Cell cycle regulation of PML modification and ND10 composition

Journal of Cell Science

Volumn 112, Issue 24, 1999, Pages 4581-4588

  Everett, Roger D ^a   Lomonte, Patrick ^a   Sternsdorf, Thomas ^b   Van Driel, Roel ^c   Orr, Anne ^a  

^a INSTITUTE OF VIROLOGY   (United Kingdom)

^b LEIBNIZ INSTITUTE FOR EXPERIMENTAL VIROLOGY   (Germany)

^c UNIVERSITY OF AMSTERDAM   (Netherlands)

Author keywords

Cell cycle; ND10; PML

Indexed keywords

CELL PROTEIN; ENZYME INHIBITOR; PHOSPHATASE;

ADENOVIRUS; ARTICLE; CELL CYCLE; CELL NUCLEUS INCLUSION BODY; CONJUGATION; CONTROLLED STUDY; ELECTROPHORETIC MOBILITY; HERPES SIMPLEX VIRUS; HUMAN; HUMAN CELL; INTERPHASE; MITOSIS; PRIORITY JOURNAL; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE;

CELL CYCLE; CELL DIVISION; CELL LINE; CELL NUCLEUS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; HEAT-SHOCK RESPONSE; HUMANS; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN ISOFORMS; SUMO-1 PROTEIN; UBIQUITINS;

EID: 0033380850     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (27)

1. Alcalay, M., Tomassoni, L., Colombo, E., Stoldt, S., Grignani, F., Fagioli, M., Szekely, L., Helin, K. and Pelicci, P. G. (1998). The promyelocytic leukaemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol. Cell. Biol. 18, 1084-1093.
2. Boddy, M. N., Howe, K., Etkin, L. D., Solomon, E. and Freemont, P. S. (1996). PIC1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 13, 971-982.
3. Carvalho, T., Seeler, J. S., Ohman, K., Jordan, P., Pettersson, U., Akusjarvi, G., Carmo-Fonseca, M. and Dejean, A. (1995). Targeting of adenovirus E1a and E4-orf3 proteins to nuclear matrix associated PML bodies. J. Cell Biol. 131, 45-56.
4. Doucas, V., Ishov, A. M., Remo, A., Juguilon, H., Weitzman, M. D., Evans, R. M. and Maul, G. G. (1996). Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev. 10, 196-207.
5. Duprez, E., Saurin, A. J., Desterro, J. M., Lallemand-Breilenbach, V., Howe, K., Boddy, M. N., Soloman, E., de The, H., Hay, R. T. and Freemont, P. S. (1999). SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear organisation. J. Cell Sci. 112, 381-393.
6. Everett, R. D., Freemont, P. S., Saitoh, H., Dasso, M., Orr, A., Kathoria, M. and Parkinson, J. (1998). The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110 and proteasome-dependent loss of several PML isoforms. J. Virol. 72, 6581-6591.
7. Everett, R. D., Earnshaw, W. C., Findlay, J. and Lomonte, P. (1999). Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. EMBO J. 18, 1526-1538.
8. Grötzinger, T., Sternsdorf, T., Jensen, K. and Will, H. (1996). Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML). Eur. J. Biochem. 238, 554-560.
9. Kamitani, T., Nguyen, H. P., Kito, K., Fukuda-Kamitani, T. and Yeh, E. T. H. (1998a). Covalent modification of PML by the Sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273, 3117-3120.
10. Kamitani, T., Kito, K., Nguyen, H. P., Wada, H., Fukuda-Kamitani, T. and Yeh, E. T. H. (1998b). Identification of three major sentrinization sites in PML. J. Biol. Chem. 273, 26675-26682.
11. Lehming, N., Le Saux, A., Schuller, J. and Ptashne, M. (1998). Chromatin components as part of a putative transcriptional repressing complex. Proc. Nat. Acad. Sci. USA 95, 7322-7326.
12. Leppard, K. N. and Everett, R. D. (1999). The adenovirus type 5 E1b 55K and E4 Orf3 proteins associate in infected cells and affect ND10 components. J. Gen. Virol. 80, 997-1008.
13. Li, S.-J. and Hochstrasser, M. (1999). A new protease required for cell cycle progression in yeast. Nature 398, 246-251.
14. Maul, G. G., Yu, E., Ishov, A. and Epstein, A. L. (1995). 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, 498-513.
15. Mu, Z.-M., Chin, K.-V., Liu, J.-H., Lozano, G. and Chang, K-S. (1994). PML, a growth suppressor disrupted in promyelocytic leukaemia. Mol. Cell. Biol. 14, 6858-6867.
16. Muda, M., Boschert, U., Smith, A., Antonsson, B., Gillieron, C., Chabert, C., Camps, M., Martinou, I., Ashworth, A. and Arkinstall, S. (1997). Molecular cloning and functional characterisation of a novel mitogen-activated protein kinase phosphatase, MKP-4. J. Biol Chem. 272, 5141-5151.
17. Muller, S., Matunis, M. J. and Dejean, A. (1998). Conjugation of the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17, 61-70.
18. Quignon, F., DeBels, F., Koken, M., Feunteun, J., Ameisen, J. C. and de The, H. (1998). PML induces a novel caspase-independent death process. Nature Genet. 20, 259-265.
19. Saitoh, H., Pu, R. T. and Dasso, M. (1997). SUMO-1: wrestling wirth a new ubiquitin-related modifier. Trends Biochem. Sci. 22, 374-376.
20. Schwarz, S. E., Matuschewski, K., Liakopoulos, D., Scheffner, M. and Jensch, S. (1998). The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the Ubc9 E2 enzyme. Proc. Nat. Acad. Sci. USA 95, 560-564.
21. Seeler, J. S., Marchio, A., Sitterlin, D., Transby, C. and Dejean, A. (1998). Interaction of Sp100 with HP1 proteins: A link between the promyelocytic leukaemia-associated nuclear bodies and the chromatin compartment. Proc. Nat. Acad. Sci. USA 95, 7316-7321.
22. Sternsdorf, T., Guldner, H. H., Szostecki, C., Grötzinger, T. and Will, H. (1995). Two nuclear-dot associated proteins. PML and Sp100, are often coautoimmunogenic in patients with primary biliary cirrhosis. Scand. J. Immunol. 42, 257-268.
23. Sternsdorf, T., Grötzinger, T., Jensen, K. and Will, H. (1997a). Nuclear dots: Actors on many stages. Immunobiology 198, 307-331.
24. Sternsdorf, T., Jensen, K. and Will, H. (1997b). Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 139, 1621-1634.
25. Stuurman, N., de Graaf, A., Floore, A., Josso, A., Humbel, B., de Jong, L. and van Driel, R. (1992). A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies. J. Cell Sci. 101, 773-784.
26. Vallian, S., Chin, K. and Chang, K. (1998). The promyelocytic leukaemia protein interacts with Sp1 and inhibits its transactivation of the epidermal growth factor receptor promoter. Mol. Cell. Biol. 18, 7147-7156.
27. Wang, Z. G., Delva, L., Gaboli, M., Riva, R., Giorgio, M., Cordon-Cardo, C., Grosveld, F. and Pandolfi, P. P. (1998). Role of PML in cell growth and the retinoic acid pathway. Science 279, 1547-1551.