Role of nuclear bodies in apoptosis signalling

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1783, Issue 11, 2008, Pages 2185-2194

  Krieghoff Henning, Eva ^a   Hofmann, Thomas G ^a  

^a GERMAN CANCER RESEARCH CENTER   (Germany)

Author keywords

Apoptosis; Crosstalk; Death receptor signalling; Genotoxic stress; Nuclear domain; p53; PML nuclear body

Indexed keywords

APOPTOSIS REGULATORY PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; DEATH RECEPTOR; FLICE ASSOCIATED HUGE PROTEIN; HOMEODOMAIN INTERACTING PROTEIN KINASE 2; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN P53; UNCLASSIFIED DRUG;

APOPTOSIS; CANCER INHIBITION; CELL AGING; CELL COMMUNICATION; CELL DEATH; CELL FUNCTION; CELL NUCLEUS INCLUSION BODY; CELL TRANSFORMATION; CELLULAR STRESS RESPONSE; COILED BODY; GENOTOXICITY; HUMAN; NONHUMAN; PRIORITY JOURNAL; RECEPTOR UPREGULATION; REVIEW; SENESCENCE;

ANIMALS; APOPTOSIS; CELL NUCLEUS; HUMANS; INTRANUCLEAR INCLUSION BODIES; LEUKEMIA, PROMYELOCYTIC, ACUTE; NEOPLASMS; NUCLEAR PROTEINS; PROTEIN ISOFORMS; RECEPTORS, DEATH DOMAIN; RECEPTORS, TRANSFORMING GROWTH FACTOR BETA; SIGNAL TRANSDUCTION; TRANSCRIPTION FACTORS; TUMOR SUPPRESSOR PROTEIN P53; TUMOR SUPPRESSOR PROTEINS;

EID: 53449090838     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.07.002     Document Type: Review

References (143)

1. Peter M.E., and Krammer P.H. The CD95(APO-1/Fas) DISC and beyond. Cell Death Differ. 10 (2003) 26-35
2. Scaffidi C., Fulda S., Srinivasan A., Friesen C., Li F., Tomaselli K.J., Debatin K.M., Krammer P.H., and Peter M.E. Two CD95 (APO-1/Fas) signaling pathways. EMBO J. 17 (1998) 1675-1687
3. Fesik S.W. Promoting apoptosis as a strategy for cancer drug discovery. Nature Rev. Cancer 5 (2005) 876-885
4. Puthalakath H., and Strasser A. Keeping killers on a tight leash: transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins. Cell Death Differ. 9 (2002) 505-512
5. Wang X. The expanding role of mitochondria in apoptosis. Genes Dev. 15 (2001) 2922-2933
6. Debatin K.M., and Krammer P.H. Death receptors in chemotherapy and cancer. Oncogene 23 (2004) 2950-2966
7. Aylon Y., and Oren M. Living with p53, dying of p53. Cell 130 (2007) 597-600
8. Vousden K.H., and Lane D.P. p53 in health and disease. Nature Rev. Mol. Cell Biol. 8 (2007) 275-283
9. Spector D.L. Nuclear domains. J. Cell Sci. 114 (2001) 2891-2893
10. Bernardi R., and Pandolfi P.P. Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nature Rev. Mol. Cell Biol. 8 (2007) 1006-1016
11. Hofmann T.G., and Will H. Body language: the function of PML nuclear bodies in apoptosis regulation. Cell Death Differ. 10 (2003) 1290-1299
12. Wang Z.G., Ruggero D., Ronchetti S., Zhong S., Gaboli M., Rivi R., and Pandolfi P.P. PML is essential for multiple apoptotic pathways. Nature Genet. 20 (1998) 266-272
13. Mu Z.M., Chin K.V., Liu J.H., Lozano G., and Chang K.S. PML, a growth suppressor disrupted in acute promyelocytic leukemia. Mol. Cell Biol. 14 (1994) 6858-6867
14. Pearson M., Carbone R., Sebastiani C., Cioce M., Fagioli M., Saito S., Higashimoto Y., Appella E., Minucci S., Pandolfi P.P., and Pelicci P.G. PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406 (2000) 207-210
15. Wang J., Shiels C., Sasieni P., Wu P.J., Islam S.A., Freemont P.S., and Sheer D. Promyelocytic leukemia nuclear bodies associate with transcriptionally active genomic regions. J. Cell Biol. 164 (2004) 515-526
16. Seeler J.S., and Dejean A. Nuclear and unclear functions of SUMO. Nature Rev. Mol. Cell Biol. 4 (2003) 690-699
17. Shen T.H., Lin H.K., Scaglioni P.P., Yung T.M., and Pandolfi P.P. The mechanisms of PML-nuclear body formation. Mol. Cell 24 (2006) 331-339
18. Quimby B.B., Yong-Gonzalez V., Anan T., Strunnikov A.V., and Dasso M. The promyelocytic leukemia protein stimulates SUMO conjugation in yeast. Oncogene 25 (2006) 2999-3005
19. Fagioli M., Alcalay M., Tomassoni L., Ferrucci P.F., Mencarelli A., Riganelli D., Grignani F., Pozzan T., Nicoletti I., Grignani F., and Pelicci P.G. Cooperation between the RING+ B1-B2 and coiled-coil domains of PML is necessary for its effects on cell survival. Oncogene 16 (1998) 2905-2913
20. Jensen K., Shiels C., and Freemont P.S. PML protein isoforms and the RBCC/TRIM motif. Oncogene 20 (2001) 7223-7233
21. Condemine W., Takahashi Y., Zhu J., Puvion-Dutilleul F., Guegan S., Janin A., and de The H. Characterization of endogenous human promyelocytic leukemia isoforms. Cancer Res. 66 (2006) 6192-6198
22. Guo A., Salomoni P., Luo J., Shih A., Zhong S., Gu W., and Pandolfi P.P. The function of PML in p53-dependent apoptosis. Nature Cell Biol. 2 (2000) 730-736
23. Chelbi-Alix M.K., Quignon F., Pelicano L., Koken M.H., and de The H. Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein. J. Virol. 72 (1998) 1043-1051
24. Dellaire G., Ching R.W., Dehghani H., Ren Y., and Bazett-Jones D.P. The number of PML nuclear bodies increases in early S phase by a fission mechanism. J. Cell Sci. 119 (2006) 1026-1033
25. Everett R.D., Lomonte P., Sternsdorf T., van Driel R., and Orr A. Cell cycle regulation of PML modification and ND10 composition. J. Cell Sci. 112 Pt 24 (1999) 4581-4588
26. Yeager T.R., Neumann A.A., Englezou A., Huschtscha L.I., Noble J.R., and Reddel R.R. Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body. Cancer Res. 59 (1999) 4175-4179
27. Cesare A.J., and Reddel R.R. Telomere uncapping and alternative lengthening of telomeres. Mech. Ageing Dev. 129 (2008) 99-108
28. Nabetani A., Yokoyama O., and Ishikawa F. Localization of hRad9, hHus1, hRad1, and hRad17 and caffeine-sensitive DNA replication at the alternative lengthening of telomeres-associated promyelocytic leukemia body. J. Biol. Chem. 279 (2004) 25849-25857
29. Stagno D'Alcontres M., Mendez-Bermudez A., Foxon J.L., Royle N.J., and Salomoni P. Lack of TRF2 in ALT cells causes PML-dependent p53 activation and loss of telomeric DNA. J. Cell Biol. 179 (2007) 855-867
30. Lombard D.B., and Guarente L. Nijmegen breakage syndrome disease protein and MRE11 at PML nuclear bodies and meiotic telomeres. Cancer Res. 60 (2000) 2331-2334
31. Naka K., Ikeda K., and Motoyama N. Recruitment of NBS1 into PML oncogenic domains via interaction with SP100 protein. Biochem. Biophys. Res. Commun. 299 (2002) 863-871
32. Wu W.S., Xu Z.X., Hittelman W.N., Salomoni P., Pandolfi P.P., and Chang K.S. Promyelocytic leukemia protein sensitizes tumor necrosis factor alpha-induced apoptosis by inhibiting the NF-kappaB survival pathway. J. Biol. Chem. 278 (2003) 12294-12304
33. Ishov A.M., Sotnikov A.G., Negorev D., Vladimirova O.V., Neff N., Kamitani T., Yeh E.T., Strauss III J.F., and Maul G.G. 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 (1999) 221-234
34. Torii S., Egan D.A., Evans R.A., and Reed J.C. Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs). EMBO J. 18 (1999) 6037-6049
35. Ferbeyre G., de Stanchina E., Querido E., Baptiste N., Prives C., and Lowe S.W. PML is induced by oncogenic ras and promotes premature senescence. Genes Dev. 14 (2000) 2015-2027
36. Fogal V., Gostissa M., Sandy P., Zacchi P., Sternsdorf T., Jensen K., Pandolfi P.P., Will H., Schneider C., and Del Sal G. Regulation of p53 activity in nuclear bodies by a specific PML isoform. EMBO J. 19 (2000) 6185-6195
37. Boisvert F.M., Kruhlak M.J., Box A.K., Hendzel M.J., and Bazett-Jones D.P. The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J. Cell Biol. 152 (2001) 1099-1106
38. Hofmann T.G., Moller A., Sirma H., Zentgraf H., Taya Y., Droge W., Will H., and Schmitz M.L. Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. Nature Cell Biol. 4 (2002) 1-10
39. D'Orazi G., Cecchinelli B., Bruno T., Manni I., Higashimoto Y., Saito S., Gostissa M., Coen S., Marchetti A., Del Sal G., Piaggio G., Fanciulli M., Appella E., and Soddu S. Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis. Nature Cell Biol. 4 (2002) 11-19
40. Alcalay M., Tomassoni L., Colombo E., Stoldt S., Grignani F., Fagioli M., Szekely L., Helin K., and Pelicci P.G. The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol. Cell Biol. 18 (1998) 1084-1093
41. Milovic-Holm K., Krieghoff E., Jensen K., Will H., and Hofmann T.G. FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies. EMBO J. 26 (2007) 391-401
42. Wei X., Yu Z.K., Ramalingam A., Grossman S.R., Yu J.H., Bloch D.B., and Maki C.G. Physical and functional interactions between PML and MDM2. J. Biol. Chem. 278 (2003) 29288-29297
43. Brooks C.L., and Gu W. p53 ubiquitination: Mdm2 and beyond. Mol. Cell 21 (2006) 307-315
44. Oren M. Decision making by p53: life, death and cancer. Cell Death Differ. 10 (2003) 431-442
45. de Stanchina E., Querido E., Narita M., Davuluri R.V., Pandolfi P.P., Ferbeyre G., and Lowe S.W. PML is a direct p53 target that modulates p53 effector functions. Mol. Cell 13 (2004) 523-535
46. el-Deiry W.S., Tokino T., Velculescu V.E., Levy D.B., Parsons R., Trent J.M., Lin D., Mercer W.E., Kinzler K.W., and Vogelstein B. WAF1, a potential mediator of p53 tumor suppression. Cell 75 (1993) 817-825
47. Haupt S., Louria-Hayon I., and Haupt Y. P53 licensed to kill? Operating the assassin. J. Cell Biochem. 88 (2003) 76-82
48. Yang S., Jeong J.H., Brown A.L., Lee C.H., Pandolfi P.P., Chung J.H., and Kim M.K. Promyelocytic leukemia activates Chk2 by mediating Chk2 autophosphorylation. J. Biol. Chem. 281 (2006) 26645-26654
49. Knippschild U., Milne D.M., Campbell L.E., DeMaggio A.J., Christenson E., Hoekstra M.F., and Meek D.W. p53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase-directed drugs. Oncogene 15 (1997) 1727-1736
50. Alsheich-Bartok O., Haupt S., Alkalay-Snir I., Saito S., Appella E., and Haupt Y. PML enhances the regulation of p53 by CK1 in response to DNA damage. Oncogene (2008)
51. Knippschild U., Gocht A., Wolff S., Huber N., Lohler J., and Stoter M. The casein kinase 1 family: participation in multiple cellular processes in eukaryotes. Cell Signal 17 (2005) 675-689
52. Oda Y., Yamamoto H., Takahira T., Kobayashi C., Kawaguchi K., Tateishi N., Nozuka Y., Tamiya S., Tanaka K., Matsuda S., Yokoyama R., Iwamoto Y., and Tsuneyoshi M. Frequent alteration of p16(INK4a)/p14(ARF) and p53 pathways in the round cell component of myxoid/round cell liposarcoma: p53 gene alterations and reduced p14(ARF) expression both correlate with poor prognosis. J. Pathol. 207 (2005) 410-421
53. Mantovani F., Tocco F., Girardini J., Smith P., Gasco M., Lu X., Crook T., and Del Sal G. The prolyl isomerase Pin1 orchestrates p53 acetylation and dissociation from the apoptosis inhibitor iASPP. Nature Struct. Mol. Biol. 14 (2007) 912-920
54. Zacchi P., Gostissa M., Uchida T., Salvagno C., Avolio F., Volinia S., Ronai Z., Blandino G., Schneider C., and Del Sal G. The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults. Nature 419 (2002) 853-857
55. Reineke E.L., Lam M., Liu Q., Liu Y., Stanya K.J., Chang K.S., Means A.R., and Kao H.Y. Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells. Mol. Cell Biol. 28 (2008) 997-1006
56. Ryo A., Hirai A., Nishi M., Liou Y.C., Perrem K., Lin S.C., Hirano H., Lee S.W., and Aoki I. A suppressive role of the prolyl isomerase Pin1 in cellular apoptosis mediated by the death-associated protein Daxx. J. Biol. Chem. 282 (2007) 36671-36681
57. Lu K.P., and Zhou X.Z. The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease. Nature Rev. Mol. Cell Biol. 8 (2007) 904-916
58. Bulavin D.V., Saito S., Hollander M.C., Sakaguchi K., Anderson C.W., Appella E., and Fornace Jr. A.J. Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation. EMBO. J. 18 (1999) 6845-6854
59. Taira N., Nihira K., Yamaguchi T., Miki Y., and Yoshida K. DYRK2 is targeted to the nucleus and controls p53 via Ser46 phosphorylation in the apoptotic response to DNA damage. Mol. Cell 25 (2007) 725-738
60. Lee J.H., Kim H.S., Lee S.J., and Kim K.T. Stabilization and activation of p53 induced by Cdk5 contributes to neuronal cell death. J. Cell Sci. 120 (2007) 2259-2271
61. Roscic A., Moller A., Calzado M.A., Renner F., Wimmer V.C., Gresko E., Ludi K.S., and Schmitz M.L. Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2. Mol. Cell 24 (2006) 77-89
62. Winter M., Sombroek D., Dauth I., Moehlenbrink J., Scheuermann K., Crone J., and Hofmann T.G. Control of HIPK2 stability by ubiquitin ligase Siah-1 and checkpoint kinases ATM and ATR. Nat. Cell Biol. 10 (2008) 812-824
63. Choi D.W., Seo Y.M., Kim E.A., Sung K.S., Ahn J.W., Park S.J., Lee S.R., and Choi C.Y. Ubiquitination and degradation of homeodomain-interacting protein kinase 2 by WD40 repeat/SOCS box protein WSB-1. J. Biol. Chem. 283 (2008) 4682-4689
64. Moller A., Sirma H., Hofmann T.G., Rueffer S., Klimczak E., Droge W., Will H., and Schmitz M.L. PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains. Cancer Res. 63 (2003) 4310-4314
65. Moller A., Sirma H., Hofmann T.G., Staege H., Gresko E., Ludi K.S., Klimczak E., Droge W., Will H., and Schmitz M.L. Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression. Oncogene 22 (2003) 8731-8737
66. Dauth I., Kruger J., and Hofmann T.G. Homeodomain-interacting protein kinase 2 is the ionizing radiation-activated p53 serine 46 kinase and is regulated by ATM. Cancer Res. 67 (2007) 2274-2279
67. Di Stefano V., Blandino G., Sacchi A., Soddu S., and D'Orazi G. HIPK2 neutralizes MDM2 inhibition rescuing p53 transcriptional activity and apoptotic function. Oncogene 23 (2004) 5185-5192
68. Cheng Z., Ke Y., Ding X., Wang F., Wang H., Ahmed K., Liu Z., Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Powell M., Liang S., Reddy S.E., Hu R., Huang H., Jin C., and Yao X. Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response. Oncogene 27 (2008) 931-941
69. Sykes S.M., Mellert H.S., Holbert M.A., Li K., Marmorstein R., Lane W.S., and McMahon S.B. Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol. Cell 24 (2006) 841-851
70. Tang Y., Luo J., Zhang W., and Gu W. Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. Mol. Cell 24 (2006) 827-839
71. Langley E., Pearson M., Faretta M., Bauer U.M., Frye R.A., Minucci S., Pelicci P.G., and Kouzarides T. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO. J. 21 (2002) 2383-2396
72. Vaziri H., Dessain S.K., Ng Eaton E., Imai S.I., Frye R.A., Pandita T.K., Guarente L., and Weinberg R.A. hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107 (2001) 149-159
73. Gostissa M., Morelli M., Mantovani F., Guida E., Piazza S., Collavin L., Brancolini C., Schneider C., and Del Sal G. The transcriptional repressor hDaxx potentiates p53-dependent apoptosis. J. Biol. Chem. 279 (2004) 48013-48023
74. Li Q., Wang X., Wu X., Rui Y., Liu W., Wang J., Wang X., Liou Y.C., Ye Z., and Lin S.C. Daxx cooperates with the Axin/HIPK2/p53 complex to induce cell death. Cancer Res. 67 (2007) 66-74
75. Cummins J.M., and Vogelstein B. HAUSP is required for p53 destabilization. Cell Cycle 3 (2004) 689-692
76. Tang J., Qu L.K., Zhang J., Wang W., Michaelson J.S., Degenhardt Y.Y., El-Deiry W.S., and Yang X. Critical role for Daxx in regulating Mdm2. Nature Cell Biol. 8 (2006) 855-862
77. Li M., Chen D., Shiloh A., Luo J., Nikolaev A.Y., Qin J., and Gu W. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416 (2002) 648-653
78. Imai Y., Kimura T., Murakami A., Yajima N., Sakamaki K., and Yonehara S. The CED-4-homologous protein FLASH is involved in Fas-mediated activation of caspase-8 during apoptosis. Nature 398 (1999) 777-785
79. Barcaroli D., Bongiorno-Borbone L., Terrinoni A., Hofmann T.G., Rossi M., Knight R.A., Matera A.G., Melino G., and De Laurenzi V. FLASH is required for histone transcription and S-phase progression. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 14808-14812
80. Barcaroli D., Dinsdale D., Neale M.H., Bongiorno-Borbone L., Ranalli M., Munarriz E., Sayan A.E., McWilliam J.M., Smith T.M., Fava E., Knight R.A., Melino G., and De Laurenzi V. FLASH is an essential component of Cajal bodies. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 14802-14807
81. Flotho C., Coustan-Smith E., Pei D., Iwamoto S., Song G., Cheng C., Pui C.H., Downing J.R., and Campana D. Genes contributing to minimal residual disease in childhood acute lymphoblastic leukemia: prognostic significance of CASP8AP2. Blood 108 (2006) 1050-1057
82. Crowder C., Dahle O., Davis R.E., Gabrielsen O.S., and Rudikoff S. PML mediates IFN-alpha-induced apoptosis in myeloma by regulating TRAIL induction. Blood 105 (2005) 1280-1287
83. Lo Y.H., Wu C.C., Shih H.M., and Lai M.Z. Selective activation of NFAT by promyelocytic leukemia protein. Oncogene (2008)
84. Salomoni P., and Khelifi A.F. Daxx: death or survival protein?. Trends Cell Biol. 16 (2006) 97-104
85. Lin D.Y., Huang Y.S., Jeng J.C., Kuo H.Y., Chang C.C., Chao T.T., Ho C.C., Chen Y.C., Lin T.P., Fang H.I., Hung C.C., Suen C.S., Hwang M.J., Chang K.S., Maul G.G., and Shih H.M. Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol. Cell 24 (2006) 341-354
86. Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.J., and Chen J.D. Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol. Cell Biol. 20 (2000) 1784-1796
87. Meinecke I., Cinski A., Baier A., Peters M.A., Dankbar B., Wille A., Drynda A., Mendoza H., Gay R.E., Hay R.T., Ink B., Gay S., and Pap T. Modification of nuclear PML protein by SUMO-1 regulates Fas-induced apoptosis in rheumatoid arthritis synovial fibroblasts. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 5073-5078
88. Hofmann T.G., Stollberg N., Schmitz M.L., and Will H. HIPK2 regulates transforming growth factor-beta-induced c-Jun NH(2)-terminal kinase activation and apoptosis in human hepatoma cells. Cancer Res. 63 (2003) 8271-8277
89. Pampin M., Simonin Y., Blondel B., Percherancier Y., and Chelbi-Alix M.K. Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense. J. Virol. 80 (2006) 8582-8592
90. Lin H.K., Bergmann S., and Pandolfi P.P. Cytoplasmic PML function in TGF-beta signalling. Nature 431 (2004) 205-211
91. Seo S.R., Ferrand N., Faresse N., Prunier C., Abecassis L., Pessah M., Bourgeade M.F., and Atfi A. Nuclear retention of the tumor suppressor cPML by the homeodomain protein TGIF restricts TGF-beta signaling. Mol. Cell 23 (2006) 547-559
92. Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., and Weinberg R.A. TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation. Nature Cell Biol. 3 (2001) 708-714
93. Kawai T., Akira S., and Reed J.C. ZIP kinase triggers apoptosis from nuclear PML oncogenic domains. Mol. Cell Biol. 23 (2003) 6174-6186
94. Diaz-Meco M.T., Municio M.M., Frutos S., Sanchez P., Lozano J., Sanz L., and Moscat J. The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C. Cell 86 (1996) 777-786
95. Roussigne M., Cayrol C., Clouaire T., Amalric F., and Girard J.P. THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis-response-4 (Par-4) to PML nuclear bodies. Oncogene 22 (2003) 2432-2442
96. Kogel D., Reimertz C., Dussmann H., Mech P., Scheidtmann K.H., and Prehn J.H. The death associated protein (DAP) kinase homologue Dlk/ZIP kinase induces p19ARF- and p53-independent apoptosis. Eur. J. Cancer 39 (2003) 249-256
97. Yang S., Kuo C., Bisi J.E., and Kim M.K. PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2. Nature Cell Biol. 4 (2002) 865-870
98. Trotman L.C., Alimonti A., Scaglioni P.P., Koutcher J.A., Cordon-Cardo C., and Pandolfi P.P. Identification of a tumour suppressor network opposing nuclear Akt function. Nature 441 (2006) 523-527
99. Xu Z.X., Zhao R.X., Ding T., Tran T.T., Zhang W., Pandolfi P.P., and Chang K.S. Promyelocytic leukemia protein 4 induces apoptosis by inhibition of survivin expression. J. Biol. Chem. 279 (2004) 1838-1844
100. Dundr M., Hebert M.D., Karpova T.S., Stanek D., Xu H., Shpargel K.B., Meier U.T., Neugebauer K.M., Matera A.G., and Misteli T. In vivo kinetics of Cajal body components. J. Cell Biol. 164 (2004) 831-842
101. Wiesmeijer K., Molenaar C., Bekeer I.M., Tanke H.J., and 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 (2002) 180-188
102. Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., and Pandolfi P.P. PML regulates p53 stability by sequestering Mdm2 to the nucleolus. Nature Cell Biol. 6 (2004) 665-672
103. Sun J., Xu H., Subramony S.H., and Hebert M.D. Interactions between coilin and PIASy partially link Cajal bodies to PML bodies. J. Cell Sci. 118 (2005) 4995-5003
104. Cioce M., Boulon S., Matera A.G., and Lamond A.I. UV-induced fragmentation of Cajal bodies. J. Cell Biol. 175 (2006) 401-413
105. Ochs R.L., Stein Jr. T.W., and Tan E.M. Coiled bodies in the nucleolus of breast cancer cells. J. Cell Sci. 107 Pt 2 (1994) 385-399
106. Mayer C., and Grummt I. Cellular stress and nucleolar function. Cell Cycle 4 (2005) 1036-1038
107. Condemine W., Takahashi Y., Le Bras M., and de The H. A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells. J. Cell Sci. 120 (2007) 3219-3227
108. Stark L.A., and Dunlop M.G. Nucleolar sequestration of RelA (p65) regulates NF-kappaB-driven transcription and apoptosis. Mol. Cell Biol. 25 (2005) 5985-6004
109. Thoms H.C., Dunlop M.G., and Stark L.A. CDK4 inhibitors and apoptosis: a novel mechanism requiring nucleolar targeting of RelA. Cell Cycle 6 (2007) 1293-1297
110. Thoms H.C., Dunlop M.G., and Stark L.A. p38-mediated inactivation of cyclin D1/cyclin-dependent kinase 4 stimulates nucleolar translocation of RelA and apoptosis in colorectal cancer cells. Cancer Res. 67 (2007) 1660-1669
111. Korgaonkar C., Hagen J., Tompkins V., Frazier A.A., Allamargot C., Quelle F.W., and Quelle D.E. Nucleophosmin (B23) targets ARF to nucleoli and inhibits its function. Mol. Cell Biol. 25 (2005) 1258-1271
112. Lee C., Smith B.A., Bandyopadhyay K., and Gjerset R.A. DNA damage disrupts the p14ARF-B23(nucleophosmin) interaction and triggers a transient subnuclear redistribution of p14ARF. Cancer Res. 65 (2005) 9834-9842
113. Tago K., Chiocca S., and Sherr C.J. Sumoylation induced by the Arf tumor suppressor: a p53-independent function. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 7689-7694
114. Weber J.D., Taylor L.J., Roussel M.F., Sherr C.J., and Bar-Sagi D. Nucleolar Arf sequesters Mdm2 and activates p53. Nature Cell Biol. 1 (1999) 20-26
115. Moulin S., Llanos S., Kim S.H., and Peters G. Binding to nucleophosmin determines the localization of human and chicken ARF but not its impact on p53. Oncogene (2007)
116. Kerr L.E., Birse-Archbold J.L., Short D.M., McGregor A.L., Heron I., Macdonald D.C., Thompson J., Carlson G.J., Kelly J.S., McCulloch J., and Sharkey J. Nucleophosmin is a novel Bax chaperone that regulates apoptotic cell death. Oncogene 26 (2007) 2554-2562
117. Song Z., and Wu M. Identification of a novel nucleolar localization signal and a degradation signal in Survivin-deltaEx3: a potential link between nucleolus and protein degradation. Oncogene 24 (2005) 2723-2734
118. Gurrieri C., Capodieci P., Bernardi R., Scaglioni P.P., Nafa K., Rush L.J., Verbel D.A., Cordon-Cardo C., and Pandolfi P.P. Loss of the tumor suppressor PML in human cancers of multiple histologic origins. J. Natl. Cancer Inst. 96 (2004) 269-279
119. Gurrieri C., Nafa K., Merghoub T., Bernardi R., Capodieci P., Biondi A., Nimer S., Douer D., Cordon-Cardo C., Gallagher R., and Pandolfi P.P. Mutations of the PML tumor suppressor gene in acute promyelocytic leukemia. Blood 103 (2004) 2358-2362
120. Bernardi R., Guernah I., Jin D., Grisendi S., Alimonti A., Teruya-Feldstein J., Cordon-Cardo C., Simon M.C., Rafii S., and Pandolfi P.P. PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR. Nature 442 (2006) 779-785
121. Guccione E., Lethbridge K.J., Killick N., Leppard K.N., and Banks L. HPV E6 proteins interact with specific PML isoforms and allow distinctions to be made between different POD structures. Oncogene 23 (2004) 4662-4672
122. Herzer K., Weyer S., Krammer P.H., Galle P.R., and Hofmann T.G. Hepatitis C virus core protein inhibits tumor suppressor protein promyelocytic leukemia function in human hepatoma cells. Cancer Res. 65 (2005) 10830-10837
123. Wang Z.Y., and Chen Z. Acute promyelocytic leukemia: from highly fatal to highly curable. Blood 111 (2008) 2505-2515
124. Kastner P., Perez A., Lutz Y., Rochette-Egly C., Gaub M.P., Durand B., Lanotte M., Berger R., and Chambon P. Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins. EMBO J. 11 (1992) 629-642
125. Koken M.H., Puvion-Dutilleul F., Guillemin M.C., Viron A., Linares-Cruz G., Stuurman N., de Jong L., Szostecki C., Calvo F., Chomienne C., et al. The t(15;17) translocation alters a nuclear body in a retinoic acid-reversible fashion. EMBO J. 13 (1994) 1073-1083
126. Testa U., Grignani F., Samoggia P., Zanetti C., Riccioni R., Lo Coco F., Diverio D., Felli N., Passerini C.G., Grell M., Pelicci P.G., and Peschle C. The PML/RARalpha fusion protein inhibits tumor necrosis factor-alpha-induced apoptosis in U937 cells and acute promyelocytic leukemia blasts. J. Clin. Invest. 101 (1998) 2278-2289
127. Grignani F., Ferrucci P.F., Testa U., Talamo G., Fagioli M., Alcalay M., Mencarelli A., Grignani F., Peschle C., Nicoletti I., et al. The acute promyelocytic leukemia-specific PML-RAR alpha fusion protein inhibits differentiation and promotes survival of myeloid precursor cells. Cell 74 (1993) 423-431
128. Nervi C., Poindexter E.C., Grignani F., Pandolfi P.P., Lo Coco F., Avvisati G., Pelicci P.G., and Jetten A.M. Characterization of the PML-RAR alpha chimeric product of the acute promyelocytic leukemia-specific t(15;17) translocation. Cancer Res. 52 (1992) 3687-3692
129. Yoshida H., Kitamura K., Tanaka K., Omura S., Miyazaki T., Hachiya T., Ohno R., and Naoe T. Accelerated degradation of PML-retinoic acid receptor alpha (PML-RARA) oncoprotein by all-trans-retinoic acid in acute promyelocytic leukemia: possible role of the proteasome pathway. Cancer Res. 56 (1996) 2945-2948
130. Hayakawa F., and Privalsky M.L. Phosphorylation of PML by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis. Cancer Cell 5 (2004) 389-401
131. Joe Y., Jeong J.H., Yang S., Kang H., Motoyama N., Pandolfi P.P., Chung J.H., and Kim M.K. ATR, PML, and CHK2 play a role in arsenic trioxide-induced apoptosis. J. Biol. Chem. 281 (2006) 28764-28771
132. Muller S., Miller Jr. W.H., and Dejean A. Trivalent antimonials induce degradation of the PML-RAR oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells. Blood 92 (1998) 4308-4316
133. Chen G.Q., Zhu J., Shi X.G., Ni J.H., Zhong H.J., Si G.Y., Jin X.L., Tang W., Li X.S., Xong S.M., Shen Z.X., Sun G.L., Ma J., Zhang P., Zhang T.D., Gazin C., Naoe T., Chen S.J., Wang Z.Y., and Chen Z. In vitro studies on cellular and molecular mechanisms of arsenic trioxide (As2O3) in the treatment of acute promyelocytic leukemia: As2O3 induces NB4 cell apoptosis with downregulation of Bcl-2 expression and modulation of PML-RAR alpha/PML proteins. Blood 88 (1996) 1052-1061
134. Altucci L., Rossin A., Raffelsberger W., Reitmair A., Chomienne C., and Gronemeyer H. Retinoic acid-induced apoptosis in leukemia cells is mediated by paracrine action of tumor-selective death ligand TRAIL. Nature Med. 7 (2001) 680-686
135. Andre C., Guillemin M.C., Zhu J., Koken M.H., Quignon F., Herve L., Chelbi-Alix M.K., Dhumeaux D., Wang Z.Y., Degos L., Chen Z., and de The H. The PML and PML/RARalpha domains: from autoimmunity to molecular oncology and from retinoic acid to arsenic. Exp. Cell Res. 229 (1996) 253-260
136. Lallemand-Breitenbach V., Zhu J., Puvion F., Koken M., Honore N., Doubeikovsky A., Duprez E., Pandolfi P.P., Puvion E., Freemont P., and de The H. Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation. J. Exp. Med. 193 (2001) 1361-1371
137. Lallemand-Breitenbach V., Jeanne M., Benhenda S., Nasr R., Lei M., Peres L., Zhou J., Zhu J., Raught B., and de The H. Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway. Nature Cell Biol. 10 (2008) 547-555
138. Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., and Hay R.T. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nature Cell Biol. 10 (2008) 538-546
139. Barr S.M., Leung C.G., Chang E.E., and Cimprich K.A. ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation. Curr. Biol. 13 (2003) 1047-1051
140. Scaglioni P.P., Yung T.M., Cai L.F., Erdjument-Bromage H., Kaufman A.J., Singh B., Teruya-Feldstein J., Tempst P., and Pandolfi P.P. A CK2-dependent mechanism for degradation of the PML tumor suppressor. Cell 126 (2006) 269-283
141. Kogel D., Bierbaum H., Preuss U., and Scheidtmann K.H. C-terminal truncation of Dlk/ZIP kinase leads to abrogation of nuclear transport and high apoptotic activity. Oncogene 18 (1999) 7212-7218
142. von Mikecz A., Zhang S., Montminy M., Tan E.M., and Hemmerich P. CREB-binding protein (CBP)/p300 and RNA polymerase II colocalize in transcriptionally active domains in the nucleus. J. Cell Biol. 150 (2000) 265-273
143. S. Weidtkamp-Peters, T. Lenser, D. Negorev, N. Gerstner, T.G. Hofmann, G. Schwanitz, C. Hoischen, G. Maul, P. Dittrich, P. Hemmerich, Dynamics of component exchange at PML nuclear bodies, J. Cell. Sci. (in press). doi: 10.1242/jcs.031922.