GW182 is critical for the stability of GW bodies expressed during the cell cycle and cell proliferation

Journal of Cell Science

Volumn 117, Issue 23, 2004, Pages 5567-5578

  Yang, Zheng ^a,e   Jakymiw, Andrew ^a   Wood, Malcolm R ^b   Eystathioy, Theophany ^c   Rubin, Robert L ^d   Fritzler, Marvin J ^c   Chan, Edward K L ^a  

^a UNIVERSITY OF FLORIDA   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

^c UNIVERSITY OF CALGARY   (Canada)

^d UNIVERSITY OF NEW MEXICO SCHOOL OF MEDICINE   (United States)

^e UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

GW bodies; GW repeats; mRNA degradation complex

Indexed keywords

AUTOANTIBODY; CELL PROTEIN; CONCANAVALIN A; GW182 PROTEIN; MESSENGER RNA; UNCLASSIFIED DRUG;

ARTICLE; CELL COMPARTMENTALIZATION; CELL CYCLE G1 PHASE; CELL CYCLE G2 PHASE; CELL CYCLE S PHASE; CELL PROLIFERATION; CELL STIMULATION; CELL STRAIN 3T3; CELL SYNCHRONIZATION; CELL TYPE; CONTROLLED STUDY; CYTOPLASM; GW BODY; HELA CELL; HUMAN; HUMAN CELL; IMMUNOGOLD ELECTRON MICROSCOPY; IN VITRO STUDY; LIPID BILAYER; MAMMAL CELL; MITOSIS; MOLECULAR STABILITY; PRIORITY JOURNAL; PROTEIN EXPRESSION; RNA DEGRADATION; RNA STABILITY; SPLEEN CELL; STAINING; T LYMPHOCYTE;

3T3 CELLS; ANIMALS; AUTOANTIGENS; CELL COMPARTMENTATION; CELL PROLIFERATION; CHROMOSOMAL PROTEINS, NON-HISTONE; CONCANAVALIN A; CULTURE MEDIA, SERUM-FREE; CYTOPLASMIC STRUCTURES; DOWN-REGULATION; FEMALE; G1 PHASE; G2 PHASE; HELA CELLS; HUMANS; IMMUNOHISTOCHEMISTRY; MICE; MICROFILAMENT PROTEINS; MICROSCOPY, ELECTRON, TRANSMISSION; PROLIFERATING CELL NUCLEAR ANTIGEN; RNA STABILITY; RNA, MESSENGER; S PHASE;

MAMMALIA;

EID: 10944256057     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01477     Document Type: Article

References (36)

1. Andrade, L. E. C., Tan, E. M. and Chan, E. K. L. (1993). Immunocytochemical analysis of the coiled body in the cell cycle and during cell proliferation. Proc. Natl. Acad. Sci. USA 90, 1947-1951.
2. Bootsma, D., Budke, L. and Vos, O. (1964). Studies on synchronous division of tissue culture cells initiated by excess thymidine. Exp. Cell Res. 33, 301-309.
3. Bouveret, E., Rigaut, G., Shevchenko, A., Wilm, M. and Séraphin, B. (2000). A Sm-like protein complex that participates in mRNA degradation. EMBO J. 19, 1661-1671.
4. Bravo, R. and Macdonald-Bravo, H. (1987). Existence of two populations of cyclin/proliferating cell nuclear antigen during the cell cycle: association with DNA replication sites. J. Cell Biol. 105, 1549-1554.
5. Casiano, C. A., Landberg, G., Ochs, R. L. and Tan, E. M. (1993). Autoantibodies to a novel cell cycle-regulated protein that accumulates in the nuclear matrix during S phase and is localized in the kinetochores and spindle midzone during mitosis. J. Cell Sci. 106, 1045-1056.
6. Casiano, C. A., Humbel, R. L., Peebles, C. L., Covini, G. and Tan, E. M. (1995). Autoimmunity to the cell cycle-dependent centromere protein p330d/CENP-F in disorders associated with cell proliferation. J. Autoimmun. 8, 575-586.
7. Couttet, P., Fromont-Racine, M., Steel, D., Pictet, R. and Grange, T. (1997). Messenger RNA deadenylylation precedes decapping in mammalian cells. Proc. Natl. Acad. Sci. USA 94, 5628-5633.
8. Dunckley, T. and Parker, R. (1999). The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif. EMBO J. 18, 5411-5422.
9. Dunckley, T. and Parker, R. (2001). Yeast mRNA decapping enzyme. Methods Enzymol. 342, 226-233.
10. Eystathioy, T., Chan, E. K. L., Tenenbaum, S. A., Keene, J. D., Griffith, K. and Fritzler, M. J. (2002a). A phosphorylated cytoplasmic autoantigen, GW182, associates with a unique population of human mRNAs within novel cytoplasmic speckles. Mol. Biol. Cell 13, 1338-1351.
11. Eystathioy, T., Peebles, C. L., Hamel, J. C., Vaughn, J. H. and Chan, E. K. L. (2002b). Autoantibody to hLSm4 and the heptameric LSm complex in anti-Sm sera. Arthritis Rheum. 46, 726-734.
12. Eystathioy, T., Chan, E. K. L., Mahler, M., Luft, L. M., Fritzler, M. L. and Fritzler, M. J. (2003a). A panel of monoclonal antibodies to cytoplasmic GW bodies and the mRNA binding protein GW182. Hybrid. Hybridomics 22, 79-86.
13. Eystathioy, T., Chan, E. K. L., Takeuchi, K., Mahler, M., Luft, L. M., Zochodne, D. W. and Fritzler, M. J. (2003b). Clinical and serological associations of autoantibodies to GW bodies and a novel cytoplasmic autoantigen GW182. J. Mol. Med. 81, 811-818.
14. Eystathioy, T., Jakymiw, A., Chan, E. K. L., Séraphin, B., Cougot, N. and Fritzler, M. J. (2003c). The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies. RNA 9, 1171-1173.
15. Gao, M., Wilusz, C. J., Peitz, S. W. and Wilusz, J. (2001). A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements. EMBO J. 20, 1134-1143.
16. He, W. and Parker, R. (2000). Functions of Lsm proteins in mRNA degradation and splicing. Curr Opin. Cell Biol. 12, 346-350.
17. Ingelfinger, D., Arndt-Jovin, D. J., Luhrmann, R. and Achsel, T. (2002). The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA 8, 1489-1501.
18. Keene, J. D. (2003). Posttranscriptional generation of macromolecular complexes. Mol. Cell 12, 1347-1349.
19. Liao, H., Winkfein, R. J., Mack, G., Rattner, J. B. and Yen, T. J. (1995). CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis. J. Cell Biol. 130, 507-518.
20. Linstedt, A. D. and Hauri, H. P. (1993). Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa. Mol. Biol. Cell 4, 679-693.
21. Mishell, B. B. and Shiigi, S. M. (1980). Methods in Cellular Immunology, pp. 182-185. New York, NY: W. H. Freeman and Company.
22. Monneron, A. and Bernhard, W. (1969). Fine structural organization of the interphase nucleus in some mammalian cells. J. Ultrastruct. Res. 27, 266-288.
23. Oliver, B., Parisi, M. and Clark, D. (2002). Gene expression neighborhoods. J. Biol. 1, 4.
24. Ou, Y., Enarson, P., Rattner, J. B., Barr, S. G. and Fritzler, M. J. (2004). The nuclear pore complex protein Tpr is a common autoantigen in sera that demonstrate nuclear envelope staining by indirect immunofluorescence. Clin. Exp. Immunol. 136, 379-387.
25. Paddison, P. J., Candy, A. A., Bernstein, E., Hannon, G. J. and Conklin, D. S. (2002). Short hairpin RNAs (shRNAs) induce sequence-specific silencing in mammalian cells. Genes Dev. 16 948-958.
26. Raposo, G., Kleijmeer, M. J., Posthuma, G., Slot, J. W. and Geuze, H. J. (1996). Immunogold labeling of ultrathin cryosections: application in immunology. In Weir's Handbook of Experimental Immunology (ed. D. M. Weir), pp. 1-11. New York, NY: Blackwell Publishers.
27. Raska, I., Andrade, L. E. C., Ochs, R., Chan, E. K. L., Chang, C. M., Roos, G. and Tan, E. M. (1991). Immunological and ultrastructural studies of the nuclear coiled body with autoimmune antibodies. Exp. Cell Res. 195, 27-37.
28. Rattner, J. B., Rao, A., Fritzler, M. J., Valencia, D. W. and Yen, T. J. (1993). CENP-F is a ca 400 kDa kinetochore protein that exhibits a cell-cycle dependent localization. Cell Motil. Cytoskeleton 26, 214-226.
29. Reimer, G., Pollard, K. M., Penning, C. A., Ochs, R. L., Lischwe, M. A., Busch, H. and Tan, E. M. (1987). Monoclonal autoantibody from a (New Zealand black × New Zealand white) F1 mouse and some human scleroderma sera target an Mr 34,000 nucleolar protein of the U3 RNP particle. Arthritis Rheum. 30, 793-800.
30. Sheth, U. and Parker, R. (2003). Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300, 805-808.
31. Spellman, P. T. and Rubin, G. M. (2002). Evidence for large domains of similarly expressed genes in the Drosophila genome. J. Biol. 1, 5.
32. Takasaki, Y., Fishwild, D. and Tan, E. M. (1984). Characterization of proliferating cell nuclear antigen recognized by autoantibodies in lupus sera. J. Exp. Med. 159, 981-992.
33. Tharun, S. and Parker, R. (2001). Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Mol. Cell 8, 1075-1083.
34. Tharun, S., He, W., Mayes, A. E., Lennertz, P., Beggs, J. D. and Parker, R. (2000). Yeast Sm-like proteins function in mRNA decapping and decay. Nature 404, 515-518.
35. Van Dijk, E., Cougot, N., Meyer, S., Babajko, S., Wahle, E. and Séraphin, B. (2002). Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 21, 6915-6924.
36. Wickens, M. and Goldstrohm, A. (2003). Molecular biology. A place to die, a place to sleep. Science 300, 753-755.