Viral disruption of promyelocytic leukemia (PML) nuclear bodies by hijacking host PML regulators

Virulence

Volumn 2, Issue 1, 2011, Pages 58-62

  Frappier, Lori ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

Casein kinase II; CK2; EBNA1; Epstein barr virus; HAUSP; PML; USP7

Indexed keywords

CASEIN KINASE II; PROMYELOCYTIC LEUKEMIA PROTEIN;

APOPTOSIS; ARTICLE; CELL NUCLEUS INCLUSION BODY; CELL PROLIFERATION; CELL SURVIVAL; DNA REPAIR; EPSTEIN BARR VIRUS; MALIGNANT TRANSFORMATION; PROMYELOCYTIC LEUKEMIA; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; UBIQUITINATION; VIRUS REPLICATION;

HUMAN HERPESVIRUS 4;

EID: 79951477190     PISSN: 21505594     EISSN: 21505608     Source Type: Journal    
DOI: 10.4161/viru.2.1.14610     Document Type: Article

References (56)

1. Salomoni P, Ferguson BJ, Wyllie AH, Rich T. New insights into the role of PML in tumour suppression. Cell Res 2008; 18:622-640.
2. Takahashi Y, Lallemand-Breitenbach V, Zhu J, de The H. PML nuclear bodies and apoptosis. Oncogene 2004; 23:2819-2824.
3. Lallemand-Breitenbach V, de The H. PML nuclear bodies. Cold Spring Harb Perspect Biol 2010; 2:000661.
4. Bernardi R, Pandolfi PP. Structure, dynamics andm functions of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Biol 2007; 8:1006-1016.
5. Gurrieri C, Capodieci P, Bernardi R, Scaglioni PP, Nafa K, Rush LJ, et al. Loss of the tumor suppressor PML in human cancers of multiple histologic origins. J Natl Cancer Inst 2004; 96:269-279.
6. Stadler M, Chelbi-Alix MK, Koken MH, Venturini L, Lee C, Saib A, et al. Transcriptional induction of the PML growth suppressor gene by interferons is mediated through an ISRE and a GAS element. Oncogene 1995; 11:2565-2573.
7. 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.
8. Muratani M, Gerlich D, Janicki SM, Gebhard M, Eils R, Spector DL. Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus. Nat Cell Biol 2002; 4:106-110.
9. Everett RD, Murray J. ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection. J Virol 2005; 79:5078-5089.
10. Brand P, Lenser T, Hemmerich P. Assembly dynamics of PML nuclear bodies in living cells. PMC Biophys 2010; 3:3.
11. Scaglioni PP, Yung TM, Cai LF, Erdjument-Bromage H, Kaufman AJ, Singh B, et al. A CK2-dependent mechanism for degradation of the PML tumor suppressor. Cell 2006; 126:269-283.
12. Scaglioni PP, Yung TM, Choi SC, Baldini C, Konstantinidou G, Pandolfi PP. CK2 mediates phosphorylation and ubiquitin-mediated degradation of the PML tumor suppressor. Mol Cell Biochem 2008; 316:149-154.
13. Everett RD. DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 2001; 20:7266-7273.
14. Everett RD, Chelbi-Alix MK. PML and PML nuclear bodies: implications in antiviral defence. Biochimie 2007; 89:819-830.
15. Ullman AJ, Hearing P. Cellular proteins PML and Daxx mediate an innate antiviral defense antagonized by the adenovirus E4 ORF3 protein. J Virol 2008; 82:7325-7335.
16. Yondola MA, Hearing P. The adenovirus E4 ORF3 protein binds and reorganizes the TRIM family member transcriptional intermediary factor 1alpha. J Virol 2007; 81:4264-4271.
17. Adamson AL, Kenney S. Epstein-Barr virus immediate- early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies. J Virol 2001; 75:2388-2399.
18. Boutell C, Sadis S, Everett RD. Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro. J Virol 2002; 76:841-850.
19. Everett RD, Freemont P, Saitoh H, Dasso M, Orr A, Kathoria M, et al. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J Virol 1998; 72:6581-6591.
20. Everett RD, Rechter S, Papior P, Tavalai N, Stamminger T, Orr A. PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J Virol 2006; 80:7995-8005.
21. Everett R, Meredith M, Orr A, Cross A, Kathoria M, Parkinson J. A novel ubiquitin-specific protease is dyamically associted with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J 1997; 16:1519-1530.
22. Boutell C, Canning M, Orr A, Everett RD. Reciprocal activities between herpes simplex virus type 1 regulatory protein ICP0, a ubiquitin E3 ligase and ubiquitin-specific protease USP7. J Virol 2005; 79:12342-12354.
23. Faustrup H, Bekker-Jensen S, Bartek J, Lukas J, Mailand N. USP7 counteracts SCFbetaTrCP- but not APCCdh1-mediated proteolysis of Claspin. J Cell Biol 2009; 184:13-19.
24. van der Horst A, de Vries-Smits AM, Brenkman AB, van Triest MH, van den Broek N, Colland F, et al. FOXO4 transcriptional activity is regulated by monoubiquitination and USP7/HAUSP. Nat Cell Biol 2006; 8:1064-1073.
25. Li M, Chen D, Shiloh A, Luo J, Nikolaev AY, Qin J, et al. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 2002; 416:648-653.
26. Li M, Brooks CL, Kon N, Gu W. A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell 2004; 13:879-886.
27. Sheng Y, Saridakis V, Sarkari F, Duan S, Wu T, Arrowsmith CH, et al. Molecular recognition of p53 and MDM2 by USP7/HAUSP. Nat Struct Mol Biol 2006; 13:285-291.
28. van der Knaap JA, Kumar BR, Moshkin YM, Langenberg K, Krijgsveld J, Heck AJ, et al. GMP synthetase stimulates histone H2B deubiquitylation by the epigenetic silencer USP7. Mol Cell 2005; 17:695-707.
29. van der Knaap JA, Kozhevnikova E, Langenberg K, Moshkin YM, Verrijzer CP. Biosynthetic enzyme GMP synthetase cooperates with ubiquitin-specific protease 7 in transcriptional regulation of ecdysteroid target genes. Mol Cell Biol 2010; 30:736-744.
30. Sarkari F, Sanchez-Alcaraz T, Wang S, Holowaty MN, Sheng Y, Frappier L. EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication. PLoS Pathog 2009; 5:1000624.
31. Klein G, Klein E, Kashuba E. Interaction of Epstein- Barr virus (EBV) with human B-lymphocytes. Biochem Biophys Res Commun 2010; 396:67-73.
32. Frappier L. EBNA1 in viral DNA replication and persistence. In: Robertson ES, ed. Epstein-Barr Virus: Latency and Transformation. Caister Academic Press, Norwich 2010; 37-59.
33. Kennedy G, Komano J, Sugden B. Epstein-Barr virus provide a survival factor to Burkitt's lymphomas. Proc Natl Acad Sci USA 2003; 100:14269-14274.
34. Saridakis V, Sheng Y, Sarkari F, Holowaty MN, Shire K, Nguyen T, et al. Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization. Mol Cell 2005; 18:25-36.
35. Yin Q, Flemington EK. siRNAs against the Epstein Barr virus latency replication factor, EBNA1, inhibit its function and growth of EBV-dependent tumor cells. Virology 2006; 346:385-393.
36. Hong M, Murai Y, Kutsuna T, Takahashi H, Nomoto K, Cheng CM, et al. Suppression of Epstein-Barr nuclear antigen 1 (EBNA1) by RNA interference inhibits proliferation of EBV-positive Burkitt's lymphoma cells. J Cancer Res Clin Oncol 2006; 132:1-8.
37. Kaul R, Murakami M, Choudhuri T, Robertson ES. Epstein-Barr virus latent nuclear antigens can induce metastasis in a nude mouse model. J Virol 2007; 81:10352-103561.
38. Raab-Traub N. Epstein-Barr virus in the pathogenesis of NPC. Semin Cancer Biol 2002; 12:431-441.
39. Sivachandran N, Sarkari F, Frappier L. Epstein-Barr nuclear antigen 1 contributes to nasopharyngeal carcinoma through disruption of PML nuclear bodies. PLoS Pathog 2008; 4:1000170.
40. Wang ZG, Ruggero D, Ronchetti S, Zhong S, Gaboli M, Rivi R, et al. PML is essential for multiple apoptotic pathways. Nat Genet 1998; 20:266-272.
41. Pearson M, Carbone R, Sebastiani C, Cioce M, Fagioli M, Saito S, et al. PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 2000; 406:207-210.
42. Guo A, Salomoni P, Luo J, Shih A, Zhong S, Gu W, et al. The function of PML in p53-dependent apoptosis. Nat Cell Biol 2000; 2:730-736.
43. Boe SO, Haave M, Jul-Larsen A, Grudic A, Bjerkvig R, Lonning PE. Promyelocytic leukemia nuclear bodies are predetermined processing sites for damaged DNA. J Cell Sci 2006; 119:3284-3295.
44. de Stanchina E, Querido E, Narita M, Davuluri RV, Pandolfi PP, Ferbeyre G, et al. PML is a direct p53 target that modulates p53 effector functions. Mol Cell 2004; 13:523-535.
45. Li X, Wang E, Zhao YD, Ren JQ, Jin P, Yao KT, et al. Chromosomal imbalances in nasopharyngeal carcinoma: a meta-analysis of comparative genomic hybridization results. J Transl Med 2006; 4:4.
46. Shao JY, Huang XM, Yu XJ, Huang LX, Wu QL, Xia JC, et al. Loss of heterozygosity and its correlation with clinical outcome and Epstein-Barr virus infection in nasopharyngeal carcinoma. Anticancer Res 2001; 21:3021-3029.
47. Sivachandran N, Cao JY, Frappier L. Epstein-Barr virus nuclear antigen 1 Hijacks the host kinase CK2 to disrupt PML nuclear bodies. J Virol 2010; 84:11113-11123.
48. Sarkari F, Wang X, Nguyen T, Frappier L. The herpesvirus associated ubiquitin specific protease, USP7, is a negative regulator of PML proteins and PML nuclear bodies. PLOS ONE 2011; In press.
49. Shire K, Ceccarelli DFJ, Avolio-Hunter TM, Frappier L. EBP2, a human protein that interacts with sequences of the Epstein-Barr nuclear antigen 1 important for plasmid maintenance. J Virol 1999; 73:2587-2595.
50. Kapoor P, Lavoie BD, Frappier L. EBP2 plays a key role in Epstein-Barr virus mitotic segregation and is regulated by aurora family kinases. Mol Cell Biol 2005; 25:4934-4945.
51. Wang S, Frappier L. Nucleosome assembly proteins bind to Epstein-Barr nuclear antigen 1 (EBNA1) and affect its functions in DNA replication and transcriptional activation. J Virol 2009; 83:11704-11714.
52. Holowaty MN, Zeghouf M, Wu H, Tellam J, Athanasopoulos V, Greenblatt J, et al. Protein profiling with Epstein-Barr nuclear antigen 1 reveals an interaction with the herpesvirus- associated ubiquitinspecific protease HAUSP/USP7. J Biol Chem 2003; 278:29987-29994.
53. Wang Y, Finan JE, Middeldorp JM, Hayward SD. P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus. Virology 1997; 236:18-29.
54. Lin A, Wang S, Nguyen T, Shire K, Frappier L. The EBNA1 protein of Epstein-Barr virus functionally interacts with Brd4. J Virol 2008; 82:12009-12019.
55. Murakami M, Lan K, Subramanian C, Robertson ES. Epstein-Barr virus nuclear antigen 1 interacts with Nm23-H1 in lymphoblastoid cell lines and inhibits its ability to suppress cell migration. J Virol 2005; 79:1559-1568.
56. Deng Z, Atanasiu C, Zhao K, Marmorstein R, Sbodio JI, Chi NW, et al. Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1. J Virol 2005; 79:4640-4650.