MEK-ERK is involved in SUMO-1 foci formation on apoptosis

Cancer Science

Volumn 98, Issue 4, 2007, Pages 569-576

  Utsubo Kuniyoshi, Ryoko ^a,b   Terui, Yasuhito ^a   Mishima, Yuko ^a   Rokudai, Akiko ^a   Mishima, Yuji ^a   Sugimura, Natsuhiko ^a   Kojima, Kiyotsugu ^a   Sonoda, Yoshiko ^b   Kasahara, Tadashi ^b   Hatake, Kiyohiko ^a  

^a CANCER CHEMOTHERAPY CENTER   (Japan)

^b KEIO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; GREEN FLUORESCENT PROTEIN; LEPTOMYCIN B; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MITOXANTRONE; PHORBOL 13 ACETATE 12 MYRISTATE; REAGENT; SMALL INTERFERING RNA; SUMO 1 PROTEIN; TUMOR PROMOTER;

APOPTOSIS; ARTICLE; CELL NUCLEUS; CELL STRAIN K 562; CONTROLLED STUDY; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN MODIFICATION; PROTEIN STABILITY; SUMOYLATION;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; APOPTOSIS; BUTADIENES; ENZYME INHIBITORS; EXTRACELLULAR SIGNAL-REGULATED MAP KINASES; FATTY ACIDS, UNSATURATED; HUMANS; K562 CELLS; MITOGEN-ACTIVATED PROTEIN KINASE KINASES; MITOGEN-ACTIVATED PROTEIN KINASES; MITOXANTRONE; NITRILES; RNA, SMALL INTERFERING; SIGNAL TRANSDUCTION; SUMO-1 PROTEIN; TETRADECANOYLPHORBOL ACETATE; TRANSFECTION;

EID: 34147177597     PISSN: 13479032     EISSN: 13497006     Source Type: Journal    
DOI: 10.1111/j.1349-7006.2007.00422.x     Document Type: Article

References (34)

1. Muller S, Ledl A, Schmidt D. SUMO: A regulator of gene expression and genome integrity. Oncogene 2004; 23: 1998-2008.
2. Seeler JS, Dejean A. SUMO: Of branched proteins and nuclear bodies. Oncogene 2001; 20: 7243-9.
3. Verger A, Perdomo J, Crossley M. Modification with SUMO. A role in transcriptional regulation. EMBO Rep 2003; 4: 137-42.
4. Terui Y, Saad N, Jia S, McKeon F, Yuan J. Dual role of sumoylation in the nuclear localization and transcriptional activation of NFAT. J Biol Chem 2004; 279: 28 257-65.
5. Zhong S, Muller S, Ronchetti S, Freemont PS, Dejean A, Pandolfi PP. Role of SUMO-1-modified PML in nuclear body formation. Blood 2000; 95: 2748-52.
6. Salomoni P, Pandolfi PP. The role of PML in tumor suppression. Cell 2002; 108: 165-70.
7. Zhong S, Salomoni P, Pandolfi PP. The transcriptional role of PML and the nuclear body. Nat Cell Biol 2000; 2: E85-90.
8. Carbone R, Pearson M, Minucci S, Pelicci PG. PML NBs associate with the hMre11 complex and p53 at sites of irradiation induced DNA damage. Oncogene 2002; 21: 1633-40.
9. Hofmann TG, Will H. Body language. The function of PML nuclear bodies in apoptosis regulation. Cell Death Differ 2003; 10: 1290-9.
10. Capranico G, Binaschi M. DNA sequence selectivity of topoisomerases and topoisomerase poisons. Biochim Biophys Acta 1998; 1400: 185-94.
11. Desai SD, Li TK, Rodriguez-Bauman A, Rubin EH, Liu LF. Ubiquitin/26S proteasome-mediated degradation of topoisomerase I as a resistance mechanism to camptothecin in tumor cells. Cancer Res 2001; 61: 5926-32.
12. Horie K, Tomida A, Sugimoto Y et al. SUMO-1 conjugation to intact DNA topoisomerase I amplifies cleavable complex formation induced by camptothecin. Oncogene 2002; 21: 7913-22.
13. Isik S, Sano K, Tsutsui K et al. The SUMO pathway is required for selective degradation of DNA topoisomerase IIbeta induced by a catalytic inhibitor ICRF-193(1). FEBS Lett 2003; 546: 374-8.
14. Mao Y, Desai SD, Liu LF. SUMO-1 conjugation to human DNA topoisomerase II isozymes. J Biol Chem 2000; 275: 26 066-73.
15. Tabilio A, Pelicci PG, Vinci G et al. Myeloid and megakaryocytic properties of K-562 cell lines. Cancer Res 1983; 43: 4569-74.
16. Villeval JL, Pelicci PG, Tabilio A et al. Erythroid properties of K562 cells. Effect of hemin, butyrate and TPA induction. Exp Cell Res 1983; 146: 428-35.
17. Racke FK, Lewandowska K, Goueli S, Goldfarb AN. Sustained activation of the extracellular signal-regulated kinase/mitogen-activated protein kinase pathway is required for megakaryocytic differentiation of K562 cells. J Biol Chem 1997; 272: 23 366-70.
18. Terui Y, Sakurai T, Mishima Y et al. Blockade of bulky lymphoma-associated CD55 expression by RNA interference overcomes resistance to complement-dependent cytotoxicity with rituximab. Cancer Sci 2006; 97: 72-9.
19. Khokhlatchev AV, Canagarajah B, Wilsbacher J. Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation. Cell 1998; 93: 605-15.
20. Kudo N, Wolff B, Sekimoto T. Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1. Exp Cell Res 1998; 242: 540-7.
21. Adachi M, Fukuda M, Nishida E. Nuclear export of MAP kinase (ERK) involves a MAP kinase kinase (MEK)-dependent active transport mechanism. J Cell Biol 2000; 148: 849-56.
22. Lange-Carter CA, Johnson GL. Ras-dependent growth factor regulation of MEK kinase in PC12 cells. Science 1994; 265: 1458-61.
23. Seger R, Seger D, Reszka AA. Overexpression of mitogen-activated protein kinase kinase (MAPKK) and its mutants in NIH 3T3 cells. Evidence that MAPKK involvement in cellular proliferation is regulated by phosphorylation of serine residues in its kinase subdomains VII and VIII. J Biol Chem 1994; 269: 25 699-709.
24. Chan YJ, Chiou CJ, Huang Q, Hayward GS. Synergistic interactions between overlapping binding sites for the serum response factor and ELK-1 proteins mediate both basal enhancement and phorbol ester responsiveness of primate cytomegalovirus major immediate-early promoters in monocyte and T-lymphocyte cell types. J Virol 1996; 70: 8590-605.
25. Tsunobuchi H, Ishisaki A, Imamura T. Expressions of inhibitory Smads, Smad6 and Smad7, are differentially regulated by TPA in human lung fibroblast cells. Biochem Biophys Res Commun 2004; 316: 712-9.
26. Zheng X, Ravatn R, Lin Y et al. Gene expression of TPA induced differentiation in HL-60 cells by DNA microarray analysis. Nucleic Acids Res 2002; 30: 4489-99.
27. Takeuchi N, Ueda T. Down-regulation of the mitochondrial translation system during terminal differentiation of HL-60 cells by 12-O-tetradecanoyl-1-phorbol-13-acetate: Comparison with the cytoplasmic translation system. J Biol Chem 2003; 278: 45 318-24.
28. Slosberg ED, Yao Y, Xing F, Ikui A, Jirousek MR, Weinstein IB. The protein kinase C beta-specific inhibitor LY379196 blocks TPA-induced monocytic differentiation of HL60 cells the protein kinase C beta-specific inhibitor LY379196 blocks TPA-induced monocytic differentiation of HL60 cells. Mol Carcinog 2000; 27: 166-76.
29. Yang SH, Jaffray E, Hay RH, Sharrocks AD. Dynamic interplay of the SUMO and ERK pathways in regulating Elk-1 transcriptional activity. Mol Cell 2003; 12: 63-74.
30. Salinas S, Briancon-Marjollet A, Bossis G. SUMOylation regulates nucleo-cytoplasmic shuttling of Elk-1. J Cell Biol 2004; 165: 767-73.
31. Choi BK, Choi CH, Oh HL, Kim YK. Role of ERK activation in cisplatin-induced apoptosis in A172 human glioma cells. Neurotoxicology 2004; 25: 915-24.
32. Wang X, Martindale JL, Holbrook NJ. Requirement for ERK activation in cisplatin-induced apoptosis. J Biol Chem 2000; 275: 39 435-43.
33. Kim YH, Choi CY, Kim Y. Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1. Proc Natl Acad Sci USA 1999; 96: 12 3 50 -5.
34. Tojo M, Matsuzaki K, Minami T et al. The aryl hydrocarbon receptor nuclear transporter is modulated by the SUMO-1 conjugation system. J Biol Chem 2002; 277: 46 576-85.