Biology:Nuclear bodies

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Short description: Structures found in the cell nuclei
Nuclear bodies in human embryonic lung cells

Nuclear bodies (also known as nuclear domains, or nuclear dots) are membraneless structures found in the cell nuclei of eukaryotic cells.[1] Nuclear bodies include Cajal bodies, the nucleolus, and promyelocytic leukemia protein (PML) nuclear bodies (also called PML oncogenic dots).[2] Nuclear bodies also include ND10s. ND stands for nuclear domain, and 10 refers to the number of dots seen.[3]

Nuclear bodies were first seen as prominent interchromatin structures in the nuclei of malignant or hyperstimulated animal cells[4][5] identified using anti-sp100 autoantibodies from primary biliary cirrhosis and subsequently the promyelocytic leukemia (PML) factor, but appear also to be elevated in many autoimmune and cancerous diseases.[6] Nuclear dots are metabolically stable and resistant to nuclease digestion and salt extraction.[7]

A nuclear body subtype is a clastosome suggested to be a site of protein degradation.[8]

Structure

Diagram of the formation of nuclear bodies.

Simple nuclear bodies (types I and II) and the shells of complex nuclear bodies (types III, IVa and V) consist of a non-chromatinic fibrillar material which is most likely proteinaceous.[9] That nuclear bodies co-isolated with the nuclear matrix, and were linked to the fibrogranular nuclear matrix component by projections from the surface of the nuclear bodies.[9] The primary components of the nuclear dots are the proteins sp100 nuclear antigen, LYSP100(a homolog of sp100),[10] ISG20,[11] PML antigen, NDP55 and 53kDa protein associated with the nuclear matrix.[12] Other proteins, such as PIC1/SUMO-1, which are associated with nuclear pore complex also associate with nuclear dots.[13] The proteins can reorganize in the nucleus, by increasing number of dispersion in response to different stress (stimulation or heat shock, respectively).[14]

Function

One of the nuclear body proteins appears to be involved in transcriptional active regions.[15] Expression of PML antigen and sp100 is responsive to interferons. Sp100 seems to have transcriptional transactivating properties. PML protein was reported to suppress growth and transformation,[5] and specifically inhibits the infection of vesicular stomatitis virus (VSV) (a rhabdovirus) and influenza A virus,[16] but not other types of viruses. The SUMO-1 ubiquitin like protein is responsible for modifying PML protein such that it is targeted to dots.[17] whereas overexpression of PML results in programmed cell death.[18]

One hypothesized function of the dots is as a 'nuclear dump' or 'storage depot'. [19] The nuclear bodies may not all perform the same function. Sp140 associates with certain bodies and appears to be involved in transcriptional activation.[20]

ND10 nuclear bodies have been shown to play a major role in chromatin regulation.[21]

Pathology

Immunofluorescence staining pattern of sp100 antibodies. Nuclear dots can be seen in the nucleus of the cells. Produced using serum from a patient with primary biliary cirrhosis on HEp-20-10 cells with a FITC conjugate.

These, or similar, bodies have been found increased in the presence of lymphoid cancers[22][23] and SLE (lupus).[24] They are also observed at higher frequencies in subacute sclerosing panencephalitis; in this instance, antibodies to measles show expression in and localization to the nuclear bodies.[25]

  • In promyelocytic leukemia (PML), the oncogenic PML-retinoic acid receptor alpha (RARalpha) chimera disrupts the normal concentration of PML in nuclear bodies. Administration of arsenic trioxide (As2O3) plus all-trans retinoic acid (Tretinoin) causes remission of this leukemia by triggering the bodies' reorganization. As2O3 destroys the chimera, allowing new SUMO-1 ubiquitinated PML to relocalize to nuclear bodies.[17] Retinoic acid induces a caspase-3 mediated degradation of the same chimera.[26]
  • In HHV, ICP0 disrupts nuclear dots in the early stage of infection.[27]

References

  1. ↑ "Sequence-encoded material properties dictate the structure and function of nuclear bodies". Current Opinion in Cell Biology 46: 62–71. June 2017. doi:10.1016/j.ceb.2017.03.003. PMID 28343140. 
  2. ↑ "Nuclear bodies and compartments: functional roles and cellular signalling in health and disease". Cellular Signalling 16 (10): 1085–104. October 2004. doi:10.1016/j.cellsig.2004.03.020. PMID 15240004. 
  3. ↑ "Nuclear domain 10 of the viral aspect". World Journal of Virology 2 (3): 110–22. August 2013. doi:10.5501/wjv.v2.i3.110. PMID 24255882. 
  4. ↑ "Nuclear bodies (NBs): a newly "rediscovered" organelle". Experimental Cell Research 202 (2): 211–23. October 1992. doi:10.1016/0014-4827(92)90068-J. PMID 1397076. 
  5. ↑ 5.0 5.1 "Nuclear dots: actors on many stages". Immunobiology 198 (1–3): 307–31. December 1997. doi:10.1016/s0171-2985(97)80051-4. PMID 9442402. 
  6. ↑ "Multiple nuclear dots antinuclear antibodies are not specific for primary biliary cirrhosis". Hepatology 16 (1): 127–31. July 1992. doi:10.1002/hep.1840160121. PMID 1319948. 
  7. ↑ "Identification of a novel nuclear domain". The Journal of Cell Biology 112 (5): 785–95. March 1991. doi:10.1083/jcb.112.5.785. PMID 1999457. 
  8. ↑ "Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes, ubiquitin, and protein substrates of proteasome". Molecular Biology of the Cell 13 (8): 2771–82. August 2002. doi:10.1091/mbc.e02-03-0122. PMID 12181345. 
  9. ↑ 9.0 9.1 "Nuclear bodies in mouse splenic lymphocytes: II - Cytochemistry and autoradiography during stimulation by concanavalin A". Biology of the Cell 49 (1): 35–43. 1983. doi:10.1111/j.1768-322x.1984.tb00220.x. PMID 6199062. 
  10. ↑ "LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies". Blood 88 (4): 1423–6. August 1996. doi:10.1182/blood.V88.4.1423.bloodjournal8841423. PMID 8695863. 
  11. ↑ "Molecular cloning of a new interferon-induced PML nuclear body-associated protein". The Journal of Biological Chemistry 272 (31): 19457–63. August 1997. doi:10.1074/jbc.272.31.19457. PMID 9235947. 
  12. ↑ "A human autoantibody recognizing nuclear matrix-associated nuclear protein localized in dot structures". Biology of the Cell 85 (1): 77–86. 1995. doi:10.1016/0248-4900(96)89129-5. PMID 8882521. 
  13. ↑ "Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1". The Journal of Cell Biology 139 (7): 1621–34. December 1997. doi:10.1083/jcb.139.7.1621. PMID 9412458. 
  14. ↑ "Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress". Journal of Cellular Biochemistry 59 (4): 498–513. December 1995. doi:10.1002/jcb.240590410. PMID 8749719. 
  15. ↑ "Nuclear dot antigens may specify transcriptional domains in the nucleus". Molecular and Cellular Biology 13 (10): 6170–9. October 1993. doi:10.1128/MCB.13.10.6170. PMID 8413218. 
  16. ↑ "Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein". Journal of Virology 72 (2): 1043–51. February 1998. doi:10.1128/JVI.72.2.1043-1051.1998. PMID 9444998. 
  17. ↑ 17.0 17.1 "Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus". The EMBO Journal 17 (1): 61–70. January 1998. doi:10.1093/emboj/17.1.61. PMID 9427741. 
  18. ↑ "PML induces a novel caspase-independent death process". Nature Genetics 20 (3): 259–65. November 1998. doi:10.1038/3068. PMID 9806544. 
  19. ↑ "Nuclear domain 10, the site of DNA virus transcription and replication". BioEssays 20 (8): 660–7. August 1998. doi:10.1002/(SICI)1521-1878(199808)20:8<660::AID-BIES9>3.0.CO;2-M. PMID 9780840. 
  20. ↑ "Structural and functional heterogeneity of nuclear bodies". Molecular and Cellular Biology 19 (6): 4423–30. June 1999. doi:10.1128/MCB.19.6.4423. PMID 10330182. 
  21. ↑ "Role of ND10 nuclear bodies in the chromatin repression of HSV-1". Virology Journal 13: 62. April 2016. doi:10.1186/s12985-016-0516-4. PMID 27048561. 
  22. ↑ "Nuclear bodies in Hodgkin's disease". Pathologia Europaea 9 (4): 297–301. 1974. PMID 4457783. 
  23. ↑ "Nuclear Characteristics of Malignant Lymphoma in the Brain". Malignant Lymphomas of the Nervous System. Suppl 6. 1975. 167–71. doi:10.1007/978-3-662-08456-4_28. ISBN 978-3-540-07208-9. 
  24. ↑ "Systemic lupus erythematosus". Archives of Pathology 99 (3): 152–7. March 1975. PMID 164172. 
  25. ↑ "Immunoperoxidase staining of simple nuclear bodies in sclerosing panencephalitis (SSPE) by antiserum to Measles nucleocapsids". Acta Neuropathologica 36 (3): 259–67. November 1976. doi:10.1007/BF00685370. PMID 795259. 
  26. ↑ "Caspases mediate retinoic acid-induced degradation of the acute promyelocytic leukemia PML/RARalpha fusion protein". Blood 92 (7): 2244–51. October 1998. PMID 9746761. 
  27. ↑ Dermody, Terence S., ed (May 2019). "Early Steps in Herpes Simplex Virus Infection Blocked by a Proteasome Inhibitor". mBio 10 (3): e00732–19, /mbio/10/3/mBio.00732–19.atom. doi:10.1128/mBio.00732-19. PMID 31088925. 



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