Role of SUMO-1-modified PML in nuclear body formation

Blood

Volumn 95, Issue 9, 2000, Pages 2748-2753

  Zhong, Sue ^b   Müller, Stefan ^b   Ronchetti, Simona ^b   Freemont, Paul S ^b   Dejean, Anne ^b   Pandolfi, Pier Paolo ^a  

^a Department of Obstetrics Gynecology   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR PROTEIN; UBIQUITIN;

ACUTE MYELOBLASTIC LEUKEMIA; ANIMAL CELL; ARTICLE; CELL NUCLEUS INCLUSION BODY; CELLULAR DISTRIBUTION; CONTROLLED STUDY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION;

EID: 0343776952     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v95.9.2748.009k31a_2748_2752     Document Type: Article

References (39)

1. Scheer U, Weisenberger D. The nucleolus. Curr Opin Cell Biol. 1994;6:354-359.
2. Sternsdorf T, Grotzinger T, Jensen K, Will H. Nuclear dots: actors on many stages. Immunobiology. 1997;198:307-331.
3. Bouteille M, Laval M, Dupuy-Coin AM. Localization of nuclear functions as revealed by ultrastructural autoradiography and cytochemistry. In: Busch H, ed. The Cell Nucleus. New York, NY: Academic Press; 1974;5-64.
4. Ascoli CA, Maul GG. Identification of a novel nuclear domain. J Cell Biol. 1991;112:785-795.
5. Dyck J, Maul GG, Miller WH Jr, Chen JD, Kakizuka A, Evans RM. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell. 1994;76:333-343.
6. Koken MHM, Puvion-Dutilleul F, Guillemin MC, et al. The t(15;17) translocation alters a nuclear body in a retinoic acid-reversible fashion. EMBO J. 1994;13:1073-1083.
7. Weis K, Rambaud S, Lavau C, et al. Retinoic acid regulates aberrant nuclear localization of PML-RARα in acute promyelocytic leukemic cells. Cell. 1994;76:345-356.
8. 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.
9. Zhong S, Salomoni P, Ronchetti S, Guo A, Ruggero D, Pandolfi PP. PML and Daxx participate in a novel nuclear pathway for apoptosis. J Exp Med. 2000;191:631-640.
10. Freemont PS, Hanson IM, Trowsdale J. A novel cysteine-rich sequence motif. Cell. 1991;64:483-484.
11. Borden KLB, Freemont PS. The RING finger domain: a recent example of a sequence-structure family. Curr Opin Struct Biol. 1996;6:395-401.
12. Lavau C, Marchio A, Fagioli M, et al. The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene. 1995;11:871-876.
13. Gaboli M, Gandini D, Delva L, Wang ZG, Pandolfi PP. Acute promyelocytic leukemia as a model for cross-talk between interferon and retinoic acid pathways: from molecular biology to clinical applications. Leuk Lymphoma. 1998;30:11-22.
14. Nason-Burchenal K, Gandini D, Botto M, et al. Interferon augments PML and PML/RARα expression in normal meyloid and acute promyelocytic cells and cooperates with all-trans retinoic acid to induce maturation of a retinoid resistant promyelocytic cell line. Blood. 1996;88:3926-3936.
15. Wang ZG, Delva L, Gaboli M, et al. Role of PML in cell growth and the retinoic acid pathway. Science. 1998;279:1547-1551.
16. Wang Z-G, Ruggero D, Ronchetti S, et al. Pml is essential for multiple apoptotic pathways. Nat Genet. 1998;20:266-271.
17. Zhong S, Delva L, Rachez C, et al. A RA-dependent tumor-growth suppressive transcription complex is the target of the PML-RARα and T18 oncoproteins. Nat Genet. 1999;23:287-295.
18. Matunis MJ, Wu J, Blobel G. SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex. J Cell Biol. 1998;140:499-509.
19. Desterro JM, Rodriguez MS, Hay RT. SUMO-1 modification of IκBα inhibits NF-kappaB activation. Mol Cell. 1998;2:233-239.
20. 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.
21. Müller 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.
22. Sternsdorf T, Jensen K, Will H. Evidence for covalent modification ot the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J Cell Biol. 1997;139:1621-1634.
23. Kalantry S, Delva L, Gaboli M, et al. Gene rearrangements in the molecular pathogenesis of acute promyelocytic leukemia. J Cell Physiol. 1997;173:288-296.
24. Perez A, Kastner P, Sethi S, Lutz Y, Reibel C, Chambon P. PML/RAR homodimers: distinct DNA binding properties and heteromeric interactions with RAR. EMBO J. 1993;12:3171-3182.
25. Filvaroff E, Stern DF, Dotto GP. Tyrosine phosphorylation is an early and specific event involved in primary keratinocyte differentiation. Mol Cell Biol. 1990;10:1164-1173.
26. de Thé H, Lavau C, Marchio A, Chomienne C, Degos L, Dejean A. The PML/RARα fusion mRNA generated by the t(15; 17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell. 1991;66:675-684.
27. Kamitani T, Kito K, Nguyen HP, Wada H, Fukuda-Kamitani T, Yeh ET. Identification of three major sentrinization sites in PML. J Biol Chem. 1998; 273:26,675-25,682.
28. Szostecki C, Guldner HH, Netter HJ, Will H. Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis. J Immunol. 1990;145:4338-4347.
29. Guldner HH, Szostecki C, Grotzinger T, Will H. IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis. J Immunol. 1992; 149:4067-4073.
30. Yang X, Khosravi-Far R, Chang HY, Baltimore D. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell. 1997;89:1067-1076.
31. Chakravati D, LaMorte VJ, Nelson MC, et al. Role of CBP/P300 in nuclear receptor signalling. Nature. 1996;383:99-103.
32. Bannister AJ, Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature. 1996;384: 641-643.
33. 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 U S A. 1998;95:4991-4996
34. Gongora C, David G, Pintard L, et al. Molecular cloning of a new interferon-induced PML nuclear body-associated protein. J Biol Chem. 1997;272: 19,457-19,463.
35. Maul GG. Nuclear domain 10, the site of DNA virus transcription and replication. Bioessays. 1998;20:660-667.
36. Zhong S, Hu P, Ye TZ, Stan R, Ellis NA, Pandolfi PP. A role for PML and nuclear body in genomic stability. Oncogene. 1999;18:7941-7947.
37. 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: 221-233.
38. Sternsdorf T, Jensen K, Reich B, Will H. The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J Biol Chem. 1999;274:12,555-12,566.
39. Michaelson JS, Bader D, Kuo F, Kozak C, Leder P. Loss of Daxx, a promiscuously interacting protein, results in extensive apoptosis in early mouse development. Genes Dev. 1999;13:1918-1923.