Characterization of endogenous human promyelocytic leukemia isoforms

Cancer Research

Volumn 66, Issue 12, 2006, Pages 6192-6198

  Condemine, Wilfried ^a   Takahashi, Yuki ^a   Zhu, Jun ^a   Puvion Dutilleul, Francine ^a   Guegan, Sarah ^b   Janin, Anne ^b   De Thé, Hugues ^a  

^a CNRS   (France)

^b INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN P53;

AMINO ACID SEQUENCE; ARTICLE; CELL STRAIN COS1; CENTROSOME; EXON; GENE EXPRESSION; HELA CELL; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STABILITY; PROTEIN TARGETING; TERMINAL SEQUENCE;

ANIMALS; CELL NUCLEUS; CENTROSOME; CERCOPITHECUS AETHIOPS; COS CELLS; HELA CELLS; HUMANS; MICE; NEOPLASM PROTEINS; NEOPLASMS; NUCLEAR PROTEINS; PROTEIN ISOFORMS; RNA, MESSENGER; TRANSCRIPTION FACTORS; TRANSFECTION; TUMOR SUPPRESSOR PROTEINS;

EID: 33745728153     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-3792     Document Type: Article

References (63)

1. de Thé H, Chomienne C, Lanotte M, Degos L, Dejean A. The t(15;17) translocation of acute promyelocytic leukemia fuses the retinoic acid receptor α gene to a novel transcribed locus. Nature 1990;347:558-61.
2. de Thé H, Lavau C, Marchio A, Chomienne C, Degos L, Dejean A. The PML-RAR α fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 1991;66:675-84.
3. Fagioli M, Alcalay M, Pandolfi PP, et al. Alternative splicing of PML transcripts predicts coexpression of several carboxy-terminally different protein isoforms. Oncogene 1992;7:1083-91.
4. Jensen K, Shiels C, Freemont PS. PML protein isoforms and the RBCC/TRIM motif. Oncogene 2001;20:7223-33.
5. Stadler M, Chelbi-Alix MK, Koken MHM, et al. Transcriptional induction of the PML growth suppressor gene by interferons is mediated through an ISRE and a GAS element. Oncogene 1995;11:2565-73.
6. de Stanchina E, Querido E, Narita M, et al. PML is a direct p53 target that modulates p53 effector functions. Mol Cell 2004;13:523-35.
7. Daniel M-T, Koken M, Romagné O, et al. PML protein expression in hematopoietic and acute promyelocytic leukemia cells. Blood 1993;82:1858-67.
8. Flenghi L, Fagioli M, Tomassoni 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 1995;85:1871-80.
9. Koken MHM, Linares-Cruz G, Quignon F, et al. The PML growth-suppressor has an altered expression in human oncogenesis. Oncogene 1995;10:1315-24.
10. Terris B, Baldin V, Dubois S, et al. PML nuclear bodies are general targets for inflammation and cell proliferation. Cancer Res 1995;55:1590-7.
11. Gurrieri C, Capodieci P, Bernardi R, et al. Loss of the tumor suppressor PML in human cancers of multiple histologic origins. J Natl Cancer Inst 2004;96:269-79.
12. Reymond A, Meroni G, Fantozzi A, et al. The tripartite motif family identifies cell compartments. EMBO J 2001;20:2140-51.
13. Kastner P, Perez A, Lutz Y, et al. Structure, localization and transcriptional properties of two classes of retinoic acid receptor α fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins. EMBO J 1992;11:629-42.
14. Lin HK, Bergmann S, Pandolfi PP. Cytoplasmic PML function in TGF-β signalling. Nature 2004;431:205-11.
15. Niikura T, Hashimoto Y, Tajima H, et al. A tripartite motif protein TRIM11 binds and destabilizes Humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults. Eur J Neurosci 2003;17:1150-8.
16. Urano T, Saito T. Tsukui T, et al. Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth. Nature 2002;417:871-5.
17. Uchida D, Hatakeyama S, Matsushima A, et al. AIRE functions as an E3 ubiquitin ligase. J Exp Med 2004;199:167-72.
18. Casaletto JB, Nutt LK, Wu Q, et al. Inhibition of the anaphase-promoting complex by the Xnf7 ubiquitin ligase. J Cell Biol 2005;169:61-71.
19. Duprez E, Saurin AJ, Desterro JM, et al. SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation. J Cell Sci 1999;112:381-93.
20. Kamitani T, Kito K, Nguyen HP, Wada H, Fukuda-Kamitani T, Yeh ETH. Identification of three major sentrinization sites in PML. J Biol Chem 1998;41:26675-82.
21. Lallemand-Breitenbach V, Zhu J, Puvion F, et al. Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, US proteasome recruitment, and As(2)O(3)-induced PML or PML/retinoic acid receptor α degradation. J Exp Med 2001;193:1361-72.
22. Zhu J, Koken MHM, Quignon F, et al. Arsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemia. Proc Natl Acad Sci U S A 1997;94:3978-83.
23. Muller S, Matunis MJ, Dejean A. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J 1998;17:61-70.
24. Salomoni P, Pandolfi PP. The role of PML in tumor suppression. Cell 2002;108:165-70.
25. Ishov AM, Sotnikov AG, Negorev D, 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 1999;147:221-34.
26. Zhong S, Muller S, Ronchetti S, Freemont PS, Dejean A, Pandolfi PP. Role of SUMO-1-modified PML in nuclear body formation. Blood 2000;95:2748-52.
27. Lafarga M, Berciano MT, Pena E, et al. Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes, ubiquitin, and protein substrates of proteasome. Mol Biol Cell 2002;13:2771-82.
28. Li H, Leo C, Zhu J, et al. Sequestration and inhibition of daxx-mediated transcriptional repression by PML. Mol Cell Biol 2000;20:1784-96.
29. Lehembre F, Muller S, Pandolfi PP, Dejean A. Regulation of Pax3 transcriptional activity by SUMO-1-modified PML. Oncogene 2001;20:1-9.
30. Zhong S, Salomoni P, Ronchetti S, Guo A, Ruggero D, Pandolfi PP. Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. J Exp Med 2000;191:631-9.
31. Vallian S, Gäken JA, Trayner ID, et al. Transcriptional repression by the promyelocytic leukemia protein, PML. Exp Cell Res 1997;237:371-82.
32. Wu WS, Vallian S, Seto E, et al. The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol Cell Biol 2001;21:2259-68.
33. Maul GG, Negorev D, Bell P, Ishov AM. Review: properties and assembly mechanisms of ND10, PML Bodies, or PODs. J Struct Biol 2000;129:278-87.
34. Wang ZG, Delva L, Gaboli M, et al. Role of PML in cell growth and the retinoic acid pathway. Science 1998;279:1547-51.
35. Pearson M, Carbone R, Sebastiani C, et al. PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 2000;406:207-10.
36. 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;14:2015-27.
37. Bischof O, Nacerddine K, Dejean A. Human papillomavirus oncoprotein E7 targets the promyelocytic leukemia protein and circumvents cellular senescence via the Rb and p53 tumor suppressor pathways. Mol Cell Biol 2005;25:1013-24.
38. Mallette FA, Goumard S, Gaumont-Leclerc MF, Moiseeva O, Ferbeyre G. Human fibroblasts require the Rb family of tumor suppressors, but not p53, for PML-induced senescence. Oncogene 2004;23:91-9.
39. Louria-Hayon I, Grossman T, Sionov RV, Alsheich O, Pandolfi PP, Haupt Y. The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation. J Biol Chem 2003;278:33134-41.
40. Bernardi R, Scaglioni PP, Bergmann S, Horn HF, Vousden KH, Pandolfi PP. PML regulates p53 stability by sequestering Mdm2 to the nucleolus. Nat Cell Biol 2004;6:665-72.
41. D'Orazi G, Cecchinelli B. Bruno T, et al. Homeo-domain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis. Nat Cell Biol 2002;4:11-9.
42. Hofmann TG, Moller A, Sirma H, et al. Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. Nat Cell Biol 2001;10:10.
43. Xu ZX, Zou WX, Lin P, Chang KS. A role for PML3 in centrosome duplication and genome stability. Mol Cell 2005;17:721-32.
44. Hu P, Beresten SF, van Brabant AJ, et al. Evidence for BLM and topoisomerase IIIα interaction in genomic stability. Hum Mol Genet 2001;10:1287-98.
45. Wang Z-G, Ruggero D, Ronchetti S, et al. PML is essential for multiple apoptotic pathways. Nat Genet 1998;20:266-72.
46. Henderson BR, Eleftheriou A. A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals. Exp Cell Res 2000;256:213-24.
47. Boutell C, Orr A, Everett RD. PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0. J Virol 2003;77:8686-94.
48. Goddard AD, Yuan JQ, Fairbairn L, et al. Cloning of the murine homolog of the leukemia- associated PM1 gene. Mamm Genome 1995;6:732-7.
49. Koken MHM, Puvion-Dutilleul F, Guillemin MC, et al. The t(15;17) translocation alters a nuclear body in a RA-reversible fashion. EMBO J 1994;13:1073-83.
50. Bailly E, Doree M, Nurse P, Bornens M. p34cdc2 is located in both nucleus and cytoplasm; part is centrosomally associated at G2/M and enters vesicles at anaphase. EMBO J 1989;8:3985-95.
51. Puvion-Dutilleul F, Venturini L, Guillemin M-C, de Thé H, Puvion E. Sequestration of PML and Sp100 proteins in an intranuclear viral structure during herpes simplex virus type 1 infection. Exp Cell Res 1995;221:448-61.
52. Ausubel FM, Brent R, Kingston RE, et al. Current protocols in molecular biology. New York: Wiley (Interscience): 1994.
53. Harlow E, Lane D. Antibodies. A laboratory manual. In: NY: Cold Spring Harbor Laboratory; 1988.
54. Falini B, Flenghi L, Fagioli M, et al. Immunocytochemical diagnosis of acute promyelocytic leukemia (M3) with the monoclonal antibody PG-M3 (anti-PML). Blood 1997;90:4046-53.
55. Zhu J, Gianni M, Kopf E, et al. Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor-α (RAH-α) and oncogenic RAR-α fusion proteins. Proc Natl Acad Sci U S A 1999;96:14807-12.
56. Lavau C, Marchio A, Fagioli M. et al. The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene 1995;11:871-6.
57. Beech SJ, Lethbridge KJ, Killick N, McGlincy N, Leppard KN. Isoforms of the promyelocytic leukemia protein differ in their effects on ND10 organization. Exp Cell Res 2005;307:109-17.
58. Borden KL, Dwyer EJC, 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;72:758-66.
59. Stuurman N, de Graaf A, Floore A, et al. A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies. J Cell Sci 1992;101:773-84.
60. Doucas V, Ishov A, Romo A, et at. Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev 1996;10:196-207.
61. Carvalho T, Seeler J-S, Öhman K, et al. Targeting of adenovirus E1A and E4-3 proteins to nuclear matrix-associated PML bodies. J Cell Biol 1995;131:45-56.
62. Hoppe A, Beech SJ, Dimmock J, Leppard KN. Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption. J Virol 2006;80:3042-9.
63. Bischof O, Kirsh O, Pearson M, Itahana K, Pelicci PG, Dejean A. Deconstructing PML-induced premature senescence. EMBO J 2002;21:3358-69.