Abstract
Apoptosis is a physiological mechanism to maintain human tissues or cells, and pathological dysfunction of this process explains some disease states or drug resistance. P53, mdm2, sumoylation, signal transduction, and transcriptional control are important in regulation in cancer cells. We focus on the mechanisms of apoptosis in cancer cells involving SUMO.
References
Babic, I., Cherry, E. and Fujita, D. J., 2006, SUMO modification of Sam68 enhances its ability to repress cyclin D1 expression and inhibits its ability to induce apoptosis. Oncogene 25, 4955–4964.
Bischof, O., Schwamborn, K., Martin, N., Werner, A., Sustman, C., Grosschendl, R. and Dejean, A., 2006, The E3 SUMO ligase PIASy is a regulator of cellular senescence and apoptosis. Mol. Cell 22, 783–794.
Buschmann, T., Fuchs, S. Y., Lee, C. G., Pan, Z. Q. and Ronai, Z., 2000, SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53. Cell 101, 753–762.
Carvajal, D., Tovar, C., Yang, H., Vu, B. T., Heimbrook, D. C and Vassilev, L. T., 2005, Activation of p53 by MDM2 antagonists can protect proliferating cells from mitotic inhibitors. Cancer Res. 65, 1918–1924.
Coll-Mulet, L., Iglesias-Serret, D., Santidrián, A. F., Cosialls, A. M., de Frias, M., Castano, E., Campas, C., Barragan, M., de Sevilla, A. F., Domingo, A., Vassilev, L. T., Pons, G. and Gil, J., 2006, MDM2 antagonists activate p53 and synergize with genotoxic drugs in B-cell chronic lymphocytic leukemia cells. Blood 107, 4109–4114.
Efeyan, A., Ortega-Molina, A., Velasco-Miguel, S., Herranz, D., Vassilev, L. T. and Serrano, M., 2007, Induction of p53-dependent senescence by the MDM2 antagonist nutlin-3a in mouse cells of fibroblast origin. Cancer Res. 67, 7350–7357.
Ennishi, D., Yokoyama, M., Terui, Y., Asai, H., Sakajiri, S., Mishima, Y., Takahashi, S., Komatsu, H., Ikeda, K., Takeuchi, K., Tanimoto, M. and Hatake, K., 2009, Soluble interleukin-2 receptor retains prognostic value in patients with diffuse large B-cell lymphoma receiving rituximab plus CHOP (RCHOP) therapy. Ann. Oncol. 20, 526–533.
Fu, M., Wang, C., Wang, J., Zhang, X., Sakamaki, T., Yeung, Y. G., Chang, C., Hopp, T., Fuqua, S. A., Jaffray, E., Hay, R. T., Palvimo, J. J., Janne, O. A. and Pestell, R. G., 2002, Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function. Mol. Cell. Biol. 22, 3373–3388.
Huang, T. T., Wuerzberger-Davis, S. M., Wu, Z. H. and Miyamoto, S., 2003, Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress. Cell 115, 565–576.
Janz, M., Stühmer, T., Vassilev, L. T. and Bargou, R. C., 2007, Pharmacologic activation of p53-dependent and p53-independent apoptotic pathways in Hodgkin/Reed-Sternberg cells. Leukemia 21, 772–779.
Jennewein, C., Kuhn, A. M., Schmidt, M. V., Meilladec-Jullig, V., von Knethen, A., Gonzalez, F. J. and Brune, B., 2008, Sumoylation of peroxisome proliferator-activated receptor gamma by apoptotic cells prevents lipopolysaccharide-induced NCoR removal from kappaB binding sites mediating transrepression of proinflammatory cytokines. J. Immunol. 181, 5646–5652.
Kojima, K., Konopleva, M., Samudio, I. J., Shikami, M., Cabreira-Hansen, M., McQueen, T., Ruvolo, V., Tsao, T., Zeng, Z., Vassilev, L. T. and Andreeff, M., 2005, MDM2 antagonists induce p53-dependent apoptosis in AML: implications for leukemia therapy. Blood 106, 3150–3159.
Lee, P. S., Chang, C., Liu, D. and Derynck, R., 2003, Sumoylation of Smad4, the common Smad mediator of transforming growth factor-beta family signaling. J. Biol. Chem. 278, 27853–27863.
Lee, Y. S., Jang, M. S., Lee, J. S., Choi, E. J. and Kim, E., 2005, SUMO-1 represses apoptosis signal-regulating kinase 1 activation through physical interaction and not through covalent modification. EMBO Rep. 6, 949–955.
Mao, Y., Sun, M., Desai, S. D. and Liu, L. F., 2000. SUMO-1 conjugation to topoisomerase I: a possible repair response to topoisomerase-mediated DNA damage. Proc. Natl. Acad. Sci. U.S.A. 97, 4046–4051.
Meinecke, I., Cinski, A., Baier, A., Peters, M. A., Dankbar, B., Wille, A., Drynda, A., Mendoza, H., Gay, R. E., Hay, R. T., Ink, B., Gay, S. and Pap, T., 2007, Modification of nuclear PML protein by SUMO-1 regulates Fas-induced apoptosis in rheumatoid arthritis synovial fibroblasts. Proc. Natl. Acad. Sci. U.S.A. 104, 5073–5078.
Muromoto, R., M. Ishida, K. Sugiyama, Y. Sekine, K. Oritani, K. Shimoda, and Matsuda, T., 2006. Sumoylation of Daxx regulates IFN-induced growth suppression of B lymphocytes and the hormone receptor-mediated transactivation. J. Immunol. 177, 1160–1170.
Poukka, H., Karvonen, U., Janne, O. A. and Palvimo, J. J., 2000, Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. U.S.A. 97, 14145–14150.
Stühmer, T., Chatterjee, M., Hildebrandt, M., Herrmann, P., Gollasch, H., Gerecke, C., Theurich, S., Cigliano, L., Manz, R. A., Daniel, P. T., Bommert, K., Vassilev, L. T. and Bargou, R. C., 2005, Nongenotoxic activation of the p53 pathway as a therapeutic strategy for multiple myeloma. Blood 106, 3609–3617.
Utsubo-Kuniyoshi, R., Terui, Y., Mishima, Y., Rokudai, A., Mishima, Y., Sugimura, N., Kojima, K., Sonoda, Y., Kasahara, T. and Hatake, K., 2007, MEK-ERK is involved in SUMO-1 foci formation on apoptosis. Cancer Sci. 98, 569–576.
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., Fotouhi, N. and Liu, E. A., 2004, In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 303, 844–848.
Wasiak, S., Zunino, R. and McBride, H. M., 2007, Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death. J. Cell Biol. 177, 439–450.
Yang, Y., Ludwig, R. L., Jensen, J. P., Pierre, S. A., Medaglia, M. V., Davydov, I. V., Safiran, Y. J., Oberoi, P., Kenten, J. H., Phillips, A. C., Weissman, A. M. and Vousden, K. H., 2005, Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells. Cancer Cell 7, 547–559.
Zunino, R., Schauss, A., Rippstein, P., Andrade-Navarro, M. and McBride, H. M., 2007, The SUMO protease SENP5 is required to maintain mitochondrial morphology and function. J. Cell Sci. 120, 1178–1188.
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Hatake, K., Kuniyoshi, R., Mishima, Y., Terui, Y. (2009). Sumoylation and Apoptosis. In: Wilson, V. (eds) SUMO Regulation of Cellular Processes. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-2649-1_13
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DOI: https://doi.org/10.1007/978-90-481-2649-1_13
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