Review: Properties and assembly mechanisms of ND10, PML2 bodies, or PODs

Journal of Structural Biology

Volumn 129, Issue 2-3, 2000, Pages 278-287

  Maul, Gerd G ^a   Negorev, Dmitri ^a   Bell, Peter ^a   Ishov, Alexander M ^a  

^a WISTAR INSTITUTE   (United States)

Author keywords

Daxx; Knock out cells; Nuclear proteins; Nuclear structure; PML; Protein interaction; Sp100; SUMO 1; Supramolecular regulation

Indexed keywords

PROTEIN ND10; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

BINDING SITE; CELL NUCLEUS MATRIX; CHROMATIN CONDENSATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN LOCALIZATION; REVIEW;

EID: 0033925534     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2000.4239     Document Type: Article

References (55)

1. Ahn J. H., Brignole E. J. III, Hayward G. S. Disruption of PML subnuclear domains by the acidic IE1 protein of human cytomegalovirus is mediated through interaction with PML and may modulate a RING finger-dependent cryptic transactivator function of PML. Mol. Cell. Biol. 18:1998;4899-4913.
2. Alcalay M., Tomassoni L., Colombo E., Stoldt S., Grignani F., Fagioli M., Szekely L., Helin K., Pelicci P. G. The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol. Cell. Biol. 18:1998;1084-1093.
3. 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., 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.
4. Anton L. C., Schubert U., Bacik I., Princiotta M. F., Wearsch P. A., Gibbs J., Day P. M., Realini C., Rechsteiner M. C., Bennink J. R., Yewdell J. W. Intracellular localization of proteasomal degradation of a viral antigen. J. Cell Biol. 146:1999;113-124.
5. Ascoli C. A., Maul G. G. Identification of a novel nuclear domain. J. Cell Biol. 112:1991;785-795.
6. Bernstein R. M. Antinuclear antibodies in primary biliary cirrhosis. Lancet. 1:1984;508.
7. Bernstein R. M., Neuberger J. M., Bunn C. C., Callender M. E., Hughes G. R., Williams R. Diversity of autoantibodies in primary biliary cirrhosis and chronic active hepatitis. Clin. Exp. Immunol. 55:1984;553-560.
8. Bouteille M., Laval M., Dupuy-Coin A. M. Localization of nuclear functions as revealed by ultrastructural autoradiography and cytochemistry. Bush H. The Cell Nucleus. 1974;5-65 Academic Press, New York.
9. Bridger J. M., Herrmann H., Munkel C., Lichter P. Identification of an interchromosomal compartment by polymerization of nuclear-targeted vimentin. J. Cell Sci. 111:1998;1241-1253.
10. Chelbi-Alix M. K., Pelicano L., Quignon F., Koken M. H., Venturini L., Stadler M., Pavlovic J., Degos L., de The H. Induction of the PML protein by interferons in normal and APL cells. Leukemia. 9:1995;2027-2033.
11. 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. 273:1996;951-953.
12. de The G., Riviere M., Bernhard W. Examen au microscope electronique de la tumeur VX2 du lapin domestice derivee du papillome de Shope. Bull. Cancer. 47:1960;570-584.
13. Doucas V., Tini M., Egan D. A., Evans R. M. 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. 96:1999;2627-2632.
14. Duprez E., Saurin A. J., Desterro J. M., Lallemand-Breitenbach V., Howe K., Boddy M. N., Solomon E., de The H., Hay R. T., Freemont P. S. SUMO-1 modification of the acute promyelocytic leukaemia protein PML: Implications for nuclear localisation. J. Cell Sci. 112:1999;381-393.
15. Dyck J. A., Maul G. G., Miller W. H. Jr., Chen J. D., Kakizuka A., Evans R. M. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell. 76:1994;333-343.
16. Epstein A. L. Immunobiochemical characterization with monoclonal antibodies of Epstein-Barr virus-associated early antigens in chemically induced cells. J. Virol. 50:1984;372-379.
17. Everett R. D., Freemont P., Saitoh H., Dasso M., Orr A., Kathoria M., Parkinson J. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72:1998;6581-6591.
18. Everett R. D., Lomonte P., Sternsdorf T., van Driel R., Orr A. Cell cycle regulation of PML modification and ND10 composition. J. Cell Sci. 112:1999;4581-4588.
19. Everett R. D., Maul G. G. HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J. 13:1994;5062-5069.
20. Gong L., Millas S., Maul G. G., Yeh E. T. H. Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J. Biochem. 275:2000;3355-3359.
21. Hollenbach A. D., Sublett J. E., McPherson C. J., Grosveld G. The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx. EMBO J. 18:1999;3702-3711.
22. Ishov A. M., Sotnikov A. G., Negorev D., Vladimirova O. V., Neff N., Kamitani T., Yeh E. T., Strauss J. F. III, 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.
23. Ishov A. M., Stenberg R. M., Maul G. G. Human cytomegalovirus immediate early interaction with host nuclear structures: Definition of an immediate transcript environment. J. Cell Biol. 138:1997;5-16.
24. Kamitani T., Kito K., Nguyen H. P., Wada H., Fukuda-Kamitani T., Yeh E. T. Identification of three major sentrinization sites in PML. J. Biol. Chem. 273:1998;26675-26682.
25. Kelly C., Van Driel R., Wilkinson G. W. Disruption of PML-associated nuclear bodies during human cytomegalovirus infection. J. Gen. Virol. 76:1995;2887-2893.
26. Kiriakidou M., Driscoll D. A., Lopez-Guisa J. M., Strauss J. F. III. Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region. DNA Cell Biol. 16:1997;1289-1298.
27. 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. The t(15;17) translocation alters a nuclear body in a retinoic acid-reversible fashion. EMBO J. 13:1994;1073-1083.
28. Korioth F., Gieffers C., Maul G. G., Frey J. Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment. J. Cell Biol. 130:1995;1-13.
29. LaMorte V. J., Dyck J. A., Ochs R. L., Evans R. M. Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc. Natl. Acad. Sci. USA. 95:1998;4991-4996.
30. Lavau C., Marchio A., Fagioli M., Jansen J., Falini B., Lebon P., Grosveld F., Pandolfi P. P., Pelicci P. G., Dejean A. The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene. 11:1995;871-876.
31. Lehming N., Le Saux A., Schuller J., Ptashne M. Chromatin components as part of a putative transcriptional repressing complex. Proc. Natl. Acad. Sci. USA. 95:1998;7322-7326.
32. Liu Q., Dreyfuss G. A novel nuclear structure containing the survival of motor neurons protein. EMBO J. 15:1996;3555-3565.
33. Matunis M. J., Coutavas E., Blobel G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135:1996;1457-1470.
34. Maul G. G. Nuclear domain 10, the site of DNA virus transcription and replication. BioEssays. 20:1998;660-667.
35. Maul G. G., Guldner H. H., Spivack J. G. Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0). J. Gen. Virol. 74:1993;2679-2690.
36. Maul G. G., Jensen D. E., Ishov A. M., Herlyn M., Rauscher F. J. III. Nuclear redistribution of BRCA1 during viral infection. Cell. Growth Differ. 9:1998;743-755.
37. Maul G. G., Yu E., Ishov A. M., Epstein A. L. Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress. J. Cell Biochem. 59:1995;498-513.
38. Muller S., Matunis M. J., Dejean A. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17:1998;61-70.
39. Plehn-Dujowich D., Ishov B. P., Baumann A. M., Maul G. G. Non-apoptotic chromosome condensation induced by stress: Delineation of interchromosomal spaces. Chromosome. 2000.
40. Pluta A. F., Earnshaw W. C., Goldberg I. G. Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death. J. Cell Sci. 111:1998;2029-2041.
41. Quignon F., De Bels F., Koken M., Feunteun J., Ameisen J. C., de The H. PML induces a novel caspase-independent death process. Nat. Genet. 20:1998;259-265.
42. Schul W., de Jong L., van Driel R. Nuclear neighbours: The spatial and functional organization of genes and nuclear domains. J. Cell Biochem. 70:1998;159-171.
43. Schul W., van Der Kraan I., Matera A. G., 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. 10:1999;3815-3824.
44. Seeler J. S., Dejean A. The PMC nuclear bodies: Actors or extras. Curr. Opin. Genet. Dev. 9:1999;362-367.
45. Seeler J. S., Marchio A., Sitterlin D., Transy C., Dejean A. Interaction of SP100 with HP1 proteins: A link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc. Natl. Acad. Sci. USA. 95:1998;7316-7321.
46. Snyder L. C., Trusko S. P., Freeman N., Eshleman J. R., Fakharzadeh S. S., George D. L. A gene amplified in a transformed mouse cell line undergoes complex transcriptional processing and encodes a nuclear protein. J. Biol. Chem. 263:1988;17150-17158.
47. 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. 274:1999;12555-12566.
48. Sternsdorf T., Jensen K., Will H. Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 139:1997a;1621-1634.
49. Sternsdorf T., Jensen K., Zuchner D., Will H. Cellular localization, expression, and structure of the nuclear dot protein 52. J. Cell Biol. 138:1997b;435-448.
50. 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. 101:1992;773-784.
51. Szostecki C., Guldner H. H., Netter H. J., Will H. Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis. J. Immunol. 145:1990;4338-4347.
52. Terris B., Baldin V., Dubois S., Degott C., Flejou J. F., Henin D., Dejean A. PML nuclear bodies are general targets for inflammation and cell proliferation. Cancer Res. 55:1995;1590-1597.
53. Wang Z. G., Ruggero D., Ronchetti S., Zhong S., Gaboli M., Rivi R., Pandolfi P. P. PML is essential for multiple apoptotic pathways. Nat. Genet. 20:1998;266-272.
54. 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. 76:1994;345-356.
55. Yang X., Khosravi-Far R., Chang H. Y., Baltimore D. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell. 89:1997;1067-1076.