Finding a role for PML in APL pathogenesis: A critical assessment of potential PML activities

Leukemia

Volumn 16, Issue 10, 2002, Pages 1906-1917

  Strudwick, S ^a   Borden, K L B ^a  

^a NEW YORK UNIVERSITY   (United States)

Author keywords

APL; eIF4E; ND10; PML; POD; RING

Indexed keywords

NUCLEAR PROTEIN; RETINOIC ACID; ZINC FINGER PROTEIN;

APOPTOSIS; BIOCHEMISTRY; BLAST CELL; CELL AGING; CELL CYCLE G1 PHASE; CELL DIFFERENTIATION; CELL FUNCTION; CELL NUCLEUS INCLUSION BODY; CELL TRANSFORMATION; CONTROLLED STUDY; GENE EXPRESSION; HUMAN; HUMAN CELL; LEUKEMIA REMISSION; MAMMAL CELL; MEDICAL RESEARCH; MITOSIS INHIBITION; MOLECULAR BIOLOGY; PATHOGENESIS; PRIORITY JOURNAL; PROMYELOCYTIC LEUKEMIA; PROTEIN FUNCTION; PROTEIN LOCALIZATION; REVIEW;

EID: 0036798404     PISSN: 08876924     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.leu.2402724     Document Type: Review

References (151)

1. Melnick A, Licht JD. Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia. Blood 1999; 93: 3167-3215.
2. Grimwade D, Solomon E. Characterisation of the PML/RAR alpha rearrangement associated with t(15;17) acute promyelocytic leukaemia. Curr Top Microbiol Immunol 1997; 220: 81-112.
3. de Thé H, Chomienne C, Lanotte M, Degos L, Dejean A. The t(15;17) translocation of acute promyelocytic leukaemia fuses the retinoic acid receptor alpha gene to a novel transcribed locus. Nature 1990; 347: 558-561.
4. de Thé H, Lavau C, Marchio A, Chomienne C, Degos L, Dejean A. The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 1991; 66: 675-684.
5. Rowley JD, Golomb HM, Dougherty C. 15/17 translocation, a consistent chromosomal change in acute promyelocytic leukaemia. Lancet 1977; 1: 549-550.
6. Kogan SC, Bishop JM. Acute promyelocytic leukemia: from treatment to genetics and back. Oncogene 1999; 18: 5261-5267.
7. Daniel MT, Koken M, Romagne O, Barbey S, Bazarbachi A, Stadler M, Guillemin MC, Degos L, Chomienne C, de Thé H. PML protein expression in hematopoietic and acute promyelocytic leukemia cells. Blood 1993; 82: 1858-1867.
8. Mu ZM, Chin KV, Liu JH, Lozano G, Chang KS. PML, a growth suppressor disrupted in acute promyelocytic leukemia. Mol Cell Biol 1994; 14: 6858-6867.
9. Minucci S, Nervi C, Lo Coco F, Pelicci PG. Histone deacetylases: a common molecular target for differentiation treatment of acute myeloid leukemias? Oncogene 2001; 20: 3110-3115.
10. Borden KLB, Campbell Dwyer H, Salvato MS. The promyelocytic leukemia protein PML has a pro-apoptotic activity mediated through its RING domain. FEBS Lett 1997; 418: 30-34.
11. Chan JY, Li L, Fan YH, Mu ZM, Zhang WW, Chang KS. Cell-cycle regulation of DNA damage-induced expression of the suppressor gene PML. Biochem Biophys Res Commun 1997; 240: 640-646.
12. Le XF, Yang P, Chang KS. Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene, PML. J Biol Chem 1996; 271: 130-135.
13. Le XF, Vallian S, Mu ZM, Hung MC, Chang KS. Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis. Oncogene 1998; 16: 1839-1849.
14. Cohen N, Sharma M, Kentsis A, Perez JM, Strudwick S, Borden KL. PML RING suppresses oncogenic transformation by reducing the affinity of elF4E for mRNA. EMBO J 2001; 20: 4547-4559.
15. Wang ZG, Ruggero D, Ronchetti S, Zhong S, Gaboli M, Rivi R, Pandolfi PP. PML is essential for multiple apoptotic pathways. Nat Genet 1998; 20: 266-272.
16. Flenghi L, Fagioli M, Tomassoni L, Pileri S, Gambacorta M, Pacini R, Grignani F, Casini T, Ferrucci PF, Martelli MF, Pelici PG, Falini B. 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 1995; 85: 1871-1880.
17. Terris B, Baldin V, Dubois S, Degott C, Flejou JF, Henin D, Dejean A. PML nuclear bodies are general targets for inflammation and cell proliferation. Cancer Res 1995; 55: 1590-1597.
18. Seeler JS, Dejean A. The PML nuclear bodies: actors or extras? Curr Opin Genet Dev 1999; 9: 362-367.
19. Maul GG, Negorev D, Bell P, Ishov AM. Review: properties and assembly mechanisms of ND10, PML bodies, or PODs. J Struct Biol 2000; 129: 278-287.
20. Huang ME, Ye YC, Chen SR, Chai JR, Lu JX, Zhoa L, Gu LJ, Wang ZY. Use of all-trans retinoic acid in the treatment of acute promyelocytic leukemia. Blood 1988; 72: 567-572.
21. Weis K, Rambaud S, Lavau C, Jansen J, Carvalho T, Carmo-Fonseca M, Lamond A, Dejean A. Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell 1994; 76: 345-356.
22. Wang ZG, Delva L, Gaboli M, Rivi R, Giorgio M, Cordon-Cardo C, Grosveld F, Pandolfi PP. Role of PML in cell growth and the retinoic acid pathway. Science 1998; 279: 1547-1551.
23. Borden KLB. Pondering the PML puzzle: possible functions for promyelocytic leukemia PML nuclear bodies. Mol Cell Biol 2002; 22: 5259-5269.
24. Borden KL. RING domains: master builders of molecular scaffolds? J Mol Biol 2000; 295: 1103-1112.
25. Kentsis A, Borden K. Construction of macromolecular assemblages in eukaryotic processes and their role in human disease: linking RINGs together. Curr Peptide Prot Sci 2000; 1: 49-74.
26. Goddard AD, Borrow J, Freemont PS, Solomon E. Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia. Science 1991; 254: 1371-1374.
27. Borden KLB, Boddy MN, Lally J, O'Reilly NJ, Martin S, Howe K, Solomon E, Freemont PS. The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. EMBO J 1995; 14: 1532-1541.
28. Borden KLB, Lally JM, Martin SR, O'Reilly NJ, Solomon E, Freemont PS. In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML. Proc Natl Acad Sci USA 1996; 93: 1601-1606.
29. Jensen K, Shiels C, Freemont PS. PML protein isoforms and the RBCC/TRIM motif. Oncogene 2001; 20: 7223-7233.
30. Negorev D, Maul GG. Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene 2001; 20: 7234-7242.
31. Lai HK, Borden KL. The promyelocytic leukemia (PML) protein suppresses cyclin D1 protein production by altering the nuclear cytoplasmic distribution of cyclin D1 mRNA. Oncogene 2000; 19: 1623-1634.
32. Stuurman N, de Graaf A, Floore A, Josso A, Humbel B, de Jong L, van Driel R. A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies. J Cell Sci 1992; 101: 773-784.
33. Everett RD, Lomonte P, Sternsdorf T, van Driel R, Orr A. Cell cycle regulation of PML modification and ND10 composition. J Cell Sci 1999; 112: 4581-4588.
34. Fagioli M, Alcalay M, Pandolfi PP, Venturini L, Mencarelli A, Simeone A, Acampora D, Grignani F, Pelicci PG. Alternative splicing of PML transcripts predicts coexpression of several carboxy-terminally different protein isoforms. Oncogene 1992; 7: 1083-1091.
35. Maul GG, Yu E, Ishov AM, Epstein AL. Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress. J Cell Biochem 1995; 59: 498-513.
36. Everett RD. DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 2001; 20: 7266-7273.
37. Regad T, Chelbi-Alix MK. Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene 2001; 20: 7274-7286.
38. Lanotte M, Martin-Thouvenin V, Najman S, Balerini P, Valensi F, Berger R. NB4, a maturation inducible cell line with t(15;17) marker isolated from a human acute promyelocytic leukemia (M3). Blood 1991; 77: 1080-1086.
39. Benoit G, Roussel M, Pendino F, Segal-Bendirdjian E, Lanotte M. Orchestration of multiple arrays of signal cross-talk and combinatorial interactions for maturation and cell death: another vision of t(15;17) preleukemic blast and APL-cell maturation. Oncogene 2001; 20: 7161-7177.
40. Roussel MJ, Lanotte M. Maturation sensitive and resistant t(15;17) NB4 cell lines as tools for APL physiopathology: nomenclature of cells and repertory of their known genetic alterations and phenotypes. Oncogene 2001; 20: 7287-7291.
41. Duprez E, Lillehaug JR, Gaub MP, Lanotte M. Differential changes of retinoid-X-receptor (RXR alpha) and its RAR alpha and PML-RAR alpha partners induced by retinoic acid and cAMP distinguish maturation sensitive and resistant t(15;17) promyelocytic leukemia NB4 cells. Oncogene 1996; 12: 2443-2450.
42. Duprez E, Lillehaug JR, Naoe T, Lanotte M. cAMP signalling is decisive for recovery of nuclear bodies (PODs) during maturation of RA-resistant t(15;17) promyelocytic leukemia NB4 cells expressing PML-RAR alpha. Oncogene 1996; 12: 2451-2459.
43. 3 induces NB4 cell apoptosis with downregulation of Bcl-2 expression and modulation of PML-RAR alpha/PML proteins. Blood 1996; 88: 1052-1061.
44. 3 exerts dose-dependent dual effects on APL cells. Blood 1997; 89: 3345-3353.
45. Zhu J, Koken MH, Quignon F, Chelbi-Alix MK, Degos L, Wang ZY, Chen Z, de Thé H. Arsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemia. Proc Natl Acad Sci USA 1997; 94: 3978-3983.
46. Wang XW, Tseng A, Ellis NA, Spillare EA, Linke SP, Robles AI, Seker H, Yang Q, Hu P, Beresten S, Bemmels NA, Garfield S, Harris CC. Functional interaction of p53 and BLM DNA helicase in apoptosis. J Biol Chem 2001; 276: 32948-32955.
47. LaMorte VJ, Dyck JA, Ochs RL, Evans RM. Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc Natl Acad Sci USA 1998; 95: 4991-4996.
48. Borden KLB, Campbell Dwyer EJ, Carlile GW, Djavani M, Salvato MS. Two RING finger proteins, the oncoprotein PML and the arenavirus Z protein, colocalize with the nuclear fraction of the ribosomal P proteins. J Virol 1998; 72: 3819-3826.
49. Tsukamoto T, Hashiguchi N, Janicki SM, Tumbar T, Belmont AS, Spector DL. Visualization of gene activity in living cells. Nat Cell Biol 2000; 2: 871-878.
50. Boddy MN, Howe K, Etkin LD, Solomon E, Freemont PS. 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 1996; 13: 971-982.
51. Duprez E, Saurin AJ, Desterro JM, Lallemand-Breitenbach V, Howe K, Boddy MN, Solomon E, de The H, Hay RT, Freemont PS. SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation. J Cell Sci 1999; 112: 381-393.
52. Topcu Z, Mack DL, Hromas RA, Borden KL. The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control. Oncogene 1999; 18: 7091-7100.
53. Melchior F. SUMO - nonclassical ubiquitin. Annu Rev Cell Dev Biol 2000; 16: 591-626.
54. Boddy MN, Duprez E, Borden KL, Freemont PS. Surface residue mutations of the PML RING finger domain alter the formation of nuclear matrix-associated PML bodies. J Cell Sci 1997; 110: 2197-2205.
55. Ishov AM, Sotnikov AC, Negorev D, Vladimirova OV, Neff N, Kamitani T, Yeh ET, Strauss JF, 3rd, Maul GG. 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 1999; 147: 221-234.
56. Kentsis A, Dwyer EC, Perez JM, Sharma M, Chen A, Pan ZQ Borden KL. The RING domains of the promyelocytic leukemia protein PML and the arenaviral protein Z repress translation by directly inhibiting translation initiation factor elF4E. J Mol Biol 2001; 312: 609-623.
57. Grande MA, van der Kraan I, van Steensel B, Schul W, de Thé H, van der Voort HT, de Jong L, van Driel R. PML-containing nuclear bodies: their spatial distribution in relation to other nuclear components. J Cell Biochem 1996; 63: 280-291.
58. Shiels C, Islam SA, Vatcheva R, Sasieni P, Sternberg MJ, Freemont PS, Sheer D. PML bodies associate specifically with the MHC gene cluster in interphase nuclei. J Cell Sci 2001; 114: 3705-3716.
59. Schul W, van Der Kraan I, Matera AG, van Driel R, de Jong L. Nuclear domains enriched in RNA 3′-processing factors associate with coiled bodies and histone genes in a cell cycle-dependent manner. Mol Biol Cell 1999; 10: 3815-3824.
60. Fu XD, Maniatis T. The 35-kDa mammalian splicing factor SC35 mediates specific interactions between U1 and U2 small nuclear ribonucleoprotein particles at the 3′ splice site. Proc Natl Acad Sci USA 1992; 89: 1725-1729.
61. Gall JG. Cajal bodies: The first 100 years. Annu Rev Cell Dev Biol 2000; 16: 273-300.
62. Gottifredi V, Prives C. P53 and PML: new partners in tumor suppression. Trends Cell Biol 2001; 11: 184-187.
63. Pearson M, Pelicci PG. PML interaction with p53 and its role in apoptosis and replicative senescence. Oncogene 2001; 20: 7250-7256.
64. Li H, Chen JD. PML and the oncogenic nuclear domains in regulating transcriptional repression. Curr Opin Cell Biol 2000; 12: 641-644.
65. Doucas V. The promyelocytic (PML) nuclear compartment and transcription control. Biochem Pharmacol 2000; 60: 1197-1201.
66. Vallian S, Gaken JA, Trayner ID, Gingold EB, Kouzarides T, Chang KS, Farzaneh F. Transcriptional repression by the promyelocytic leukemia protein, PML. Exp Cell Res 1997; 237: 371-382.
67. Alcalay M, Tomassoni L, Colombo E, Stoldt S, Grignani F, Fagioli M, Szekely L, Helin K, Pelicci PG. The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol Cell Biol 1998; 18: 1084-1093.
68. Ferbeyre G, de Stanchina E, Querido E, Baptiste N, Prives C, Lowe SW. PML is induced by oncogenic ras and promotes premature senescence. Genes Dev 2000; 14: 2015-2027.
69. Boisvert FM, Kruhlak MJ, Box AK, Hendzel MJ, Bazett-Jones DP. The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J Cell Biol 2001; 152: 1099-1106.
70. Doucas V, Tini M, Egan DA, Evans RM. Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. Proc Natl Acad Sci USA 1999; 96: 2627-2632.
71. Pearson M, Carbone R, Sebastiani C, Cioce M, Fagioli M, Saito S, Higashimoto Y, Appella E, Minucci S, Pandolfi PP, Pelicci PG. PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 2000; 406: 207-210.
72. Khan MM, Nomura T, Kim H, Kaul SC, Wadhwa R, Shinagawa T, Ichikawa-Iwata E, Zhong S, Pandolfi PP, Ishii S. Role of PML and PML-RARalpha in Mad-mediated transcriptional repression. Mol Cell 2001; 7: 1233-1243.
73. Jepsen K, Hermanson O, Onami TM, Gleiberman AS, Lunyak V, McEvilly RJ, Kurokawa R, Kumar V, Liu F, Seto E, Hedrick SM, Mandel C, Glass CK, Rose DW, Rosenfeld MG. Combinatorial roles of the nuclear receptor corepressor in transcription and development. Cell 2000; 102: 753-763.
74. McMahon C, Suthiphongchai T, DiRenzo J, Ewen ME. P/CAF associates with cyclin D1 and potentiates its activation of the estrogen receptor. Proc Natl Acad Sci USA 1999; 96: 5382-5387.
75. Guiochon-Mantel A, Savouret JF, Quignon F, Delabre K, Milgrom E, De Thé H. Effect of PML and PML-RAR on the transactivation properties and subcellular distribution of steroid hormone receptors. Mol Endocrinol 1995; 9: 1791-1803.
76. Abid MR, Li Y, Anthony C, De Benedetti A. Translational regulation of ribonucleotide reductase by eukaryotic initiation factor 4E links protein synthesis to the control of DNA replication. J Biol Chem 1999; 274: 35991-35998.
77. Gingras AC, Raught B, Sonenberg N. elF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu Rev Biochem 1999; 68: 913-963.
78. Sonenberg N, Gingras AC. The mRNA 5′ cap-binding protein elF4E and control of cell growth. Curr Opin Cell Biol 1998; 10: 268-275.
79. Lejbkowicz F, Goyer C, Darveau A, Neron S, Lemieux R, Sonenberg N. A fraction of the mRNA 5′ cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus. Proc Natl Acad Sci USA 1992; 89: 9612-9616.
80. Iborra FJ, Jackson DA, Cook PR. Coupled transcription and translation within nuclei of mammalian cells. Science 2001, 293: 1139-1142.
81. Ptushkina M, von der Haar T, Vasilescu S, Frank R, Birkenhager R, McCarthy JE. Cooperative modulation by elF4G of elF4E-binding to the mRNA 5′ cap in yeast involves a site partially shared by p20. EMBO J 1998; 17: 4798-4808.
82. Ptushkina M, von der Haar T, Karim MM, Hughes JM, McCarthy JE. Repressor binding to a dorsal regulatory site traps human elF4E in a high cap-affinity state. EMBO J 1999; 18: 4068-4075.
83. Lang V, Zanchin NI, Lunsdorf H, Tuite M, McCarthy JE. Initiation factor elF-4E of Saccharomyces cerevisiae. Distribution within the cell, binding to mRNA, and consequences of its overproduction. J Biol Chem 1994; 269: 6117-6123.
84. Strudwick S, Borden KLB. The emerging roles of translation factor elF4E in the nucleus. Differentiation 2002; 70 10-22.
85. Dostie J, Lejbkowicz F, Sonenberg N. Nuclear eukaryotic initiation factor 4E (elF4E) colocalizes with splicing factors in speckles. J Cell Biol 2000; 148: 239-247.
86. McCubbin WD, Edery I, Altmann M, Sonenberg N, Kay CM. Circular dichroism and fluorescence studies on protein synthesis initiation factor elF-4E and two mutant forms from the yeast Saccharomyces cerevisiae. J Biol Chem 1988; 263: 17663-17671.
87. von Der Haar T, Ball PD, McCarthy JE. Stabilization of eukaryotic initiation factor 4E binding to the mRNA 5′-cap by domains of elF4G. J Biol Chem 2000; 275: 30551-30555.
88. Cai A, Jankowska-Anyszka M, Centers A, Chlebicka L, Stepinski J, Stolarski R, Darzynkiewicz E, Rhoads RE. Quantitative assessment of mRNA cap analogues as inhibitors of in vitro translation. Biochemistry 1999; 38: 8538-8547.
89. De Benedetti A, Joshi B, Graff JR, Zimmer SG. CHO cells transformed by the translation factor elF-4E display increased c-myc expression, but require overexpression of Max for tumorigenicity. Mol Cell Diff 1994; 2: 347-371.
90. Kevil CG, De Benedetti A, Payne DK, Coe LL, Laroux FS, Alexander JS. Translational regulation of vascular permeability factor by eukaryotic initiation factor 4E: implications for tumor angiogenesis. Int J Cancer 1996; 65: 785-790.
91. Rosenwald IB, Lazaris-Karatzas A, Sonenberg N, Schmidt EV. Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor 4E. Mol Cell Biol 1993; 13: 7358-7363.
92. Rosenwald IB, Kaspar R, Rousseau D, Gehrke L, Leboulch P, Chen JJ, Schmidt EV, Sonenberg N, London IM. Eukaryotic translation initiation factor 4E regulates expression of cyclin D1 at transcriptional and post-transcriptional levels. J Biol Chem 1995; 270: 21176-21180.
93. Shantz LM, Pegg AE. Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation. Cancer Res 1994; 54: 2313-2316.
94. Shantz LM, Hu RH, Pegg AE. Regulation of ornithine decarboxylase in a transformed cell line that overexpresses translation initiation factor elF-4E. Cancer Res 1996; 56: 3265-3269.
95. Polunovsky VA, Rosenwald IB, Tan AT, White J, Chiang L, Sonenberg N, Bitterman PB. Translational control of programmed cell death: eukaryotic translation initiation factor 4E blocks apoptosis in growth-factor-restricted fibroblasts with physiologically expressed or deregulated Myc. Mol Cell Biol 1996; 16: 6573-6581.
96. Lazaris-Karatzas A, Montine KS, Sonenberg N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap. Nature 1990; 345: 544-547.
97. Zimmer SG, DeBenedetti A, Graff JR. Translational control of malignancy: The mRNA cap-binding protein, elF-4E, as a central regulator of tumor formation, growth, invasion and metastasis. Anticancer Res 2000; 20: 1343-1351.
98. Rousseau D, Kaspar R, Rosenwald I, Gehrke L, Sonenberg N. Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E. Proc Natl Acad Sci USA 1996; 93: 1065-1070.
99. Haghighat A, Sonenberg N. elF4G dramatically enhances the binding of elF4E to the mRNA 5′-cap structure. J Biol Chem 1997; 272: 21677-21680.
100. Grolleau A, Wietzerbin J, Beretta L. Defect in the regulation of 4E-BP1 and 2, two repressors of translation initiation, in the retinoid acid resistant cell lines, NB4-R1 and NB4-R2. Leukemia 2000; 14: 1909-1914.
101. Desbois C, Rousset R, Bantignies F, Jalinot P. Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I Tax oncoprotein. Science 1996; 273: 951-953.
102. Morris-Desbois C, Bochard V, Reynaud C, Jalinot P. Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies. J Cell Sci 1999; 112: 3331-3342.
103. Gongora C, David G, Pintard L, Tissot C, Hua TD, Dejean A, Mechti N. Molecular cloning of a new interferon-induced PML nuclear body-associated protein. J Biol Chem 1997; 272: 19457-19463.
104. Carlile GW, Tatton WG, Borden KL. Demonstration of a RNA-dependent nuclear interaction between the promyelocytic leukaemia protein and glyceraldehyde-3-phosphate dehydrogenase. Biochem J 1998; 335: 691-696.
105. Nguyen LH, Espert L, Mechti N, Wilson DM, 3rd. The human interferon- and estrogen-regulated ISG20/HEM45 gene product degrades single-stranded RNA and DNA in vitro. Biochemistry 2001; 40: 7174-7179.
106. Nagy E, Rigby WF. Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD(+)-binding region (Rossmann fold). J Biol Chem 1995; 270: 2755-2763.
107. Singh R, Green MR. Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science 1993; 259: 365-368.
108. Vareli K, Frangou-Lazaridis M, van der Kraan I, Tsolas O, van Driel R. Nuclear distribution of prothymosin alpha and parathymosin: evidence that prothymosin alpha is associated with RNA synthesis processing and parathymosin with early DNA replication. Exp Cell Res 2000; 257: 152-161.
109. Yeager TR, Neumann AA, Englezou A, Huschtscha LI, Noble JR, Reddel RR. Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body. Cancer Res 1999; 59: 4175-4179.
110. Ford LP, Zou Y, Pongracz K, Gryaznov SM, Shay JW, Wright WE. Telomerase can inhibit the recombination-based pathway of telomere maintenance in human cells. J Biol Chem 2001; 276: 32198-32203.
111. Grobelny JV, Godwin AK, Broccoli D. ALT-associated PML bodies are present in viable cells and are enriched in cells in the G(2)/M phase of the cell cycle. J Cell Sci 2000; 113: 4577-4585.
112. Hachiya Y, Motonaga K, Itoh M, Masuko T, Enomoto T, Sonobe H, Takashima S. Immunohistochemical expression and pathogenesis of BLM in the human brain and visceral organs. Neuropathology 2001; 21: 123-128.
113. Turley H, Wu L, Canamero M, Gatter KC, Hickson ID. The distribution and expression of the Bloom's syndrome gene product in normal and neoplastic human cells. Br J Cancer 2001; 85: 261-265.
114. Yankiwski V, Marciniak RA, Guarente L, Neff NF. Nuclear structure in normal and Bloom syndrome cells. Proc Natl Acad Sci USA 2000; 97: 5214-5219.
115. Gharibyan V, Youssoufian H. Localization of the Bloom syndrome helicase to punctate nuclear structures and the nuclear matrix and regulation during the cell cycle: comparison with the Werner's syndrome helicase. Mol Carcinog 1999; 26: 261-273.
116. Borden KL, Campbell Dwyer EJ, Salvato MS. An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm. J Virol 1998; 72: 758-766.
117. Turelli P, Doucas V, Craig E, Mangeat B, Klages N, Evans R, Kalpana G, Trono D. Cytoplasmic recruitment of INI1 and PML on incoming HIV preintegration complexes: interference with early steps of viral replication. Mol Cell 2001; 7: 1245-1254.
118. Freemont PS. RING for destruction? Curr Biol 2000; 10: R84-R87.
119. Haghighat A, Mader S, Pause A, Sonenberg N. Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E. EMBO J 1995; 14: 5701-5709.
120. Rousseau D, Gingras AC, Pause A, Sonenberg N. The elF4F-binding proteins 1 and 2 are negative regulators of cell growth. Oncogene 1996; 13: 2415-2420.
121. Yasuda S, Inoue K, Hirabayashi M, Higashiyama H, Yamamoto Y, Fuyuhiro H, Komure O, Tanaka F, Sobue G, Tsuchiya K, Hamada K, Sasaki H, Takeda K, Ichijo H, Kakizuka A. Triggering of neuronal cell death by accumulation of activated SEK1 on nuclear polyglutamine aggregations in PML bodies. Genes Cells 1999; 4: 743-756.
122. Baumann CT, Ma H, Wolford R, Reyes JC, Maruvada P, Lim C, Yen PM, Stallcup MR, Hager GL. The glucocorticoid receptor interacting protein 1 (GRIP1) localizes in discrete nuclear foci that associate with ND10 bodies and are enriched in components of the 26S proteasome. Mol Endocrinol 2001; 15: 485-500.
123. Lallemand-Breitenbach V, Zhu J, Puvion F, Koken M, Honore N, Doubeikovsky A, Duprez E, Pandolfi PP, Puvion E, Freemont P, de Thé 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 2001; 193: 1361-1371.
124. Kentsis A, Gordon RE, Borden KLB. Self-assembly properties of a model RING domain. Proc Natl Acad Sci USA 2002; 99 667-672.
125. Djavani M, Rodas J, Lukashevich IS, Horejsh D, Pandolfi PP, Borden KL, Salvato MS. Role of the promyelocytic leukemia protein PML in the interferon sensitivity of lymphocytic choriomeningitis virus. J Virol 2001; 75: 6204-6208.
126. Chelbi-Alix MK, Quignon F, Pelicano L, Koken MH, de Thé H. Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein. J Virol 1998; 72: 1043-1051.
127. Regad T, Saib A, Lallemand-Breitenbach V, Pandolfi PP, de Thé H, Chelbi-Alix MK. PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator. EMBO J 2001; 20: 3495-3505.
128. Bell P, Montaner LJ, Maul GG. Accumulation and intranuclear distribution of unintegrated human immunodeficiency virus type 1 DNA. J Virol 2001; 75: 7683-7691.
129. Salvato MS, Shimomaye EM. The completed sequence of lymphocytic choriomeningitis virus reveals a unique RNA structure and a gene for a zinc finger protein. Virology 1989; 173: 1-10.
130. MacConnell WP, Kaplan NO. The activity of the acidic phosphoproteins from the 80 S rat liver ribosome. J Biol Chem 1982; 257: 5359-5366.
131. Uchiumi T, Traut RR, Kominami R. Monoclonal antibodies against acidic phosphoproteins P0, P1, and P2 of eukaryotic ribosomes as functional probes. J Biol Chem 1990; 265: 89-95.
132. Campbell Dwyer EJ, Lai H, MacDonald RC, Salvato MS, Borden KL. The lymphocytic choriomeningitis virus RING protein Z associates with eukaryotic initiation factor 4E and selectively represses translation in a RING-dependent manner. J Virol 2000; 74: 3293-3300.
133. Maul GG, Guldner HH, Spivack JG. Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0). J Gen Virol 1993; 74: 2679-2690.
134. Chelbi-Alix MK, de Thé H. Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 1999; 18: 935-941.
135. Everett RD, Earnshaw WC, Findlay J, Lomonte P. Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. Embo J 1999; 18: 1526-1538.
136. Parkinson J, Everett RD. Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins. J Viroll 2000; 74: 10006-10017.
137. Everett RD. ICP0 induces the accumulation of colocalizing conjugated ubiquitin. J Viroll 2000; 74: 9994-10005.
138. Hodges M, Tissot C, Howe K, Grimwade D, Freemont PS. Structure, organization, and dynamics of promyelocytic leukemia protein nuclear bodies. Am J Hum Genet 1998; 63: 297-304.
139. De Benedetti A, Harris AL. elF4E expression in tumors: its possible role in progression of malignancies. Int J Biochem Cell Biol 1999; 31: 59-72.
140. Wang S, Rosenwald IB, Hutzler MJ, Pihan GA, Savas L, Chen JJ, Woda BA. Expression of the eukaryotic translation initiation factors 4E and 2alpha in non-Hodgkin's lymphomas. Am J Pathol 1999; 155: 247-255.
141. Berkel HJ, Turbat-Herrera EA, Shi R, de Benedetti A. Expression of the translation initiation factor elF4E in the polyp-cancer sequence in the colon. Cancer Epidemiol Biomarkers Prev 2001; 10: 663-666.
142. DeFatta RJ, Turbat-Herrera EA, Li BD, Anderson W, De Benedetti A. Elevated expression of elF4E in confined early breast cancer lesions: possible role of hypoxia. Int J Cancer 1999; 80: 516-522.
143. Franklin S, Pho T, Abreo FW, Nassar R, De Benedetti A, Stucker FJ, Nathan CA. Detection of the proto-oncogene elF4E in larynx and hypopharynx cancers. Arch Otolaryngol Head Neck Surg 1999; 125: 177-182.
144. Li BD, McDonald JC, Nassar R, De Benedetti A. Clinical outcome in stage I to III breast carcinoma and elF4E overexpression. Ann Sorg 1998; 227: 756-761; discussion 761-763.
145. Kogan SC, Hong SH, Shultz DB, Privalsky ML, Bishop JM. Leukemia initiated by PMLRARalpha: The PML domain plays a critical role while retinoic acid-mediated transactivation is dispensable. Blood 2000; 95: 1541-1550.
146. Brown D, Kogan S, Lagasse E, Weissman I, Alcalay M, Pelicci PG, Atwater S, Bishop JM. A PMLRARalpha transgene initiates murine acute promyelocytic leukemia. Proc Natl Acad Sci USA 1997; 94: 2551-2556.
147. Bargonetti J, Manfredi JJ. Multiple roles of the tumor suppressor p53. Curr Opin Oncol 2002; 14: 86-91.
148. Rubin DM, Coux O, Wefes I, Hengartner C, Young RA, Goldberg AL, Finley D. Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome. Nature 1996; 379: 655-657.
149. Donehower LA, Harvey M, Slagle BL, McArthur MJ, Montgomery CA Jr, Butel JS, Bradley A. Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours. Nature 1992; 356: 215-221.
150. Topisirovic I, Capili AD, Borden KLB. Interferon γ and cadmium treatments modulate elF4E dependent mRNA transport of cyclin D1 in a PML dependent manner. Mol Cell Biol 2002 (in press).
151. Minucci S, Maccarana M, Cioci M, De Luca P, Gelmetti V, Segalla S, Di Croce L, Giavara S, Matteucci C, Gobbi A, Bianchini A, Colombo E, Schiavoni I, Badaracco G, Hu X, Lazar M, Pelicci PG. Oligomerization of RAR and AML1 transcription factors as a novel mechanism of oncogenic activation. Mol Cell Biol 2000; 5: 811-820.