Multifaceted functions of Siva-1: More than an Indian God of Destruction

Protein and Cell

Volumn 3, Issue 2, 2012, Pages 117-122

  Mei, Yide ^a   Wu, Mian ^a  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

Author keywords

apoptosis; p53; Siva 1; stathmin; tumor metastasis

Indexed keywords

ANTIMETASTATIC AGENT; BINDING PROTEIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; PROTEIN BCL 2; PROTEIN BCL X; PROTEIN MDM2; PROTEIN P53; SIVA 1 PROTEIN; STATHMIN; UNCLASSIFIED DRUG;

ANTINEOPLASTIC ACTIVITY; APOPTOSIS; AUTOREGULATION; CELLULAR STRESS SIGNAL; DNA DAMAGE; EPITHELIAL MESENCHYMAL TRANSITION; GENE; GENE EXPRESSION REGULATION; GENE FUNCTION; GENE OVEREXPRESSION; GENE SILENCING; GENETIC ASSOCIATION; HUMAN; METASTASIS; METASTASIS INHIBITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; REVIEW; SIVA 1 GENE; SIVA 2 GENE;

EID: 84862839296     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-012-2018-5     Document Type: Review

References (42)

1. Barkinge, J. L., Gudi, R., Sarah, H., Chu, F., Borthakur, A., Prabhakar, B. S., and Prasad, K. V. (2009). The p53-induced Siva-1 plays a significant role in cisplatin-mediated apoptosis. J Carcinog 8, 2.
2. Beckerman, R., and Prives, C. (2010). Transcriptional regulation by p53. Cold Spring Harb Perspect Biol 2, a000935.
3. Cao, C., Ren, X., Kharbanda, S., Koleske, A., Prasad, K. V., and Kufe, D. (2001). The ARG tyrosine kinase interacts with Siva-1 in the apoptotic response to oxidative stress. J Biol Chem 276, 11465-11468.
4. Chambers, A. F., Groom, A. C., and MacDonald, I. C. (2002). Dissemination and growth of cancer cells in metastatic sites. Nat Rev Cancer 2, 563-572.
5. Chu, F., Barkinge, J., Hawkins, S., Gudi, R., Salgia, R., and Kanteti, P. V. (2005). Expression of Siva-1 protein or its putative amphipathic helical region enhances cisplatin-induced apoptosis in breast cancer cells: effect of elevated levels of BCL-2. Cancer Res 65, 5301-5309.
6. Daoud, S. S., Munson, P. J., Reinhold, W., Young, L., Prabhu, V. V., Yu, Q., LaRose, J., Kohn, K. W., Weinstein, J. N., and Pommier, Y. (2003). Impact of p53 knockout and topotecan treatment on gene expression profiles in human colon carcinoma cells: a pharmacogenomic study. Cancer Res 63, 2782-2793.
7. Du, W., Jiang, P., Li, N., Mei, Y., Wang, X., Wen, L., Yang, X., and Wu, M. (2009). Suppression of p53 activity by Siva1. Cell Death Differ 16, 1493-1504.
8. E, S., Lai, Y. J., Tsukahara, R., Chen, C. S., Fujiwara, Y., Yue, J., Yu, J. H., Guo, H., Kihara, A., Tigyi, G., et al. (2009). Lysophosphatidic acid 2 receptor-mediated supramolecular complex formation regulates its antiapoptotic effect. J Biol Chem 284, 14558-14571.
9. Elmore, S. (2007). Apoptosis: a review of programmed cell death. Toxicol Pathol 35, 495-516.
10. Fortin, A., MacLaurin, J. G., Arbour, N., Cregan, S. P., Kushwaha, N., Callaghan, S. M., Park, D. S., Albert, P. R., and Slack, R. S. (2004). The proapoptotic gene SIVA is a direct transcriptional target for the tumor suppressors p53 and E2F1. J Biol Chem 279, 28706-28714.
11. Gudi, R., Barkinge, J., Hawkins, S., Chu, F., Manicassamy, S., Sun, Z., Duke-Cohan, J. S., and Prasad, K. V. (2006). Siva-1 negatively regulates NF-kappaB activity: effect on T-cell receptor-mediated activation-induced cell death (AICD). Oncogene 25, 3458-3462.
12. Haupt, Y., Maya, R., Kazaz, A., and Oren, M. (1997). Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299.
13. Henke, A., Launhardt, H., Klement, K., Stelzner, A., Zell, R., and Munder, T. (2000). Apoptosis in coxsackievirus B3-caused diseases: interaction between the capsid protein VP2 and the proapoptotic protein siva. J Virol 74, 4284-4290.
14. Henke, A., Nestler, M., Strunze, S., Saluz, H. P., Hortschansky, P., Menzel, B., Martin, U., Zell, R., Stelzner, A., and Munder, T. (2001). The apoptotic capability of coxsackievirus B3 is influenced by the efficient interaction between the capsid protein VP2 and the proapoptotic host protein Siva. Virology 289, 15-22.
15. Jacobs, S. B., Basak, S., Murray, J. I., Pathak, N., and Attardi, L. D. (2007). Siva is an apoptosis-selective p53 target gene important for neuronal cell death. Cell Death Differ 14, 1374-1385.
16. Korsmeyer, S. J. (1999). BCL-2 gene family and the regulation of programmed cell death. Cancer Res 59, 1693s-1700s.
17. Kubbutat, M. H., Jones, S. N., and Vousden, K. H. (1997). Regulation of p53 stability by Mdm2. Nature 387, 299-303.
18. Li, N., Jiang, P., Du, W., Wu, Z., Li, C., Qiao, M., Yang, X., and Wu, M. (2011). Siva1 suppresses epithelial-mesenchymal transition and metastasis of tumor cells by inhibiting stathmin and stabilizing microtubules. Proc Natl Acad Sci U S A 108, 12851-12856.
19. Lin, F. T., Lai, Y. J., Makarova, N., Tigyi, G., and Lin, W. C. (2007). The lysophosphatidic acid 2 receptor mediates down-regulation of Siva-1 to promote cell survival. J Biol Chem 282, 37759-37769.
20. Manna, T., Thrower, D. A., Honnappa, S., Steinmetz, M. O., and Wilson, L. (2009). Regulation of microtubule dynamic instability in vitro by differentially phosphorylated stathmin. J Biol Chem 284, 15640-15649.
21. Maya, R., Balass, M., Kim, S. T., Shkedy, D., Leal, J. F., Shifman, O., Moas, M., Buschmann, T., Ronai, Z., Shiloh, Y., et al. (2001). ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage. Genes Dev 15, 1067-1077.
22. Muller, P. A., Vousden, K. H., and Norman, J. C. (2011). p53 and its mutants in tumor cell migration and invasion. J Cell Biol 192, 209-218.
23. Okuno, K., Yasutomi, M., Nishimura, N., Arakawa, T., Shiomi, M., Hida, J., Ueda, K., and Minami, K. (2001). Gene expression analysis in colorectal cancer using practical DNA array filter. Dis Colon Rectum 44, 295-299.
24. Padanilam, B. J., Lewington, A. J., and Hammerman, M. R. (1998). Expression of CD27 and ischemia/reperfusion-induced expression of its ligand Siva in rat kidneys. Kidney Int 54, 1967-1975.
25. Polyak, K., and Weinberg, R. A. (2009). Transitions between epithelial and mesenchymal states: acquisition of malignant and stem cell traits. Nat Rev Cancer 9, 265-273.
26. Prasad, K. V., Ao, Z., Yoon, Y., Wu, M. X., Rizk, M., Jacquot, S., and Schlossman, S. F. (1997). CD27, a member of the tumor necrosis factor receptor family, induces apoptosis and binds to Siva, a proapoptotic protein. Proc Natl Acad Sci U S A 94, 6346-6351.
27. Py, B., Bouchet, J., Jacquot, G., Sol-Foulon, N., Basmaciogullari, S., Schwartz, O., Biard-Piechaczyk, M., and Benichou, S. (2007). The Siva protein is a novel intracellular ligand of the CD4 receptor that promotes HIV-1 envelope-induced apoptosis in T-lymphoid cells. Apoptosis 12, 1879-1892.
28. Py, B., Slomianny, C., Auberger, P., Petit, P. X., and Benichou, S. (2004). Siva-1 and an alternative splice form lacking the death domain, Siva-2, similarly induce apoptosis in T lymphocytes via a caspase-dependent mitochondrial pathway. J Immunol 172, 4008-4017.
29. Rana, S., Maples, P. B., Senzer, N., and Nemunaitis, J. (2008). Stathmin 1: a novel therapeutic target for anticancer activity. Expert Rev Anticancer Ther 8, 1461-1470.
30. Resch, U., Schichl, Y. M., Winsauer, G., Gudi, R., Prasad, K., and de Martin, R. (2009). Siva1 is a XIAP-interacting protein that balances NFkappaB and JNK signalling to promote apoptosis. J Cell Sci 122, 2651-2661.
31. Shimoda, H. K., Shide, K., Kameda, T., Matsunaga, T., and Shimoda, K. (2010). Tyrosine kinase 2 interacts with the proapoptotic protein Siva-1 and augments its apoptotic functions. Biochem Biophys Res Commun 400, 252-257.
32. Spinicelli, S., Nocentini, G., Ronchetti, S., Krausz, L. T., Bianchini, R., and Riccardi, C. (2002). GITR interacts with the pro-apoptotic protein Siva and induces apoptosis. Cell Death Differ 9, 1382-1384.
33. Thiery, J. P., Acloque, H., Huang, R. Y., and Nieto, M. A. (2009). Epithelial-mesenchymal transitions in development and disease. Cell 139, 871-890.
34. Thompson, C. B. (1995). Apoptosis in the pathogenesis and treatment of disease. Science 267, 1456-1462.
35. Vaux, D. L., and Korsmeyer, S. J. (1999). Cell death in development. Cell 96, 245-254.
36. Vogelstein, B., Lane, D., and Levine, A. J. (2000). Surfing the p53 network. Nature 408, 307-310.
37. Vousden, K. H., and Lu, X. (2002). Live or let die: the cell's response to p53. Nat Rev Cancer 2, 594-604.
38. Walmsley, S. R., Chilvers, E. R., Thompson, A. A., Vaughan, K., Marriott, H. M., Parker, L. C., Shaw, G., Parmar, S., Schneider, M., Sabroe, I., et al. (2011). Prolyl hydroxylase 3 (PHD3) is essential for hypoxic regulation of neutrophilic inflammation in humans and mice. J Clin Invest 121, 1053-1063.
39. Xiao, H., Palhan, V., Yang, Y., and Roeder, R. G. (2000). TIP30 has an intrinsic kinase activity required for up-regulation of a subset of apoptotic genes. EMBO J 19, 956-963.
40. Xue, L., Chu, F., Cheng, Y., Sun, X., Borthakur, A., Ramarao, M., Pandey, P., Wu, M., Schlossman, S. F., and Prasad, K. V. (2002). Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosis. Proc Natl Acad Sci U S A 99, 6925-6930.
41. Yan, J., Menendez, D., Yang, X. P., Resnick, M. A., and Jetten, A. M. (2009). A regulatory loop composed of RAP80-HDM2-p53 provides RAP80-enhanced p53 degradation by HDM2 in response to DNA damage. J Biol Chem 284, 19280-19289.
42. Yoon, Y., Ao, Z., Cheng, Y., Schlossman, S. F., and Prasad, K. V. (1999). Murine Siva-1 and Siva-2, alternate splice forms of the mouse Siva gene, both bind to CD27 but differentially transduce apoptosis. Oncogene 18, 7174-7179.