Table of Contents
ISRN Cell Biology
Volume 2013 (2013), Article ID 867613, 11 pages
http://dx.doi.org/10.1155/2013/867613
Research Article

Generation of Constitutive Active ERK Mutants as Tools for Cancer Research in Zebrafish

Institute of Biology, Leiden University, Einsteinweg 55, 2333 CC Leiden, The Netherlands

Received 26 August 2013; Accepted 26 September 2013

Academic Editors: J.-F. Bodart, R. Hurta, and P. Storz

Copyright © 2013 Hanan Rian et al. 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. J. A. McCubrey, L. S. Steelman, W. H. Chappell et al., “Roles of the Raf/MEK/ERK pathway in cell growth, malignant transformation and drug resistance,” Biochimica et Biophysica Acta, vol. 1773, no. 8, pp. 1263–1284, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. P. J. Roberts and C. J. Der, “Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer,” Oncogene, vol. 26, no. 22, pp. 3291–3310, 2007. View at Publisher · View at Google Scholar · View at Scopus
  3. S. Yoon and R. Seger, “The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions,” Growth Factors, vol. 24, no. 1, pp. 21–44, 2006. View at Publisher · View at Google Scholar · View at Scopus
  4. A. Zebisch, A. P. Czernilofsky, G. Keri, J. Smigelskaite, H. Sill, and J. Troppmair, “Signaling through RAS-RAF-MEK-ERK: from basics to bedside,” Current Medicinal Chemistry, vol. 14, no. 5, pp. 601–623, 2007. View at Publisher · View at Google Scholar · View at Scopus
  5. Z. Wei and H. T. Liu, “MAPK signal pathways in the regulation of cell proliferation in mammalian cells,” Cell Research, vol. 12, no. 1, pp. 9–18, 2002. View at Google Scholar · View at Scopus
  6. R. Hoshino, Y. Chatani, T. Yamori et al., “Constitutive activation of the 41-/43-kDa mitogen-activated protein kinase signaling pathway in human tumors,” Oncogene, vol. 18, no. 3, pp. 813–822, 1999. View at Publisher · View at Google Scholar · View at Scopus
  7. N. Askari, R. Diskin, M. Avitzour, G. Yaakov, O. Livnah, and D. Engelberg, “MAP-quest: could we produce constitutively active variants of MAP kinases?” Molecular and Cellular Endocrinology, vol. 252, no. 1-2, pp. 231–240, 2006. View at Publisher · View at Google Scholar · View at Scopus
  8. S. J. Mansour, W. T. Matten, A. S. Hermann et al., “Transformation of mammalian cells by constitutively active MAP kinase kinase,” Science, vol. 265, no. 5174, pp. 966–970, 1994. View at Google Scholar · View at Scopus
  9. S. Cowley, H. Paterson, P. Kemp, and C. J. Marshall, “Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells,” Cell, vol. 77, no. 6, pp. 841–852, 1994. View at Publisher · View at Google Scholar · View at Scopus
  10. W. Kolch, G. Heidecker, P. Lloyd, and U. R. Rapp, “Raf-1 protein kinase is required for growth of induced NIH/3T3 cells,” Nature, vol. 349, no. 6308, pp. 426–428, 1991. View at Publisher · View at Google Scholar · View at Scopus
  11. F. A. Scholl, P. A. Dumesic, and P. A. Khavari, “Effects of active MEK1 expression in vivo,” Cancer Letters, vol. 230, no. 1, pp. 1–5, 2005. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Karasarides, A. Chiloeches, R. Hayward et al., “B-RAF is a therapeutic target in melanoma,” Oncogene, vol. 23, no. 37, pp. 6292–6298, 2004. View at Publisher · View at Google Scholar · View at Scopus
  13. E. E. Patton, H. R. Widlund, J. L. Kutok et al., “BRAF mutations are sufficient to promote nevi formation and cooperate with p53 in the genesis of melanoma,” Current Biology, vol. 15, no. 3, pp. 249–254, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. E. E. Patton and L. I. Zon, “Taking human cancer genes to the fish: a transgenic model of melanoma in zebrafish,” Zebrafish, vol. 1, no. 4, pp. 363–368, 2005. View at Publisher · View at Google Scholar · View at Scopus
  15. J. F. Amatruda and E. E. Patton, “Genetic models of cancer in zebrafish,” International Review of Cell and Molecular Biology, vol. 271, pp. 1–34, 2008. View at Google Scholar · View at Scopus
  16. J. F. Amatruda, J. L. Shepard, H. M. Stern, and L. I. Zon, “Zebrafish as a cancer model system,” Cancer Cell, vol. 1, no. 3, pp. 229–231, 2002. View at Publisher · View at Google Scholar · View at Scopus
  17. W. Goessling, T. E. North, and L. I. Zon, “New waves of discovery: modeling cancer in zebrafish,” Journal of Clinical Oncology, vol. 25, no. 17, pp. 2473–2479, 2007. View at Publisher · View at Google Scholar · View at Scopus
  18. H. L. Siew, L. W. Yi, V. B. Vega et al., “Conservation of gene expression signatures between zebrafish and human liver tumors and tumor progression,” Nature Biotechnology, vol. 24, no. 1, pp. 73–75, 2006. View at Publisher · View at Google Scholar · View at Scopus
  19. K. Stoletov and R. Klemke, “Catch of the day: zebrafish as a human cancer model,” Oncogene, vol. 27, no. 33, pp. 4509–4520, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. D. E. Abbott, L.-M. Postovit, E. A. Seftor, N. V. Margaryan, R. E. B. Seftor, and M. J. C. Hendrix, “Exploiting the convergence of embryonic and tumorigenic signaling pathways to develop new therapeutic targets,” Stem Cell Reviews, vol. 3, no. 1, pp. 68–78, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. M. J. C. Hendrix, E. A. Seftor, R. E. B. Seftor, J. Kasemeier-Kulesa, P. M. Kulesa, and L.-M. Postovit, “Reprogramming metastatic tumour cells with embryonic microenvironments,” Nature Reviews Cancer, vol. 7, no. 4, pp. 246–255, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. A. Moustakas and C.-H. Heldin, “Signaling networks guiding epithelial-mesenchymal transitions during embryogenesis and cancer progression,” Cancer Science, vol. 98, no. 10, pp. 1512–1520, 2007. View at Publisher · View at Google Scholar · View at Scopus
  23. S. F. G. Krens, S. He, G. E. M. Lamers et al., “Distinct functions for ERK1 and ERK2 in cell migration processes during zebrafish gastrulation,” Developmental Biology, vol. 319, no. 2, pp. 370–383, 2008. View at Publisher · View at Google Scholar · View at Scopus
  24. M. A. Emrick, A. N. Hoofnagle, A. S. Miller, L. F. Ten Eyck, and N. G. Ahn, “Constitutive activation of extracellular signal-regulated kinase 2 by synergistic point mutations,” Journal of Biological Chemistry, vol. 276, no. 49, pp. 46469–46479, 2001. View at Publisher · View at Google Scholar · View at Scopus
  25. J. P. Hall, V. Cherkasova, E. Elion, M. C. Gustin, and E. Winter, “The osmoregulatory pathway represses mating pathway activity in Saccharomyces cerevisiae: isolation of a FUS3 mutant that is insensitive to the repression mechanism,” Molecular and Cellular Biology, vol. 16, no. 12, pp. 6715–6723, 1996. View at Google Scholar · View at Scopus
  26. D. Brunner, N. Oellers, J. Szabad, W. H. Biggs III, S. Lawrence Zipursky, and E. Hafen, “A gain-of-function mutation in Drosophila MAP kinase activates multiple receptor tyrosine kinase signaling pathways,” Cell, vol. 76, no. 5, pp. 875–888, 1994. View at Publisher · View at Google Scholar · View at Scopus
  27. M. Tsang, S. Maegawa, A. Kiang, R. Habas, E. Weinberg, and I. B. Dawid, “A role for MKP3 in axial patterning of the zebrafish embryo,” Development, vol. 131, no. 12, pp. 2769–2779, 2004. View at Publisher · View at Google Scholar · View at Scopus
  28. H. A. Harrington, M. Komorowski, M. Beguerisse-Diaz, G. M. Ratto, and M. P. Stumpf, “Mathematical modeling reveals the functional implications of the different nuclear shuttling rates of Erk1 and Erk2,” Physical Biology, vol. 9, Article ID 036001, 2012. View at Google Scholar
  29. H. Shankaran, D. L. Ippolito, W. B. Chrisler et al., “Rapid and sustained nuclear-cytoplasmic ERK oscillations induced by epidermal growth factor,” Molecular Systems Biology, vol. 5, article 332, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. G. A. Molina, S. C. Watkins, and M. Tsang, “Generation of FGF reporter transgenic zebrafish and their utility in chemical screens,” BMC Developmental Biology, vol. 7, article 62, 2007. View at Publisher · View at Google Scholar · View at Scopus
  31. R. A. MacCorkle and T.-H. Tan, “Mitogen-activated protein kinases in cell-cycle control,” Cell Biochemistry and Biophysics, vol. 43, no. 3, pp. 451–461, 2005. View at Publisher · View at Google Scholar · View at Scopus
  32. K. Coulonval, H. Kooken, and P. P. Roger, “Coupling of T161 and T14 phosphorylations protects cyclin B-CDK1 from premature activation,” Molecular Biology of the Cell, vol. 22, no. 21, pp. 3971–3985, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. W. Krek and E. A. Nigg, “Cell cycle regulation of vertebrate p34cdc2 activity: identification of Thr161 as an essential in vivo phosphorylation site,” The New Biologist, vol. 4, no. 4, pp. 323–329, 1992. View at Google Scholar · View at Scopus