Two-step colocalization of MORC3 with PML nuclear bodies

Journal of Cell Science

Volumn 123, Issue 12, 2010, Pages 2014-2024

  Mimura, Yasuhiro ^a,b   Takahashi, Keiko ^a,c   Kawata, Kiyo ^a   Akazawa, Takashi ^a   Inoue, Norimitsu ^a  

^a OSAKA MEDICAL CENTER FOR CANCER AND CARDIOVASCULAR DISEASES   (Japan)

^b NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

CW domain; GHL ATPase; MORC3; Promyelocytic leukemia; SUMO; SUMO interacting motif

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; PROTEIN MORC3; PROTEIN P53; SUMO 1 PROTEIN; SUMO PROTEIN; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN;

ANIMAL CELL; ARTICLE; CELL AGING; CELL NUCLEUS; CELL NUCLEUS INCLUSION BODY; CELL NUCLEUS MATRIX; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DIFFUSION; HEMATOPOIETIC CELL; HUMAN; HUMAN CELL; HYDROLYSIS; MOUSE; NONHUMAN; NUCLEOSOME; PRIORITY JOURNAL; PROMYELOCYTIC LEUKEMIA; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN LOCALIZATION; PROTEIN MOTIF; SUMOYLATION;

ADENOSINE TRIPHOSPHATASES; ANIMALS; DNA-BINDING PROTEINS; HELA CELLS; HUMANS; INTRANUCLEAR INCLUSION BODIES; LEUKEMIA, PROMYELOCYTIC, ACUTE; MICE; NUCLEAR PROTEINS; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; SUMO-1 PROTEIN; TRANSCRIPTION FACTORS; TUMOR SUPPRESSOR PROTEINS;

MAMMALIA;

EID: 77953586773     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.063586     Document Type: Article

References (37)

1. Baird, C. L., Harkins, T. T., Morris, S. K. and Lindsley, J. E. (1999). Topoisomerase II drives DNA transport by hydrolyzing one ATP. Proc. Natl. Acad. Sci. USA 96, 13685-13690.
2. Ban, C. and Yang, W. (1998). Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis. Cell 95, 541-552. (Pubitemid 28533310)
3. Ban, C., Junop, M. and Yang, W. (1999). Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair. Cell 97, 85-97. (Pubitemid 29165892)
4. Bernardi, R. and Pandolfi, P. P. (2007). Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev. Mol. Cell Biol. 8, 1006-1016.
5. de The, H., Lavau, C., Marchio, A., Chomienne, C., Degos, L. and Dejean, A. (1991). The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66, 675-684. (Pubitemid 121001703)
6. Dutta, R. and Inouye, M. (2000). GHKL, an emergent ATPase/kinase superfamily. Trends Biochem. Sci. 25, 24-28.
7. Geiss-Friedlander, R. and Melchior, F. (2007). Concepts in sumoylation: a decade on. Nat. Rev. Mol. Cell Biol. 8, 947-956.
8. Handwerger, K. E. and Gall, J. G. (2006). Subnuclear organelles: new insights into form and function. Trends Cell. Biol. 16, 19-26.
9. Inoue, N., Hess, K. D., Moreadith, R. W., Richardson, L. L., Handel, M. A., Watson, M. L. and Zinn, A. R. (1999). New gene family defined by MORC, a nuclear protein required for mouse spermatogenesis. Hum. Mol. Genet. 8, 1201-1207.
10. Iyer, L. M., Anantharaman, V., Wolf, M. Y. and Aravind, L. (2008). Comparative genomics of transcription factors and chromatin proteins in parasitic protists and other eukaryotes. Int. J. Parasitol. 38, 1-31.
11. Kakizuka, A., Miller, W. H., Jr, Umesono, K., Warrell, R. P., Jr, Frankel, S. R., Murty, V. V., Dmitrovsky, E. and Evans, R. M. (1991). Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell 66, 663-674.
12. Kamitani, T., Kito, K., Nguyen, H. P., Wada, H., Fukuda-Kamitani, T. and Yeh, E. T. (1998). Identification of three major sentrinization sites in PML. J. Biol. Chem. 273, 26675-26682.
13. Kimura, Y., Sakai, F., Nakano, O., Kisaki, O., Sugimoto, H., Sawamura, T., Sadano, H. and Osumi, T. (2002). The newly identified human nuclear protein NXP-2 possesses three distinct domains, the nuclear matrix-binding, RNA-binding, and coiled-coil domains. J. Biol. Chem. 277, 20611-20617.
14. Kimura, H., Takizawa, N., Allemand, E., Hori, T., Iborra, F. J., Nozaki, N., Muraki, M., Hagiwara, M., Krainer, A. R., Fukagawa, T. et al. (2006). A novel histone exchange factor, protein phosphatase 2Cgamma, mediates the exchange and dephosphorylation of H2A-H2B. J. Cell Biol. 175, 389-400.
15. Lamond, A. I. and Earnshaw, W. C. (1998). Structure and function in the nucleus. Science 280, 547-553.
16. Lin, D. Y., Huang, Y. S., Jeng, J. C., Kuo, H. Y., Chang, C. C., Chao, T. T., Ho, C. C., Chen, Y. C., Lin, T. P., Fang, H. I. et al. (2006). Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol. Cell 24, 341-354.
17. Minty, A., Dumont, X., Kaghad, M. and Caput, D. (2000). Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J. Biol. Chem. 275, 36316-36323.
18. Morita, S., Kojima, T. and Kitamura, T. (2000). Plat-E: an efficient and stable system for transient packaging of retroviruses. Gene Ther. 7, 1063-1066. (Pubitemid 30398356)
19. Nguyen, L. A., Pandolfi, P. P., Aikawa, Y., Tagata, Y., Ohki, M. and Kitabayashi, I. (2005). Physical and functional link of the leukemia-associated factors AML1 and PML. Blood 105, 292-300. (Pubitemid 40053096)
20. Panaretou, B., Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W. and Pearl, L. H. (1998). ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17, 4829-4836. (Pubitemid 28377183)
21. Pandolfi, P. P., Grignani, F., Alcalay, M., Mencarelli, A., Biondi, A., LoCoco, F., Grignani, F. and Pelicci, P. G. (1991). Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties. Oncogene 6, 1285-1292. (Pubitemid 21924220)
22. Perry, J. and Zhao, Y. (2003). The CW domain, a structural module shared amongst vertebrates, vertebrate-infecting parasites and higher plants. Trends Biochem. Sci. 28, 576-580.
23. Platani, M., Goldberg, I., Lamond, A. I. and Swedlow, J. R. (2002). Cajal body dynamics and association with chromatin are ATP-dependent. Nat. Cell Biol. 4, 502-508.
24. Richter, K. and Buchner, J. (2006). hsp90: twist and fold. Cell 127, 251-253.
25. Sacho, E. J., Kadyrov, F. A., Modrich, P., Kunkel, T. A. and Erie, D. A. (2008). Direct visualization of asymmetric adenine-nucleotide-induced conformational changes in MutL alpha. Mol. Cell 29, 112-121.
26. Saitoh, N., Uchimura, Y., Tachibana, T., Sugahara, S., Saitoh, H. and Nakao, M. (2006). In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies. Exp. Cell Res. 312, 1418-1430.
27. Shen, T. H., Lin, H. K., Scaglioni, P. P., Yung, T. M. and Pandolfi, P. P. (2006). The mechanisms of PML-nuclear body formation. Mol. Cell 24, 331-339.
28. Shiau, A. K., Harris, S. F., Southworth, D. R. and Agard, D. A. (2006). Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 127, 329-340.
29. Spector, D. L., Goldman, R. D. and Leinwand, L. A. (1998). Cells: a Laboratory Manual. Cold Spring Harbor NY: Cold Spring Harbor Laboratory Press.
30. Takahashi, K., Yoshida, N., Murakami, N., Kawata, K., Ishizaki, H., Tanaka-Okamoto, M., Miyoshi, J., Zinn, A. R., Shime, H. and Inoue, N. (2007). Dynamic regulation of p53 subnuclear localization and senescence by MORC3. Mol. Biol. Cell 18, 1701-1709.
31. Tran, P. T. and Liskay, R. M. (2000). Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha. Mol. Cell. Biol. 20, 6390-6398.
32. Tsai, R. Y. and McKay, R. D. (2005). A multistep, GTP-driven mechanism controlling the dynamic cycling of nucleostemin. J. Cell Biol. 168, 179-184.
33. Wang, Z. G., Delva, L., Gaboli, M., Rivi, 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. (Pubitemid 28217080)
34. Watanabe, R., Kinoshita, T., Masaki, R., Yamamoto, A., Takeda, J. and Inoue, N. (1996). PIG-A and PIG-H, which participate in glycosylphosphatidylinositol anchor biosynthesis, form a protein complex in the endoplasmic reticulum. J. Biol. Chem. 271, 26868-26875.
35. Zacharias, D. A., Violin, J. D., Newton, A. C. and Tsien, R. Y. (2002). Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296, 913-916.
36. Zhao, Y., Kwon, S. W., Anselmo, A., Kaur, K. and White, M. A. (2004). Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins. J. Biol. Chem. 279, 20999-21002.
37. Zhong, S., Muller, S., Ronchetti, S., Freemont, P. S., Dejean, A. and Pandolfi, P. P. (2000). Role of SUMO-1-modified PML in nuclear body formation. Blood 95, 2748-2752.