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Volumn 14, Issue 6, 2009, Pages 2293-2306

Expanding PML's functional repertoire through post-translational mechanisms

Author keywords

ISG15; Phosphorylation; PML; PML RAR alpha; Post translational; Review; SUMO

Indexed keywords

NUCLEAR PROTEIN; PML PROTEIN, HUMAN; RETINOIC ACID RECEPTOR; RETINOIC ACID RECEPTOR ALPHA; SUMO PROTEIN; TRANSCRIPTION FACTOR; TUMOR SUPPRESSOR PROTEIN;

EID: 63849264460     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3380     Document Type: Article
Times cited : (7)

References (77)
  • 1
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • M. N. Boddy, K. Howe, L. D. Etkin, E. Solomon and P. S. Freemont: PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene, 13(5), 971-82 (1996). (Pubitemid 26329084)
    • (1996) Oncogene , vol.13 , Issue.5 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 2
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • O. Kerscher, R. Felberbaum and M. Hochstrasser: Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol, 22, 159-80 (2006).
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 3
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • J. M. Desterro, M. S. Rodriguez and R. T. Hay: SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol Cell, 2(2), 233-9 (1998). (Pubitemid 128373648)
    • (1998) Molecular Cell , vol.2 , Issue.2 , pp. 233-239
    • Desterro, J.M.P.1    Rodriguez, M.S.2    Hay, R.T.3
  • 4
    • 0034523266 scopus 로고    scopus 로고
    • SUMO-nonclassical ubiquitin
    • F. Melchior: SUMO-nonclassical ubiquitin. Annu Rev Cell Dev Biol, 16, 591-626 (2000).
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 591-626
    • Melchior, F.1
  • 6
  • 7
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
    • DOI 10.1083/jcb.139.7.1621
    • T. Sternsdorf, K. Jensen and H. Will: Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J Cell Biol, 139(7), 1621-34 (1997). (Pubitemid 28079228)
    • (1997) Journal of Cell Biology , vol.139 , Issue.7 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 8
    • 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
    • S. Muller, M. J. Matunis and A. Dejean: Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. Embo J, 17(1), 61-70 (1998). (Pubitemid 28041048)
    • (1998) EMBO Journal , vol.17 , Issue.1 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 11
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • 0
    • M. S. Rodriguez, C. Dargemont and R. T. Hay: SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J Biol Chem, 276(16), 12654-9 (2001) 0.
    • (2001) J Biol Chem , vol.276 , Issue.16 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 13
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • DOI 10.1016/S0092-8674(02)00630-X
    • V. Bernier-Villamor, D. A. Sampson, M. J. Matunis and C. D. Lima: Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell, 108(3), 345-56 (2002). (Pubitemid 34178399)
    • (2002) Cell , vol.108 , Issue.3 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4
  • 14
    • 11444271001 scopus 로고    scopus 로고
    • Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection
    • DOI 10.1038/nsmb878
    • M. H. Tatham, S. Kim, E. Jaffray, J. Song, Y. Chen and R. T. Hay: Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. Nat Struct Mol Biol, 12(1), 67-74 (2005). (Pubitemid 40082919)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.1 , pp. 67-74
    • Tatham, M.H.1    Kim, S.2    Jaffray, E.3    Song, J.4    Chen, Y.5    Hay, R.T.6
  • 16
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • DOI 10.1016/S0092-8674(01)00633-X
    • A. Pichler, A. Gast, J. S. Seeler, A. Dejean and F. Melchior: The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell, 108(1), 109-20 (2002). (Pubitemid 34137016)
    • (2002) Cell , vol.108 , Issue.1 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 17
    • 33750447586 scopus 로고    scopus 로고
    • The Mechanisms of PML-Nuclear Body Formation
    • DOI 10.1016/j.molcel.2006.09.013, PII S1097276506006617
    • T. H. Shen, H. K. Lin, P. P. Scaglioni, T. M. Yung and P. P. Pandolfi: The mechanisms of PML-nuclear body formation. Mol Cell, 24(3), 331-9 (2006). (Pubitemid 44647906)
    • (2006) Molecular Cell , vol.24 , Issue.3 , pp. 331-339
    • Shen, T.H.1    Lin, H.-K.2    Scaglioni, P.P.3    Yung, T.M.4    Pandolfi, P.P.5
  • 18
    • 33646859205 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein stimulates SUMO conjugation in yeast
    • DOI 10.1038/sj.onc.1209335, PII 1209335
    • B. B. Quimby, V. Yong-Gonzalez, T. Anan, A. V. Strunnikov and M. Dasso: The promyelocytic leukemia protein stimulates SUMO conjugation in yeast. Oncogene, 25(21), 2999-3005 (2006). (Pubitemid 43780464)
    • (2006) Oncogene , vol.25 , Issue.21 , pp. 2999-3005
    • Quimby, B.B.1    Yong-Gonzalez, V.2    Anan, T.3    Strunnikov, A.V.4    Dasso, M.5
  • 19
    • 0034603179 scopus 로고    scopus 로고
    • Differential regulation of sentrinized proteins by a novel sentrin- specific protease
    • DOI 10.1074/jbc.275.5.3355
    • L. Gong, S. Millas, G. G. Maul and E. T. Yeh: Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J Biol Chem, 275(5), 3355-9 (2000). (Pubitemid 30083039)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.5 , pp. 3355-3359
    • Gong, L.1    Millas, S.2    Maul, G.G.3    Yeh, E.T.H.4
  • 20
    • 0035914357 scopus 로고    scopus 로고
    • Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting beta-catenin degradation
    • T. Nishida, F. Kaneko, M. Kitagawa and H. Yasuda: Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting beta-catenin degradation. J Biol Chem, 276(42), 39060-6 (2001).
    • (2001) J Biol Chem , vol.276 , Issue.42 , pp. 39060-39066
    • Nishida, T.1    Kaneko, F.2    Kitagawa, M.3    Yasuda, H.4
  • 21
    • 0033760171 scopus 로고    scopus 로고
    • A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase
    • T. Nishida, H. Tanaka and H. Yasuda: A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase. Eur J Biochem, 267(21), 6423-7 (2000).
    • (2000) Eur J Biochem , vol.267 , Issue.21 , pp. 6423-6427
    • Nishida, T.1    Tanaka, H.2    Yasuda, H.3
  • 22
    • 33744917849 scopus 로고    scopus 로고
    • Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3
    • DOI 10.1074/jbc.M511658200
    • L. Gong and E. T. Yeh: Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3. J Biol Chem, 281(23), 15869-77 (2006). (Pubitemid 43848478)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.23 , pp. 15869-15877
    • Gong, L.1    Yeh, E.T.H.2
  • 24
    • 33745046562 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling modulates activity and ubiquitination- dependent turnover of SUMO-specific protease 2
    • DOI 10.1128/MCB.01830-05
    • Y. Itahana, E. T. Yeh and Y. Zhang: Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2. Mol Cell Biol, 26(12), 4675-89 (2006). (Pubitemid 43877584)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.12 , pp. 4675-4689
    • Itahana, Y.1    Yeh, E.T.H.2    Zhang, Y.3
  • 25
    • 0036724599 scopus 로고    scopus 로고
    • Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex
    • H. Zhang, H. Saitoh and M. J. Matunis: Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. Mol Cell Biol, 22(18), 6498-508 (2002).
    • (2002) Mol Cell Biol , vol.22 , Issue.18 , pp. 6498-6508
    • Zhang, H.1    Saitoh, H.2    Matunis, M.J.3
  • 26
    • 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
    • A. M. Ishov, A. G. Sotnikov, D. Negorev, O. V. Vladimirova, N. Neff, T. Kamitani, E. T. Yeh, J. F. Strauss, 3rd and G. G. Maul: 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(2), 221-34 (1999).
    • (1999) J Cell Biol , vol.147 , Issue.2 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3    Vladimirova, O.V.4    Neff, N.5    Kamitani, T.6    Yeh, E.T.7    Strauss III, J.F.8    Maul, G.G.9
  • 27
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibition of Daxx-mediated transcriptional repression by PML
    • DOI 10.1128/MCB.20.5.1784-1796.2000
    • H. Li, C. Leo, J. Zhu, X. Wu, J. O'Neil, E. J. Park and J. D. Chen: Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol Cell Biol, 20(5), 1784-96 (2000). (Pubitemid 30100196)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.5 , pp. 1784-1796
    • Li, H.1    Leo, C.2    Zhu, J.3    Wu, X.4    O'Neil, J.5    Park, E.-J.6    Chen, J.D.7
  • 29
    • 0036066181 scopus 로고    scopus 로고
    • Modification of Daxx by small ubiquitin-related modifier-1
    • DOI 10.1016/S0006-291X(02)00699-X, PII S0006291X0200699X
    • M. S. Jang, S. W. Ryu and E. Kim: Modification of Daxx by small ubiquitin-related modifier-1. Biochem Biophys Res Commun, 295(2), 495-500 (2002). (Pubitemid 34785862)
    • (2002) Biochemical and Biophysical Research Communications , vol.295 , Issue.2 , pp. 495-500
    • Jang, M.-S.1    Ryu, S.-W.2    Kim, E.3
  • 32
    • 24644522876 scopus 로고    scopus 로고
    • Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3
    • DOI 10.1038/sj.onc.1208714, PII 1208714
    • C. Fu, K. Ahmed, H. Ding, X. Ding, J. Lan, Z. Yang, Y. Miao, Y. Zhu, Y. Shi, J. Zhu, H. Huang and X. Yao: Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3. Oncogene, 24(35), 5401-13 (2005). (Pubitemid 43080084)
    • (2005) Oncogene , vol.24 , Issue.35 , pp. 5401-5413
    • Fu, C.1    Ahmed, K.2    Ding, H.3    Ding, X.4    Lan, J.5    Yang, Z.6    Miao, Y.7    Zhu, Y.8    Shi, Y.9    Zhu, J.10    Huang, H.11    Yao, X.12
  • 33
    • 0035881526 scopus 로고    scopus 로고
    • PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA
    • DOI 10.1093/emboj/20.16.4547
    • N. Cohen, M. Sharma, A. Kentsis, J. M. Perez, S. Strudwick and K. L. Borden: PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA. EMBO J, 20(16), 4547-59 (2001). (Pubitemid 32772048)
    • (2001) EMBO Journal , vol.20 , Issue.16 , pp. 4547-4559
    • Cohen, N.1    Sharma, M.2    Kentsis, A.3    Perez, J.M.4    Strudwick, S.5    Borden, K.L.B.6
  • 34
    • 0033617169 scopus 로고    scopus 로고
    • The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers
    • T. Sternsdorf, K. Jensen, B. Reich and H. Will: The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J Biol Chem, 274(18), 12555-66 (1999).
    • (1999) J Biol Chem , vol.274 , Issue.18 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 35
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • DOI 10.1083/jcb.148.2.283
    • F. M. Boisvert, M. J. Hendzel and D. P. Bazett-Jones: Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J Cell Biol, 148(2), 283-92 (2000). (Pubitemid 30078240)
    • (2000) Journal of Cell Biology , vol.148 , Issue.2 , pp. 283-292
    • Boisvert, F.-M.1    Hendzel, M.J.2    Bazett-Jones, D.P.3
  • 36
    • 0035804220 scopus 로고    scopus 로고
    • Regulation of Pax3 transcriptional activity by SUMO-1-modified PML
    • DOI 10.1038/sj.onc.1204063
    • F. Lehembre, S. Muller, P. P. Pandolfi and A. Dejean: Regulation of Pax3 transcriptional activity by SUMO-1-modified PML. Oncogene, 20(1), 1-9 (2001). (Pubitemid 32142332)
    • (2001) Oncogene , vol.20 , Issue.1 , pp. 1-9
    • Lehembre, F.1    Muller, S.2    Pandolfi, P.P.3    Dejean, A.4
  • 37
    • 20344384269 scopus 로고    scopus 로고
    • SUMO-dependent compartmentalization in promyelocytic leukemia protein nuclear bodies prevents the access of LRH-1 to chromatin
    • DOI 10.1128/MCB.25.12.5095-5105.2005
    • A. Chalkiadaki and I. Talianidis: SUMO-dependent compartmentalization in promyelocytic leukemia protein nuclear bodies prevents the access of LRH-1 to chromatin. Mol Cell Biol, 25(12), 5095-105 (2005). (Pubitemid 40781109)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.12 , pp. 5095-5105
    • Chalkiadaki, A.1    Talianidis, I.2
  • 40
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: Implications in antiviral defence
    • DOI 10.1016/j.biochi.2007.01.004, PII S0300908407000132
    • R. D. Everett and M. K. Chelbi-Alix: PML and PML nuclear bodies: implications in antiviral defence. Biochimie, 89(6-7), 819-30 (2007). (Pubitemid 47008945)
    • (2007) Biochimie , vol.89 , Issue.6-7 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 41
    • 0027769358 scopus 로고
    • Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICPO)
    • G. G. Maul, H. H. Guldner and J. G. Spivack: Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0). J Gen Virol, 74 (Pt 12), 2679-90 (1993). (Pubitemid 24020661)
    • (1993) Journal of General Virology , vol.74 , Issue.12 , pp. 2679-2690
    • Maul, G.G.1    Guldner, H.H.2    Spivack, J.G.3
  • 42
    • 0030912888 scopus 로고    scopus 로고
    • The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PML-associated nuclear bodies at very early times in infected permissive cells
    • J. H. Ahn and G. S. Hayward: The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PML-associated nuclear bodies at very early times in infected permissive cells. J Virol, 71(6), 4599-613 (1997). (Pubitemid 27204153)
    • (1997) Journal of Virology , vol.71 , Issue.6 , pp. 4599-4613
    • Ahn, J.-H.1    Hayward, G.S.2
  • 43
    • 0028039189 scopus 로고
    • HSV-1 IE protein Vmw110 causes redistribution of PML
    • R. D. Everett and G. G. Maul: HSV-1 IE protein Vmw110 causes redistribution of PML. Embo J, 13(21), 5062-9 (1994). (Pubitemid 24341087)
    • (1994) EMBO Journal , vol.13 , Issue.21 , pp. 5062-5069
    • Everett, R.D.1    Maul, G.G.2
  • 44
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • S. Muller and A. Dejean: Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J Virol, 73(6), 5137-43 (1999). (Pubitemid 29246776)
    • (1999) Journal of Virology , vol.73 , Issue.6 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 45
    • 0028352769 scopus 로고
    • 4 viral protein ICP0
    • G. G. Maul and R. D. Everett: The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0. J Gen Virol, 75 (Pt 6), 1223-33 (1994). (Pubitemid 24174037)
    • (1994) Journal of General Virology , vol.75 , Issue.6 , pp. 1223-1233
    • Maul, G.G.1    Everett, R.D.2
  • 46
    • 0042709466 scopus 로고    scopus 로고
    • PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0
    • DOI 10.1128/JVI.77.16.8686-8694.2003
    • C. Boutell, A. Orr and R. D. Everett: PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0. J Virol, 77(16), 8686-94 (2003). (Pubitemid 36936079)
    • (2003) Journal of Virology , vol.77 , Issue.16 , pp. 8686-8694
    • Boutell, C.1    Orr, A.2    Everett, R.D.3
  • 48
    • 0031877790 scopus 로고    scopus 로고
    • Disruption of PML subnuclear domains by the acidic IE1 protein of human cytomegalovirus is mediated through interaction with PML and may modulate a RING finger-dependent cryptic transactivator function of PML
    • J. H. Ahn, E. J. Brignole, 3rd and G. S. Hayward: Disruption of PML subnuclear domains by the acidic IE1 protein of human cytomegalovirus is mediated through interaction with PML and may modulate a RING fingerdependent cryptic transactivator function of PML. Mol Cell Biol, 18(8), 4899-913 (1998). (Pubitemid 28343073)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.8 , pp. 4899-4913
    • Ahn, J.-H.1    Brignole III, E.J.2    Hayward, G.S.3
  • 49
    • 33746824547 scopus 로고    scopus 로고
    • Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein
    • DOI 10.1099/vir.0.81787-0
    • H. Kang, E. T. Kim, H. R. Lee, J. J. Park, Y. Y. Go, C. Y. Choi and J. H. Ahn: Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein. J Gen Virol, 87(Pt 8), 2181-90 (2006). (Pubitemid 44178096)
    • (2006) Journal of General Virology , vol.87 , Issue.8 , pp. 2181-2190
    • Kang, H.1    Kim, E.T.2    Lee, H.-R.3    Park, J.-J.4    Go, Y.Y.5    Choi, C.Y.6    Ahn, J.-H.7
  • 50
    • 0035124377 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies
    • DOI 10.1128/JVI.75.5.2388-2399.2001
    • A. L. Adamson and S. Kenney: Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies. J Virol, 75(5), 2388-99 (2001). (Pubitemid 32147577)
    • (2001) Journal of Virology , vol.75 , Issue.5 , pp. 2388-2399
    • Adamson, A.L.1    Kenney, S.2
  • 51
    • 33645731002 scopus 로고    scopus 로고
    • The number of PML nuclear bodies increases in early S phase by a fission mechanism
    • G. Dellaire, R. W. Ching, H. Dehghani, Y. Ren and D. P. Bazett-Jones: The number of PML nuclear bodies increases in early S phase by a fission mechanism. J Cell Sci, 119(Pt 6), 1026-33 (2006).
    • (2006) J Cell Sci , vol.119 , Issue.PART 6 , pp. 1026-1033
    • Dellaire, G.1    Ching, R.W.2    Dehghani, H.3    Ren, Y.4    Bazett-Jones, D.P.5
  • 53
    • 33645749156 scopus 로고    scopus 로고
    • Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in G1
    • G. Dellaire, C. H. Eskiw, H. Dehghani, R. W. Ching and D. P. Bazett-Jones: Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in G1. J Cell Sci, 119(Pt 6), 1034-42 (2006).
    • (2006) J Cell Sci , vol.119 , Issue.PART 6 , pp. 1034-1042
    • Dellaire, G.1    Eskiw, C.H.2    Dehghani, H.3    Ching, R.W.4    Bazett-Jones, D.P.5
  • 54
    • 0028951531 scopus 로고
    • PML nuclear bodies are general targets for inflammation and cell proliferation
    • B. Terris, V. Baldin, S. Dubois, C. Degott, J. F. Flejou, D. Henin and A. Dejean: PML nuclear bodies are general targets for inflammation and cell proliferation. Cancer Res, 55(7), 1590-7 (1995).
    • (1995) Cancer Res , vol.55 , Issue.7 , pp. 1590-1597
    • Terris, B.1    Baldin, V.2    Dubois, S.3    Degott, C.4    Flejou, J.F.5    Henin, D.6    Dejean, A.7
  • 56
    • 0037325853 scopus 로고    scopus 로고
    • Deregulated degradation of the cdk inhibitor p27 and malignant transformation
    • DOI 10.1016/S1044-579X(02)00098-6, PII S1044579X02000986
    • J. Bloom and M. Pagano: Deregulated degradation of the cdk inhibitor p27 and malignant transformation. Semin Cancer Biol, 13(1), 41-7 (2003). (Pubitemid 36269179)
    • (2003) Seminars in Cancer Biology , vol.13 , Issue.1 , pp. 41-47
    • Bloom, J.1    Pagano, M.2
  • 59
    • 0036847998 scopus 로고    scopus 로고
    • PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2
    • DOI 10.1038/ncb869
    • S. Yang, C. Kuo, J. E. Bisi and M. K. Kim: PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2. Nat Cell Biol, 4(11), 865-70 (2002). (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
  • 61
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • T. Jenuwein and C. D. Allis: Translating the histone code. Science, 293(5532), 1074-80 (2001). (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 63
    • 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
    • F. Hayakawa and M. L. Privalsky: Phosphorylation of PML by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis. Cancer Cell, 5(4), 389-401 (2004). (Pubitemid 38482074)
    • (2004) Cancer Cell , vol.5 , Issue.4 , pp. 389-401
    • Hayakawa, F.1    Privalsky, M.L.2
  • 64
    • 36749010218 scopus 로고    scopus 로고
    • The Age of Crosstalk: Phosphorylation, Ubiquitination, and Beyond
    • DOI 10.1016/j.molcel.2007.11.019, PII S1097276507007988
    • T. Hunter: The age of crosstalk: phosphorylation, ubiquitination, and beyond. Mol Cell, 28(5), 730-8 (2007). (Pubitemid 350217067)
    • (2007) Molecular Cell , vol.28 , Issue.5 , pp. 730-738
    • Hunter, T.1
  • 65
    • 33748636239 scopus 로고    scopus 로고
    • Cross talk between PML and p53 during poliovirus infection: Implications for antiviral defense
    • DOI 10.1128/JVI.00031-06
    • M. Pampin, Y. Simonin, B. Blondel, Y. Percherancier and M. K. Chelbi-Alix: Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense. J Virol, 80(17), 8582-92 (2006). (Pubitemid 44384869)
    • (2006) Journal of Virology , vol.80 , Issue.17 , pp. 8582-8592
    • Pampin, M.1    Simonin, Y.2    Blondel, B.3    Percherancier, Y.4    Chelbi-Alix, M.K.5
  • 66
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • DOI 10.1093/emboj/20.3.362
    • W. Yuan and R. M. Krug: Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. EMBO J, 20(3), 362-71 (2001). (Pubitemid 32126972)
    • (2001) EMBO Journal , vol.20 , Issue.3 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2
  • 69
    • 33751257187 scopus 로고    scopus 로고
    • The interferon regulated ubiquitin-like protein, ISG15, in tumorigenesis: Friend or foe?
    • DOI 10.1016/j.cytogfr.2006.10.001, PII S135961010600075X
    • J. B. Andersen and B. A. Hassel: The interferon regulated ubiquitin-like protein, ISG15, in tumorigenesis: friend or foe? Cytokine Growth Factor Rev, 17(6), 411-21 (2006). (Pubitemid 44793124)
    • (2006) Cytokine and Growth Factor Reviews , vol.17 , Issue.6 , pp. 411-421
    • Andersen, J.B.1    Hassel, B.A.2
  • 72
    • 0038128204 scopus 로고    scopus 로고
    • High-throughput immunoblotting: Ubiquitin-like protein ISG15 modifies key regulators of signal transduction
    • DOI 10.1074/jbc.M208435200
    • M. P. Malakhov, K. I. Kim, O. A. Malakhova, B. S. Jacobs, E. C. Borden and D. E. Zhang: High-throughput immunoblotting. Ubiquitiin-like protein ISG15 modifies key regulators of signal transduction. J Biol Chem, 278(19), 16608-13 (2003). (Pubitemid 36799523)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16608-16613
    • Malakhov, M.P.1    Kim, K.I.2    Malakhova, O.A.3    Jacobs, B.S.4    Borden, E.C.5    Zhang, D.-E.6
  • 73
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: Ubiquitin, SUMO and related modifiers
    • DOI 10.1016/S0968-0004(03)00113-0
    • D. C. Schwartz and M. Hochstrasser: A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem Sci, 28(6), 321-8 (2003). (Pubitemid 36776295)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.6 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 74
    • 0033037274 scopus 로고    scopus 로고
    • PIC-1/SUMO-1-modified PML-retinoic acid receptor α mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia
    • T. Sternsdorf, E. Puccetti, K. Jensen, D. Hoelzer, H. Will, O. G. Ottmann and M. Ruthardt: PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia. Mol Cell Biol, 19(7), 5170-8 (1999). (Pubitemid 29289555)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.7 , pp. 5170-5178
    • Sternsdorf, T.1    Puccetti, E.2    Jensen, K.3    Hoelzer, D.4    Will, H.5    Ottmann, O.G.6    Ruthardt, M.7
  • 75
    • 16244417803 scopus 로고    scopus 로고
    • Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for localization, sumoylation, and inhibition of monocyte differentiation
    • Y. E. Kim, D. Y. Kim, J. M. Lee, S. T. Kim, T. H. Han and J. H. Ahn: Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for localization, sumoylation, and inhibition of monocyte differentiation. Biochem Biophys Res Commun, 330(3), 746-54 (2005).
    • (2005) Biochem Biophys Res Commun , vol.330 , Issue.3 , pp. 746-754
    • Kim, Y.E.1    Kim, D.Y.2    Lee, J.M.3    Kim, S.T.4    Han, T.H.5    Ahn, J.H.6
  • 76
    • 13844269220 scopus 로고    scopus 로고
    • A sumoylation site in PML/RARA is essential for leukemic transformation
    • DOI 10.1016/j.ccr.2005.01.005
    • J. Zhu, J. Zhou, L. Peres, F. Riaucoux, N. Honore, S. Kogan and H. de Thé: A sumoylation site in PML/RARA is essential for leukemic transformation. Cancer Cell, 7(2), 143-53 (2005). (Pubitemid 40248340)
    • (2005) Cancer Cell , vol.7 , Issue.2 , pp. 143-153
    • Zhu, J.1    Zhou, J.2    Peres, L.3    Riaucoux, F.4    Honore, N.5    Kogan, S.6    De The, H.7
  • 77
    • 54049143319 scopus 로고    scopus 로고
    • Acetylation of PML is involved in histone deacetylase inhibitor-mediated apoptosis
    • Epub ahead of print
    • F. Hayakawa, A. Abe, I. Kitabayahi, P. P. Pandolfi and T. Naoe: Acetylation of PML is involved in histone deacetylase inhibitor-mediated apoptosis. J Biol Chem, Epub ahead of print (2008).
    • (2008) J Biol Chem
    • Hayakawa, F.1    Abe, A.2    Kitabayahi, I.3    Pandolfi, P.P.4    Naoe, T.5


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