Table of Contents
ISRN Oncology
Volume 2012, Article ID 928120, 5 pages
http://dx.doi.org/10.5402/2012/928120
Research Article

The Opposing Roles of Cellular Inhibitor of Apoptosis Proteins in Cancer

Breast Cancer Research Lab, Department of Cellular and Molecular Medicine, University of Ottawa, 451 Smyth Road, Ottawa, ON, Canada K1H 8M5

Received 17 June 2012; Accepted 19 July 2012

Academic Editors: A. M. Garcia-Lora and F. Kuhnel

Copyright © 2012 R. Lau and M. A. C. Pratt. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. G. S. Salvesen and C. S. Duckett, “IAP proteins: blocking the road to death's door,” Nature Reviews Molecular Cell Biology, vol. 3, no. 6, pp. 401–410, 2002. View at Publisher · View at Google Scholar · View at Scopus
  2. M. G. Hinds, R. S. Norton, D. L. Vaux, and C. L. Day, “Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat,” Nature Structural Biology, vol. 6, no. 7, pp. 648–651, 1999. View at Publisher · View at Google Scholar · View at Scopus
  3. S. M. Srinivasula and J. D. Ashwell, “IAPs: what's in a name?” Molecular Cell, vol. 30, no. 2, pp. 123–135, 2008. View at Publisher · View at Google Scholar · View at Scopus
  4. B. P. Eckelman and G. S. Salvesen, “The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases,” Journal of Biological Chemistry, vol. 281, no. 6, pp. 3254–3260, 2006. View at Publisher · View at Google Scholar · View at Scopus
  5. S. Hu and X. Yang, “Cellular inhibitor of apoptosis 1 and 2 are ubiquitin ligases for the apoptosis inducer Smac/DIABLO,” Journal of Biological Chemistry, vol. 278, no. 12, pp. 10055–10060, 2003. View at Publisher · View at Google Scholar · View at Scopus
  6. Y. E. Choi, M. Butterworth, S. Malladi, C. S. Duckett, G. M. Cohen, and S. B. Bratton, “The E3 ubiquitin ligase cIAP1 binds and ubiquitinates caspase-3 and -7 via unique mechanisms at distinct steps in their processing,” Journal of Biological Chemistry, vol. 284, no. 19, pp. 12772–12782, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. D. L. Vaux and J. Silke, “IAPs, RINGs and ubiquitylation,” Nature Reviews Molecular Cell Biology, vol. 6, no. 4, pp. 287–297, 2005. View at Publisher · View at Google Scholar · View at Scopus
  8. M. J. M. Bertrand, S. Milutinovic, K. M. Dickson et al., “cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination,” Molecular Cell, vol. 30, no. 6, pp. 689–700, 2008. View at Publisher · View at Google Scholar · View at Scopus
  9. T. Samuel, K. Welsh, T. Lober, S. H. Togo, J. M. Zapata, and J. C. Reed, “Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases,” Journal of Biological Chemistry, vol. 281, no. 2, pp. 1080–1090, 2006. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Karin, Y. Cao, F. R. Greten, and Z. W. Li, “NF-κB in cancer: from innocent bystander to major culprit,” Nature Reviews Cancer, vol. 2, no. 4, pp. 301–310, 2002. View at Google Scholar · View at Scopus
  11. M. Rothe, M. G. Pan, W. J. Henzel, T. M. Ayres, and D. V. Goeddel, “The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins,” Cell, vol. 83, no. 7, pp. 1243–1252, 1995. View at Publisher · View at Google Scholar · View at Scopus
  12. H. Hsu, J. Xiong, and D. V. Goeddel, “The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation,” Cell, vol. 81, no. 4, pp. 495–504, 1995. View at Google Scholar · View at Scopus
  13. C. Wang, L. Deng, M. Hong, G. R. Akkaraju, J. I. Inoue, and Z. J. Chen, “TAK1 is a ubiquitin-dependent kinase of MKK and IKK,” Nature, vol. 412, no. 6844, pp. 346–351, 2001. View at Publisher · View at Google Scholar · View at Scopus
  14. E. Varfolomeev, T. Goncharov, A. V. Fedorova et al., “c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor α (TNFα)-induced NF-κB activation,” Journal of Biological Chemistry, vol. 283, no. 36, pp. 24295–24299, 2008. View at Publisher · View at Google Scholar · View at Scopus
  15. C. Y. Wang, M. W. Mayo, R. G. Korneluk, D. V. Goeddel, and A. S. Baldwin, “NF-B antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c- IAP2 to suppress caspase-8 activation,” Science, vol. 281, no. 5383, pp. 1680–1683, 1998. View at Publisher · View at Google Scholar · View at Scopus
  16. M. Karin and A. Lin, “NF-κB at the crossroads of life and death,” Nature Immunology, vol. 3, no. 3, pp. 221–227, 2002. View at Publisher · View at Google Scholar · View at Scopus
  17. G. Liao, M. Zhang, E. W. Harhaj, and S. C. Sun, “Regulation of the NF-κB-inducing kinase by tumor necrosis factor receptor-associated factor 3-induced degradation,” Journal of Biological Chemistry, vol. 279, no. 25, pp. 26243–26250, 2004. View at Publisher · View at Google Scholar · View at Scopus
  18. B. J. Zarnegar, Y. Wang, D. J. Mahoney et al., “Noncanonical NF-κB activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK,” Nature Immunology, vol. 9, no. 12, pp. 1371–1378, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. S. Vallabhapurapu, A. Matsuzawa, W. Z. Zhang et al., “Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-κB signaling,” Nature Immunology, vol. 9, no. 12, pp. 1364–1370, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. C. M. Annunziata, R. E. Davis, Y. Demchenko et al., “Frequent engagement of the classical and alternative NF-κB pathways by diverse genetic abnormalities in multiple myeloma,” Cancer Cell, vol. 12, no. 2, pp. 115–130, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. J. J. Keats, R. Fonseca, M. Chesi et al., “Promiscuous mutations activate the noncanonical NF-κB pathway in multiple myeloma,” Cancer Cell, vol. 12, no. 2, pp. 131–144, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. Z. Liu, H. Li, X. Wu et al., “Detachment-induced upregulation of XIAP and cIAP2 delays anoikis of intestinal epithelial cells,” Oncogene, vol. 25, no. 59, pp. 7680–7690, 2006. View at Publisher · View at Google Scholar · View at Scopus
  23. R. B. Hamanaka, E. Bobrovnikova-Marjon, X. Ji, S. A. Liebhaber, and J. A. Diehl, “PERK-dependent regulation of IAP translation during ER stress,” Oncogene, vol. 28, no. 6, pp. 910–920, 2009. View at Publisher · View at Google Scholar · View at Scopus
  24. Z. L. Chu, T. A. McKinsey, L. Liu, J. J. Gentry, M. H. Malim, and D. W. Ballard, “Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-κB control,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 19, pp. 10057–10062, 1997. View at Publisher · View at Google Scholar · View at Scopus
  25. S. Y. Hong, W. H. Yoon, J. H. Park, S. G. Kang, J. H. Ahn, and T. H. Lee, “Involvement of two NF-κB binding elements in tumor necrosis factor α-, CD40-, and Epstein-Barr virus latent membrane protein 1-mediated induction of the cellular inhibitor of apoptosis protein 2 gene,” Journal of Biological Chemistry, vol. 275, no. 24, pp. 18022–18028, 2000. View at Publisher · View at Google Scholar · View at Scopus
  26. Z. Liu, H. Li, M. Derouet et al., “ras oncogene triggers up-regulation of cIAP2 and XIAP in intestinal epithelial cells: epidermal growth factor receptor-dependent and -independent mechanisms of ras-induced transformation,” Journal of Biological Chemistry, vol. 280, no. 45, pp. 37383–37392, 2005. View at Publisher · View at Google Scholar · View at Scopus
  27. H. H. Wu, J. Y. Wu, Y. W. Cheng et al., “cIAP2 upregulated by E6 oncoprotein via epidermal growth factor receptor/phosphatidylinositol 3-kinase/AKT pathway confers resistance to cisplatin in human papillomavirus 16/18-infected lung cancer,” Clinical Cancer Research, vol. 16, no. 21, pp. 5200–5210, 2010. View at Publisher · View at Google Scholar · View at Scopus
  28. C. W. Wright and C. S. Duckett, “Reawakening the cellular death program in neoplasia through the therapeutic blockade of IAP function,” Journal of Clinical Investigation, vol. 115, no. 10, pp. 2673–2678, 2005. View at Publisher · View at Google Scholar · View at Scopus
  29. Z. Dai, W. G. Zhu, C. D. Morrison et al., “A comprehensive search for DNA amplification in lung cancer identifies inhibitors of apoptosis cIAP1 and cIAP2 as candidate oncogenes,” Human Molecular Genetics, vol. 12, no. 7, pp. 791–801, 2003. View at Publisher · View at Google Scholar · View at Scopus
  30. E. C. LaCasse, D. J. Mahoney, H. H. Cheung, S. Plenchette, S. Baird, and R. G. Korneluk, “IAP-targeted therapies for cancer,” Oncogene, vol. 27, no. 48, pp. 6252–6275, 2008. View at Publisher · View at Google Scholar · View at Scopus
  31. I. Imoto, Z. Q. Yang, A. Pimkhaokham et al., “Identification of cIAP1 as a candidate target gene within an amplicon at 11q22 in esophageal squamous cell carcinomas,” Cancer Research, vol. 61, no. 18, pp. 6629–6634, 2001. View at Google Scholar · View at Scopus
  32. T. Akagi, M. Motegi, A. Tamura et al., “A novel gene, MALT1 at 18q21, is involved in t(11;18) (q21;q21) found in low-grade B-cell lymphoma of mucosa-associated lymphoid tissue,” Oncogene, vol. 18, no. 42, pp. 5785–5794, 1999. View at Publisher · View at Google Scholar · View at Scopus
  33. J. Dierlamm, M. Baens, I. Wlodarska et al., “The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are recurrently rearranged in the t(11;18)(q21;q21) associated with mucosa- associated lymphoid tissue lymphomas,” Blood, vol. 93, no. 11, pp. 3601–3609, 1999. View at Google Scholar · View at Scopus
  34. D. Vucic and W. J. Fairbrother, “The inhibitor of apoptosis proteins as therapeutic targets in cancer,” Clinical Cancer Research, vol. 13, no. 20, pp. 5995–6000, 2007. View at Publisher · View at Google Scholar · View at Scopus
  35. E. Varfolomeev, J. W. Blankenship, S. M. Wayson et al., “IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis,” Cell, vol. 131, no. 4, pp. 669–681, 2007. View at Publisher · View at Google Scholar · View at Scopus
  36. J. E. Vince, W. W. L. Wong, N. Khan et al., “IAP antagonists target cIAP1 to induce TNFα-dependent apoptosis,” Cell, vol. 131, no. 4, pp. 682–693, 2007. View at Publisher · View at Google Scholar · View at Scopus
  37. S. L. Petersen, L. Wang, A. Yalcin-Chin et al., “Autocrine TNFα signaling renders human cancer cells susceptible to smac-mimetic-induced apoptosis,” Cancer Cell, vol. 12, no. 5, pp. 445–456, 2007. View at Publisher · View at Google Scholar · View at Scopus
  38. D. J. Mahoney, H. H. Cheung, R. Lejmi Mrad et al., “Both cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 33, pp. 11778–11783, 2008. View at Publisher · View at Google Scholar · View at Scopus
  39. L. Wang, F. Du, and X. Wang, “TNF-α induces two distinct caspase-8 activation pathways,” Cell, vol. 133, no. 4, pp. 693–703, 2008. View at Publisher · View at Google Scholar · View at Scopus
  40. H. H. Cheung, D. J. Mahoney, E. C. LaCasse, and R. G. Korneluk, “Down-regulation of c-FLIP enhances death of cancer cells by Smac mimetic compound,” Cancer Research, vol. 69, no. 19, pp. 7729–7738, 2009. View at Publisher · View at Google Scholar · View at Scopus
  41. D. Rossi, S. Deaglio, D. Dominguez-Sola et al., “Alteration of BIRC3 and multiple other NF-kappaB pathway genes in splenic marginal zone lymphoma,” Blood, vol. 118, no. 18, pp. 4930–4934, 2011. View at Publisher · View at Google Scholar
  42. D. Rossi, M. Fangazio, S. Rasi et al., “Disruption of BIRC3 associates with fludarabine chemorefractoriness in TP53 wild-type chronic lymphocytic leukemia,” Blood, vol. 119, no. 12, pp. 2854–2862, 2012. View at Publisher · View at Google Scholar
  43. V. Tergaonkar, M. Pando, O. Vafa, G. Wahl, and I. Verma, “p53 stabilization is decreased upon NFκB activation: a role for NFκB in acquisition of resistance to chemotherapy,” Cancer Cell, vol. 1, no. 5, pp. 493–503, 2002. View at Publisher · View at Google Scholar · View at Scopus
  44. U. Siebenlist, K. Brown, and E. Claudio, “Control of lymphocyte development by nuclear factor-kB,” Nature Reviews Immunology, vol. 5, no. 6, pp. 435–445, 2005. View at Publisher · View at Google Scholar · View at Scopus
  45. D. S. Bassères and A. S. Baldwin, “Nuclear factor-κB and inhibitor of κB kinase pathways in oncogenic initiation and progression,” Oncogene, vol. 25, no. 51, pp. 6817–6830, 2006. View at Publisher · View at Google Scholar · View at Scopus