Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2018, Article ID 5473725, 9 pages
https://doi.org/10.1155/2018/5473725
Research Article

Oncogenic N-Ras Stimulates SRF-Mediated Transactivation via H3 Acetylation at Lysine 9

1School of Biological Sciences, College of Natural Sciences, Chungbuk National University, Cheongju, Chungbuk 361-763, Republic of Korea
2Hazardous Substances Analysis Division, Seoul Regional Food and Drug Administration, Ministry of Food and Drug Safety, Seoul 07978, Republic of Korea
3Department of Cogno-Mechatronics Engineering, Pusan National University, Busan 46241, Republic of Korea

Correspondence should be addressed to Byung H. Jhun; rk.ca.nasup@nuhjb and Kyunghwan Kim; rk.ca.kubgnuhc@mikgnuyk

Received 19 August 2017; Revised 18 October 2017; Accepted 21 November 2017; Published 3 January 2018

Academic Editor: Andrey Cherstvy

Copyright © 2018 Sun-Ju Yi 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. L. Bos, “Ras Oncogenes in human cancer: a review,” Cancer Research, vol. 49, no. 17, pp. 4682–4689, 1989. View at Google Scholar · View at Scopus
  2. H. R. Bourne, D. A. Sanders, and F. McCormick, “The GTPase superfamily: A conserved switch for diverse cell functions,” Nature, vol. 348, no. 6297, pp. 125–132, 1990. View at Publisher · View at Google Scholar · View at Scopus
  3. G. A. Hobbs, C. J. Der, and K. L. Rossman, “RAS isoforms and mutations in cancer at a glance,” Journal of Cell Science, vol. 129, no. 7, pp. 1287–1292, 2016. View at Publisher · View at Google Scholar · View at Scopus
  4. A. D. Cox and C. J. Der, “Ras history: the saga continues,” Small GTPases, vol. 1, no. 1, pp. 2–27, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. M. Barbacid, “Ras genes,” Annual Review of Biochemistry, vol. 56, pp. 779–827, 1987. View at Publisher · View at Google Scholar · View at Scopus
  6. M. D. Delgado, A. F. Quincoces, M. T. Gomez-Casares et al., “Differential expression of ras protooncogenes during in vitro differentiation of human erythroleukemia cells,” Cancer Res, vol. 52, no. 21, pp. 5979–5984, 1992. View at Google Scholar
  7. J. Leon, I. Guerrero, and A. Pellicer, “Differential expression of the ras gene family in mice,” Molecular and Cellular Biology, vol. 7, no. 4, pp. 1535–1540, 1987. View at Publisher · View at Google Scholar · View at Scopus
  8. J. A. Parker and C. Mattos, “The Ras-membrane interface: Isoform-specific differences in the catalytic domain,” Molecular Cancer Research, vol. 13, no. 4, pp. 595–603, 2015. View at Publisher · View at Google Scholar · View at Scopus
  9. R. D. Kornberg and Y. Lorch, “Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome,” Cell, vol. 98, no. 3, pp. 285–294, 1999. View at Publisher · View at Google Scholar · View at Scopus
  10. K. Luger, A. W. Mäder, R. K. Richmond, D. F. Sargent, and T. J. Richmond, “Crystal structure of the nucleosome core particle at 2.8 Å resolution,” Nature, vol. 389, no. 6648, pp. 251–260, 1997. View at Publisher · View at Google Scholar · View at Scopus
  11. T. Kouzarides, “Chromatin modifications and their function,” Cell, vol. 128, no. 4, pp. 693–705, 2007. View at Publisher · View at Google Scholar · View at Scopus
  12. T. Kusch and J. L. Workman, “Histone variants and complexes involved in their exchange,” Subcell Biochem, vol. 41, pp. 91–109, 2007. View at Google Scholar
  13. G. G. Wang, C. D. Allis, and P. Chi, “Chromatin remodeling and cancer, part II: ATP-dependent chromatin remodeling,” Trends in Molecular Medicine, vol. 13, no. 9, pp. 373–380, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. W. An, V. B. Palhan, M. A. Karymov, S. H. Leuba, and R. G. Roeder, “Selective requirements for histone H3 and H4 N termini in p300-dependent transcriptional activation from chromatin,” Molecular Cell, vol. 9, no. 4, pp. 811–821, 2002. View at Publisher · View at Google Scholar · View at Scopus
  15. K. Struhl, “Histone acetylation and transcriptional regulatory mechanisms,” Genes & Development, vol. 12, no. 5, pp. 599–606, 1998. View at Publisher · View at Google Scholar · View at Scopus
  16. Y. Liu, D.-L. Wang, S. Chen, L. Zhao, and F.-L. Sun, “Oncogene Ras/phosphatidylinositol 3-kinase signaling targets histone H3 acetylation at lysine 56,” The Journal of Biological Chemistry, vol. 287, no. 49, pp. 41469–41480, 2012. View at Publisher · View at Google Scholar · View at Scopus
  17. I. Mazón Peláez, M. Kalogeropoulou, A. Ferraro et al., “Oncogenic RAS alters the global and gene-specific histone modification pattern during epithelial-mesenchymal transition in colorectal carcinoma cells,” The International Journal of Biochemistry & Cell Biology, vol. 42, no. 6, pp. 911–920, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Sánchez-Molina, C. Estarás, J. L. Oliva et al., “Regulation of CBP and Tip60 coordinates histone acetylation at local and global levels during Ras-induced transformation,” Carcinogenesis, vol. 35, no. 10, pp. 2194–2202, 2014. View at Publisher · View at Google Scholar · View at Scopus
  19. B. Nabet, P. Ó Broin, J. M. Reyes et al., “Deregulation of the ras-erk signaling axis modulates the enhancer landscape,” Cell Reports, vol. 12, no. 8, pp. 1300–1313, 2015. View at Publisher · View at Google Scholar · View at Scopus
  20. M.-J. Oh, T. van Agthoven, J.-E. Choi et al., “BCAR3 regulates EGF-induced DNA synthesis in normal human breast MCF-12A cells,” Biochemical and Biophysical Research Communications, vol. 375, no. 3, pp. 430–434, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. B. H. Jhun, D. W. Rose, B. L. Seely et al., “Microinjection of the SH2 domain of the 85-kilodalton subunit of phosphatidylinositol 3-kinase inhibits insulin-induced DNA synthesis and c-fos expression,” Molecular and Cellular Biology, vol. 14, no. 11, pp. 7466–7475, 1994. View at Publisher · View at Google Scholar · View at Scopus
  22. K. Kim, V. Punj, J.-M. Kim et al., “MMP-9 facilitates selective proteolysis of the histone H3 tail at genes necessary for proficient osteoclastogenesis,” Genes & Development, vol. 30, no. 2, pp. 208–219, 2016. View at Publisher · View at Google Scholar · View at Scopus
  23. K. Kim, V. Punj, J. Choi et al., “Gene dysregulation by histone variant H2A.Z in bladder cancer,” Epigenetics & Chromatin, vol. 6, article 34, 2013. View at Publisher · View at Google Scholar · View at Scopus
  24. C. Gauthier-Rouviere, A. Fernandez, and N. J. C. Lamb, “Ras-induced c-fos expression and proliferation in living rat fibroblasts involves C-kinase activation and the serum response element pathway,” EMBO Journal, vol. 9, no. 1, pp. 171–180, 1990. View at Google Scholar · View at Scopus
  25. R. Johnson, B. Spiegelman, D. Hanahan, and R. Wisdom, “Cellular transformation and malignancy induced by ras require c-jun,” Molecular and Cellular Biology, vol. 16, no. 8, pp. 4504–4511, 1996. View at Publisher · View at Google Scholar · View at Scopus
  26. O. Millán, A. Ballester, A. Castrillo et al., “H-Ras-specific activation of NF-κB protects NIH 3T3 cells against stimulus-dependent apoptosis,” Oncogene, vol. 22, no. 4, pp. 477–483, 2003. View at Publisher · View at Google Scholar · View at Scopus
  27. A. Kikuchi, S. D. Demo, Z.-H. Ye, Y.-W. Chen, and L. T. Williams, “ralGDS family members interact with the effector loop of ras p21,” Molecular and Cellular Biology, vol. 14, no. 11, pp. 7483–7491, 1994. View at Publisher · View at Google Scholar · View at Scopus
  28. M. Okazaki, S. Kishida, T. Hinoi et al., “Synergistic activation of c-fos promoter activity by Raf and Ral GDP dissociation stimulator,” Oncogene, vol. 14, no. 5, pp. 515–521, 1997. View at Publisher · View at Google Scholar · View at Scopus
  29. T. Waldmann and R. Schneider, “Targeting histone modifications—epigenetics in cancer,” Current Opinion in Cell Biology, vol. 25, no. 2, pp. 184–189, 2013. View at Publisher · View at Google Scholar · View at Scopus
  30. M. E. Katz and F. McCormick, “Signal transduction from multiple Ras effectors,” Current Opinion in Genetics & Development, vol. 7, no. 1, pp. 75–79, 1997. View at Publisher · View at Google Scholar · View at Scopus
  31. S. L. Campbell, R. Khosravi-Far, K. L. Rossman, G. J. Clark, and C. J. Der, “Increasing complexity of Ras signaling,” Oncogene, vol. 17, no. 11, pp. 1395–1413, 1998. View at Publisher · View at Google Scholar · View at Scopus
  32. E. Ferro and L. Trabalzini, “RalGDS family members couple Ras to Ral signalling and that's not all,” Cellular Signalling, vol. 22, no. 12, pp. 1804–1810, 2010. View at Publisher · View at Google Scholar · View at Scopus
  33. D. Vigil, T. D. Martin, F. Williams, J. Jen Yeh, S. L. Campbell, and C. J. Der, “Aberrant overexpression of the Rgl2 Ral small GTPase-specific guanine nucleotide exchange factor promotes pancreatic cancer growth through Ral-dependent and Ral-independent mechanisms,” The Journal of Biological Chemistry, vol. 285, no. 45, pp. 34729–34740, 2010. View at Publisher · View at Google Scholar · View at Scopus
  34. C. Puppin, N. Passon, E. Lavarone et al., “Levels of histone acetylation in thyroid tumors,” Biochemical and Biophysical Research Communications, vol. 411, no. 4, pp. 679–683, 2011. View at Publisher · View at Google Scholar · View at Scopus
  35. V. Schwämmle and O. N. Jensen, “A computational model for histone mark propagation reproduces the distribution of heterochromatin in different human cell types,” PLoS ONE, vol. 8, no. 9, Article ID e73818, 2013. View at Publisher · View at Google Scholar · View at Scopus