomic stability
    • Zhong, S. et al. A role for PML and the nuclear body in genomic stability. Oncogene 18, 7941-7947 (1999).
    • (1999) Oncogene , vol.18 , pp. 7941-7947
    • Zhong, S.1
  • 69
    • 0035980070 scopus 로고    scopus 로고
    • Functional interaction of p53 and BLM DNA helicase in apoptosis
    • Wang, X. W. et al. Functional interaction of p53 and BLM DNA helicase in apoptosis. J. Biol. Chem. 276, 32948-32955 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 32948-32955
    • Wang, X.W.1
  • 70
    • 0035897415 scopus 로고    scopus 로고
    • Regulation and localization of the Bloom syndrome protein in response to DNA damage
    • Bischof, O. et al. Regulation and localization of the Bloom syndrome protein in response to DNA damage. J. Cell Biol. 153, 367-380 (2001).
    • (2001) J. Cell Biol , vol.153 , pp. 367-380
    • Bischof, O.1
  • 71
    • 0033380850 scopus 로고    scopus 로고
    • Cell cycle regulation of PML modification and ND10 composition
    • Everett, R. D., Lomonte, P., Sternsdorf, T., van Driel, R. & Orr, A. Cell cycle regulation of PML modification and ND10 composition. J. Cell Sci. 112, 4581-4588 (1999).
    • (1999) J. Cell Sci , vol.112 , pp. 4581-4588
    • Everett, R.D.1    Lomonte, P.2    Sternsdorf, T.3    van Driel, R.4    Orr, A.5
  • 72
    • 0029583591 scopus 로고
    • Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress
    • Maul, G. G., Yu, E., Ishov, A. M. & Epstein, A. L. Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress. J. Cell. Biochem. 59, 498-513 (1995).
    • (1995) J. Cell. Biochem , vol.59 , pp. 498-513
    • Maul, G.G.1    Yu, E.2    Ishov, A.M.3    Epstein, A.L.4
  • 73
    • 18244405576 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein PML regulates c-Jun function in response to DNA damage
    • Salomoni, P. et al. The promyelocytic leukemia protein PML regulates c-Jun function in response to DNA damage. Blood 105, 3686-3690 (2005).
    • (2005) Blood , vol.105 , pp. 3686-3690
    • Salomoni, P.1
  • 74
    • 0037457077 scopus 로고    scopus 로고
    • UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML
    • Seker, H. et al. UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML. Oncogene 22, 1620-1628 (2003).
    • (2003) Oncogene , vol.22 , pp. 1620-1628
    • Seker, H.1
  • 75
    • 0942290414 scopus 로고    scopus 로고
    • Proteasome-dependent dispersal of PML nuclear bodies in response to alkylating DNA damage
    • Conlan, L. A., McNees, C. J. & Heierhorst, J. Proteasome-dependent dispersal of PML nuclear bodies in response to alkylating DNA damage. Oncogene 23, 307-310 (2004).
    • (2004) Oncogene , vol.23 , pp. 307-310
    • Conlan, L.A.1    McNees, C.J.2    Heierhorst, J.3
  • 76
    • 0037034829 scopus 로고    scopus 로고
    • NBs associate with the hMre11 complex and p53 at sites of irradiation induced DNA damage
    • Carbone, R., Pearson, M., Minucci, S. & Pelicci, P. G. PML NBs associate with the hMre11 complex and p53 at sites of irradiation induced DNA damage. Oncogene 21, 1633-1640 (2002).
    • (2002) Oncogene , vol.21 , pp. 1633-1640
    • Carbone, R.1    Pearson, M.2    Minucci, S.3    Pelicci, P.G.P.4
  • 77
    • 33749547681 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR
    • Dellaire, G. et al. Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR. J. Cell Biol. 175, 55-66 (2006).
    • (2006) J. Cell Biol , vol.175 , pp. 55-66
    • Dellaire, G.1
  • 78
    • 34249938802 scopus 로고    scopus 로고
    • PML protein association with specific nucleolar structures differs in normal, tumor and senescent human cells
    • Janderova-Rossmeislova, L. et al. PML protein association with specific nucleolar structures differs in normal, tumor and senescent human cells. J. Struct. Biol. 159, 56-70 (2007).
    • (2007) J. Struct. Biol , vol.159 , pp. 56-70
    • Janderova-Rossmeislova, L.1
  • 79
    • 0142106346 scopus 로고    scopus 로고
    • Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization
    • Kurki, S., Latonen, L. & Laiho, M. Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization. J. Cell Sci. 116, 3917-3925 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 3917-3925
    • Kurki, S.1    Latonen, L.2    Laiho, M.3
  • 80
    • 0037255042 scopus 로고    scopus 로고
    • The Nuclear Protein Database (NPD): Sub-nuclear localisation and functional annotation of the nuclear proteome
    • Dellaire, G., Farrall, R. & Bickmore, W. A. The Nuclear Protein Database (NPD): sub-nuclear localisation and functional annotation of the nuclear proteome. Nucleic Acids Res. 31, 328-330 (2003).
    • (2003) Nucleic Acids Res , vol.31 , pp. 328-330
    • Dellaire, G.1    Farrall, R.2    Bickmore, W.A.3
  • 81
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong, S., Salomoni, P. & Pandolfi, P. P. The transcriptional role of PML and the nuclear body. Nature Cell Biol. 2, E85-E90 (2000).
    • (2000) Nature Cell Biol , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 82
    • 33745728153 scopus 로고    scopus 로고
    • Condemine, W. et al. Characterization of endogenous human promyelocytic leukemia isoforms. Cancer Res. 66, 6192-6198 (2006). The first report in which the generation of specific antibodies against different isoforms of PML is described. All PML isoforms are shown to be expressed in vivo.
    • Condemine, W. et al. Characterization of endogenous human promyelocytic leukemia isoforms. Cancer Res. 66, 6192-6198 (2006). The first report in which the generation of specific antibodies against different isoforms of PML is described. All PML isoforms are shown to be expressed in vivo.
  • 83
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-β signalling
    • Lin, H. K., Bergmann, S. & Pandolfi, P. P. Cytoplasmic PML function in TGF-β signalling. Nature 431, 205-211 (2004).
    • (2004) Nature , vol.431 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 84
    • 1842609780 scopus 로고    scopus 로고
    • Repression of PML nuclear body-associated transcription by oxidative stress-activated Bach2
    • Tashiro, S. et al. Repression of PML nuclear body-associated transcription by oxidative stress-activated Bach2. Mol. Cell. Biol. 24, 3473-3484 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 3473-3484
    • Tashiro, S.1
  • 85
    • 2442704958 scopus 로고    scopus 로고
    • Cell cycle-dependent association of PML bodies with sites of active transcription in nuclei of mammalian cells
    • Kiesslich, A., von Mikecz, A. & Hemmerich, P. Cell cycle-dependent association of PML bodies with sites of active transcription in nuclei of mammalian cells. J. Struct. Biol. 140, 167-179 (2002).
    • (2002) J. Struct. Biol , vol.140 , pp. 167-179
    • Kiesslich, A.1    von Mikecz, A.2    Hemmerich, P.3
  • 86
    • 0032560477 scopus 로고    scopus 로고
    • Interaction of SP100 with HP1 proteins: A link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment
    • Seeler, J. S., Marchio, A., Sitterlin, D., Transy, C. & Dejean, A. Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc. Natl Acad. Sci. USA 95, 7316-7321 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7316-7321
    • Seeler, J.S.1    Marchio, A.2    Sitterlin, D.3    Transy, C.4    Dejean, A.5
  • 87
    • 0032744386 scopus 로고    scopus 로고
    • A dynamic connection between centromeres and ND10 proteins
    • Everett, R. D. et al. A dynamic connection between centromeres and ND10 proteins. J. Cell Sci. 112, 3443-3454 (1999).
    • (1999) J. Cell Sci , vol.112 , pp. 3443-3454
    • Everett, R.D.1
  • 88
    • 33746073030 scopus 로고    scopus 로고
    • PML nuclear bodies are highly organised DNA-protein structures with a function in heterochromatin remodelling at the G2 phase
    • Luciani, J. J. et al. PML nuclear bodies are highly organised DNA-protein structures with a function in heterochromatin remodelling at the G2 phase. J. Cell Sci. 119, 2518-2531 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 2518-2531
    • Luciani, J.J.1
  • 89
    • 19944427674 scopus 로고    scopus 로고
    • Formation of macroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA
    • Zhang, R. et al. Formation of macroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA. Dev. Cell 8, 19-30 (2005).
    • (2005) Dev. Cell , vol.8 , pp. 19-30
    • Zhang, R.1
  • 90
    • 34147143631 scopus 로고    scopus 로고
    • Definition of pRB- and p53-dependent and independent steps in HIRA/ASF1a-mediated formation of senecence-associated heterochromatin foci (SAHF)
    • Ye, X. et al. Definition of pRB- and p53-dependent and independent steps in HIRA/ASF1a-mediated formation of senecence-associated heterochromatin foci (SAHF). Mol. Cell. Biol. 27, 2452-2465 (2007).
    • (2007) Mol. Cell. Biol , vol.27 , pp. 2452-2465
    • Ye, X.1
  • 91
    • 0036646102 scopus 로고    scopus 로고
    • Deconstructing PML-induced premature senescence
    • Bischof, O. et al. Deconstructing PML-induced premature senescence. EMBO J. 21, 3358-3369 (2002).
    • (2002) EMBO J , vol.21 , pp. 3358-3369
    • Bischof, O.1
  • 92
    • 19544380887 scopus 로고    scopus 로고
    • Isoforms of the promyelocytic leukemia protein differ in their effects on ND10 organization
    • Beech, S. J., Lethbridge, K. J., Killick, N., McGlincy, N. & Leppard, K. N. Isoforms of the promyelocytic leukemia protein differ in their effects on ND10 organization. Exp. Cell Res. 307, 109-117 (2005).
    • (2005) Exp. Cell Res , vol.307 , pp. 109-117
    • Beech, S.J.1    Lethbridge, K.J.2    Killick, N.3    McGlincy, N.4    Leppard, K.N.5
  • 93
    • 33748794780 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies are predetermined processing sites for damaged DNA
    • Boe, S. O. et al. Promyelocytic leukemia nuclear bodies are predetermined processing sites for damaged DNA. J. Cell Sci. 119, 3284-3295 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 3284-3295
    • Boe, S.O.1
  • 94
    • 0033199695 scopus 로고    scopus 로고
    • Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body
    • Yeager, T. R. et al. Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body. Cancer Res. 59, 4175-4179 (1999).
    • (1999) Cancer Res , vol.59 , pp. 4175-4179
    • Yeager, T.R.1
  • 96
    • 0037979238 scopus 로고    scopus 로고
    • PML colocalizes with and stabilizes the DNA damage response protein TopBP1
    • Xu, Z. X., Timanova-Atanasova, A., Zhao, R. X. & Chang, K. S. PML colocalizes with and stabilizes the DNA damage response protein TopBP1. Mol. Cell. Biol. 23, 4247-4256 (2003).
    • (2003) Mol. Cell. Biol , vol.23 , pp. 4247-4256
    • Xu, Z.X.1    Timanova-Atanasova, A.2    Zhao, R.X.3    Chang, K.S.4
  • 97
    • 1642512435 scopus 로고    scopus 로고
    • Role of PML and the PML-nuclear body in the control of programmed cell death
    • Bernardi, R. & Pandolfi, P. P. Role of PML and the PML-nuclear body in the control of programmed cell death. Oncogene 22, 9048-9057 (2003).
    • (2003) Oncogene , vol.22 , pp. 9048-9057
    • Bernardi, R.1    Pandolfi, P.P.2
  • 98
    • 27744527486 scopus 로고    scopus 로고
    • The first molecular details of ALT in human tumor cells
    • Muntoni, A. & Reddel, R. R. The first molecular details of ALT in human tumor cells. Hum. Mol. Genet. 14, R191-R196 (2005).
    • (2005) Hum. Mol. Genet , vol.14
    • Muntoni, A.1    Reddel, R.R.2
  • 100
    • 33748747143 scopus 로고    scopus 로고
    • Promyelocytic leukemia activates Chk2 by mediating Chk2 autophosphorylation
    • Yang, S. et al. Promyelocytic leukemia activates Chk2 by mediating Chk2 autophosphorylation. J. Biol. Chem. 281, 26645-26654 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 26645-26654
    • Yang, S.1
  • 101
    • 32644487258 scopus 로고    scopus 로고
    • Daxx: Death or survival protein?
    • Salomoni, P. & Khelifi, A. F. Daxx: death or survival protein? Trends Cell Biol. 16, 97-104 (2006).
    • (2006) Trends Cell Biol , vol.16 , pp. 97-104
    • Salomoni, P.1    Khelifi, A.F.2
  • 102
    • 0033229827 scopus 로고    scopus 로고
    • Torii, S., Egan, D. A., Evans, R. A. & Reed, J. C. Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs). EMBO J. 18, 6037-6049 (1999).
    • Torii, S., Egan, D. A., Evans, R. A. & Reed, J. C. Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs). EMBO J. 18, 6037-6049 (1999).
  • 103
    • 0034695883 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis
    • Zhong, S. et al. Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. J. Exp. Med. 191, 631-640 (2000).
    • (2000) J. Exp. Med , vol.191 , pp. 631-640
    • Zhong, S.1
  • 104
    • 0141529776 scopus 로고    scopus 로고
    • Daxx silencing sensitizes cells to multiple apoptotic pathways
    • Chen, L. Y. & Chen, J. D. Daxx silencing sensitizes cells to multiple apoptotic pathways. Mol. Cell. Biol. 23, 7108-7121 (2003).
    • (2003) Mol. Cell. Biol , vol.23 , pp. 7108-7121
    • Chen, L.Y.1    Chen, J.D.2
  • 105
    • 33749459830 scopus 로고    scopus 로고
    • Daxx represses expression of a subset of antiapoptotic genes regulated by nuclear factor-κB
    • Croxton, R. et al. Daxx represses expression of a subset of antiapoptotic genes regulated by nuclear factor-κB. Cancer Res. 66, 9026-9035 (2006).
    • (2006) Cancer Res , vol.66 , pp. 9026-9035
    • Croxton, R.1
  • 106
    • 34247583326 scopus 로고    scopus 로고
    • Modification of nuclear PML protein by SUMO-1 regulates Fas-induced apoptosis in rheumatoid arthritis synovial fibroblasts
    • Meinecke, I. et al. Modification of nuclear PML protein by SUMO-1 regulates Fas-induced apoptosis in rheumatoid arthritis synovial fibroblasts. Proc. Natl Acad. Sci. USA 104, 5073-5078 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 5073-5078
    • Meinecke, I.1
  • 107
    • 33846532487 scopus 로고    scopus 로고
    • FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies
    • Milovic-Holm, K., Krieghoff, E., Jensen, K., Will, H. & Hofmann, T. G. FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies. EMBO J. 26, 391-401 (2007).
    • (2007) EMBO J , vol.26 , pp. 391-401
    • Milovic-Holm, K.1    Krieghoff, E.2    Jensen, K.3    Will, H.4    Hofmann, T.G.5
  • 108
    • 0036771840 scopus 로고    scopus 로고
    • Ferbeyre, G. PML a target of translocations in APL is a regulator of cellular senescence. Leukemia 16, 1918-1926 (2002).
    • Ferbeyre, G. PML a target of translocations in APL is a regulator of cellular senescence. Leukemia 16, 1918-1926 (2002).
  • 109
    • 0037667702 scopus 로고    scopus 로고
    • Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence
    • Narita, M. et al. Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence. Cell 113, 703-716 (2003).
    • (2003) Cell , vol.113 , pp. 703-716
    • Narita, M.1
  • 110
    • 1542344522 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 and oncogenic signalling
    • Bardos, J. I. & Ashcroft, M. Hypoxia-inducible factor-1 and oncogenic signalling. Bioessays 26, 262-269 (2004).
    • (2004) Bioessays , vol.26 , pp. 262-269
    • Bardos, J.I.1    Ashcroft, M.2
  • 111
    • 0031791875 scopus 로고    scopus 로고
    • PML is essential for multiple apoptotic pathways
    • Wang, Z. G. et al. PML is essential for multiple apoptotic pathways. Nature Genet. 20, 266-272 (1998).
    • (1998) Nature Genet , vol.20 , pp. 266-272
    • Wang, Z.G.1
  • 112
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • Jensen, K., Shiels, C. & Freemont, P. S. PML protein isoforms and the RBCC/TRIM motif. Oncogene 20, 7223-7233 (2001).
    • (2001) Oncogene , vol.20 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 113
    • 34547873122 scopus 로고    scopus 로고
    • PML-RARA inhibits PML IV enhancement of PU.1-induced C/EBPε expression in myeloid differentiation
    • Yoshida, H. et al. PML-RARA inhibits PML IV enhancement of PU.1-induced C/EBPε expression in myeloid differentiation. Mol. Cell. Biol. 27, 5819-5834 (2007).
    • (2007) Mol. Cell. Biol , vol.27 , pp. 5819-5834
    • Yoshida, H.1
  • 114
    • 0034669124 scopus 로고    scopus 로고
    • Regulation of p53 activity in nuclear bodies by a specific PML isoform
    • Fogal, V. et al. Regulation of p53 activity in nuclear bodies by a specific PML isoform. EMBO J. 19, 6185-6195 (2000).
    • (2000) EMBO J , vol.19 , pp. 6185-6195
    • Fogal, V.1
  • 115
    • 34249005636 scopus 로고    scopus 로고
    • PML4 induces differentiation by Myc destabilization
    • Buschbeck, M. et al. PML4 induces differentiation by Myc destabilization. Oncogene 26, 3415-3422 (2006).
    • (2006) Oncogene , vol.26 , pp. 3415-3422
    • Buschbeck, M.1
  • 116
    • 11144219997 scopus 로고    scopus 로고
    • Physical and functional link of the leukemia-associated factors AML1 and PML
    • Nguyen, L. A. et al. Physical and functional link of the leukemia-associated factors AML1 and PML. Blood 105, 292-300 (2005).
    • (2005) Blood , vol.105 , pp. 292-300
    • Nguyen, L.A.1
  • 117
    • 14644394332 scopus 로고    scopus 로고
    • A role for PML3 in centrosome duplication and genome stability
    • Xu, Z. X., Zou, W. X., Lin, P. & Chang, K. S. A role for PML3 in centrosome duplication and genome stability. Mol. Cell 17, 721-732 (2005).
    • (2005) Mol. Cell , vol.17 , pp. 721-732
    • Xu, Z.X.1    Zou, W.X.2    Lin, P.3    Chang, K.S.4
  • 118
    • 34447559500 scopus 로고    scopus 로고
    • Identification of candidate alternative lengthening of telomeres genes by methionine restriction and RNA interference
    • Jiang, W. Q., Zhong, Z. H., Henson, J. D. & Reddel, R. R. Identification of candidate alternative lengthening of telomeres genes by methionine restriction and RNA interference. Oncogene 26, 4635-4637 (2007).
    • (2007) Oncogene , vol.26 , pp. 4635-4637
    • Jiang, W.Q.1    Zhong, Z.H.2    Henson, J.D.3    Reddel, R.R.4
  • 119
    • 16844371495 scopus 로고    scopus 로고
    • Telomerase-independent telomere length maintenance in the absence of alternative lengthening of telomeres-associated promyelocytic leukemia bodies
    • Fasching, C. L., Bower, K. & Reddel, R. R. Telomerase-independent telomere length maintenance in the absence of alternative lengthening of telomeres-associated promyelocytic leukemia bodies. Cancer Res. 65, 2722-2729 (2005).
    • (2005) Cancer Res , vol.65 , pp. 2722-2729
    • Fasching, C.L.1    Bower, K.2    Reddel, R.R.3
  • 120
    • 19944428332 scopus 로고    scopus 로고
    • A robust assay for alternative lengthening of telomeres in tumors shows the significance of alternative lengthening of telomeres in sarcomas and astrocytomas
    • Henson, J. D. et al. A robust assay for alternative lengthening of telomeres in tumors shows the significance of alternative lengthening of telomeres in sarcomas and astrocytomas. Clin. Cancer Res. 11, 217-225 (2005).
    • (2005) Clin. Cancer Res , vol.11 , pp. 217-225
    • Henson, J.D.1
  • 121
    • 33748989558 scopus 로고    scopus 로고
    • Telomere maintenance mechanisms in liposarcomas: Association with histologic subtypes and disease progression
    • Costa, A. et al. Telomere maintenance mechanisms in liposarcomas: association with histologic subtypes and disease progression. Cancer Res. 66, 8918-8924 (2006).
    • (2006) Cancer Res , vol.66 , pp. 8918-8924
    • Costa, A.1
  • 122
    • 34447129654 scopus 로고    scopus 로고
    • The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins
    • Potts, P. R. & Yu, H. The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins. Nature Struct. Mol. Biol. 14, 581-590 (2007).
    • (2007) Nature Struct. Mol. Biol , vol.14 , pp. 581-590
    • Potts, P.R.1    Yu, H.2
  • 123
    • 4444317361 scopus 로고    scopus 로고
    • Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX
    • Ishov, A. M., Vladimirova, O. V. & Maul, G. G. Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX. J. Cell Sci. 117, 3807-3820 (2004).
    • (2004) J. Cell Sci , vol.117 , pp. 3807-3820
    • Ishov, A.M.1    Vladimirova, O.V.2    Maul, G.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.