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Mediators of Inflammation
Volume 2016 (2016), Article ID 4028353, 11 pages
http://dx.doi.org/10.1155/2016/4028353
Review Article

The Role of Protein Arginine Methyltransferases in Inflammatory Responses

1Department of Genetic Engineering, Sungkyunkwan University, Suwon 440-746, Republic of Korea
2Research Institute and Hospital, National Cancer Center, Goyang 410-769, Republic of Korea

Received 29 December 2015; Accepted 14 February 2016

Academic Editor: Donna-Marie McCafferty

Copyright © 2016 Ji Hye Kim 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. S. Akira, S. Uematsu, and O. Takeuchi, “Pathogen recognition and innate immunity,” Cell, vol. 124, no. 4, pp. 783–801, 2006. View at Publisher · View at Google Scholar · View at Scopus
  2. T. Lawrence, “The nuclear factor NF-κB pathway in inflammation,” Cold Spring Harbor Perspectives in Biology, vol. 1, no. 6, Article ID a001651, 2009. View at Publisher · View at Google Scholar · View at Scopus
  3. S.-J. Moon, J.-H. Jeong, J. Y. Jhun et al., “Ursodeoxycholic acid ameliorates pain severity and cartilage degeneration in monosodium iodoacetate-induced osteoarthritis in rats,” Immune Network, vol. 14, no. 1, pp. 45–53, 2014. View at Publisher · View at Google Scholar
  4. T. J. Guzik, R. Korbut, and T. Adamek-Guzik, “Nitric oxide and superoxide in inflammation and immune regulation,” Journal of Physiology and Pharmacology, vol. 54, no. 4, pp. 469–487, 2003. View at Google Scholar · View at Scopus
  5. Y.-J. Hwang, J. Song, H.-R. Kim, and K.-A. Hwang, “Oleanolic acid regulates NF-κB signaling by suppressing MafK expression in RAW 264.7 cells,” BMB Reports, vol. 47, no. 9, pp. 524–529, 2014. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Cotran, C. Kumar, T. Collins, and W. Robbins, Pathologic Basis of Disease, Saunders, Philadelphia, Pa, USA, 1999.
  7. K. H. Kim, T. S. Kim, J. G. Lee et al., “Characterization of proinflammatory responses and innate signaling activation in macrophages infected with Mycobacterium scrofulaceum,” Immune Network, vol. 14, no. 6, pp. 307–320, 2014. View at Publisher · View at Google Scholar
  8. I. B. McInnes and G. Schett, “The pathogenesis of rheumatoid arthritis,” The New England Journal of Medicine, vol. 365, no. 23, pp. 2205–2219, 2011. View at Publisher · View at Google Scholar · View at Scopus
  9. S. Lim and S. Park, “Role of vascular smooth muscle cell in the inflammation of atherosclerosis,” BMB Reports, vol. 47, no. 1, pp. 1–7, 2014. View at Publisher · View at Google Scholar · View at Scopus
  10. X. Cheng and R. Blumenthal, S-Adenosylmethionine-Dependent Methyltransferases: Structures and Functions, World Scientific, Singapore, 1999.
  11. T. O. Yeates, “Structures of SET domain proteins: protein lysine methyltransferases make their mark,” Cell, vol. 111, no. 1, pp. 5–7, 2002. View at Publisher · View at Google Scholar · View at Scopus
  12. J. D. Romano and S. Michaelis, “Topological and mutational analysis of Saccharomyces cerevisiae Ste14p, founding member of the isoprenylcysteine carboxyl methyltransferase family,” Molecular Biology of the Cell, vol. 12, no. 7, pp. 1957–1971, 2001. View at Publisher · View at Google Scholar · View at Scopus
  13. J. E. Katz, M. Dlakić, and S. Clarke, “Automated identification of putative methyltransferases from genomic open reading frames,” Molecular & Cellular Proteomics, vol. 2, no. 8, pp. 525–540, 2003. View at Google Scholar · View at Scopus
  14. X. Zhang, L. Zhou, and X. Cheng, “Crystal structure of the conserved core of protein arginine methyltransferase PRMT3,” The EMBO Journal, vol. 19, no. 14, pp. 3509–3519, 2000. View at Publisher · View at Google Scholar · View at Scopus
  15. M. T. Bedford, “Arginine methylation at a glance,” Journal of Cell Science, vol. 120, no. 24, pp. 4243–4246, 2007. View at Publisher · View at Google Scholar · View at Scopus
  16. J.-H. Lee, J. R. Cook, Z.-H. Yang et al., “PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine,” The Journal of Biological Chemistry, vol. 280, no. 5, pp. 3656–3664, 2005. View at Publisher · View at Google Scholar · View at Scopus
  17. Y. Yang, A. Hadjikyriacou, Z. Xia et al., “PRMT9 is a Type II methyltransferase that methylates the splicing factor SAP145,” Nature Communications, vol. 6, p. 6428, 2015. View at Publisher · View at Google Scholar
  18. A. Hadjikyriacou, Y. Yang, A. Espejo, M. T. Bedford, and S. G. Clarke, “Unique features of human protein arginine methyltransferase 9 (PRMT9) and its substrate RNA splicing factor SF3B2,” The Journal of Biological Chemistry, vol. 290, no. 27, pp. 16723–16743, 2015. View at Publisher · View at Google Scholar
  19. C. I. Zurita-Lopez, T. Sandberg, R. Kelly, and S. G. Clarke, “Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues,” Journal of Biological Chemistry, vol. 287, no. 11, pp. 7859–7870, 2012. View at Publisher · View at Google Scholar · View at Scopus
  20. A. Niewmierzycka and S. Clarke, “S-adenosylmethionine-dependent methylation in Saccharomyces cerevisiae: identification of a novel protein arginine methyltransferase,” The Journal of Biological Chemistry, vol. 274, no. 2, pp. 814–824, 1999. View at Publisher · View at Google Scholar · View at Scopus
  21. Q. Feng, B. He, S.-Y. Jung et al., “Biochemical control of CARM1 enzymatic activity by phosphorylation,” The Journal of Biological Chemistry, vol. 284, no. 52, pp. 36167–36174, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. K. Higashimoto, P. Kuhn, D. Desai, X. Cheng, and W. Xu, “Phosphorylation-mediated inactivation of coactivator-associated arginine methyltransferase 1,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 30, pp. 12318–12323, 2007. View at Publisher · View at Google Scholar · View at Scopus
  23. W. D. Cheung, K. Sakabe, M. P. Housley, W. B. Dias, and G. W. Hart, “O-linked β-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins,” The Journal of Biological Chemistry, vol. 283, no. 49, pp. 33935–33941, 2008. View at Publisher · View at Google Scholar · View at Scopus
  24. K. Sakabe and G. W. Hart, “O-GlcNAc transferase regulates mitotic chromatin dynamics,” Journal of Biological Chemistry, vol. 285, no. 45, pp. 34460–34468, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. P. Kuhn, R. Chumanov, Y. Wang, Y. Ge, R. R. Burgess, and W. Xu, “Automethylation of CARM1 allows coupling of transcription and mRNA splicing,” Nucleic Acids Research, vol. 39, no. 7, pp. 2717–2726, 2011. View at Publisher · View at Google Scholar · View at Scopus
  26. F. Liu, X. Zhao, F. Perna et al., “JAK2V617F-mediated phosphorylation of PRMT5 downregulates its methyltransferase activity and promotes myeloproliferation,” Cancer Cell, vol. 19, no. 2, pp. 283–294, 2011. View at Publisher · View at Google Scholar · View at Scopus
  27. A. Frankel, N. Yadav, J. Lee, T. L. Branscombe, S. Clarke, and M. T. Bedford, “The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity,” The Journal of Biological Chemistry, vol. 277, no. 5, pp. 3537–3543, 2002. View at Publisher · View at Google Scholar · View at Scopus
  28. J. Sayegh, K. Webb, D. Cheng, M. T. Bedford, and S. G. Clarke, “Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain,” Journal of Biological Chemistry, vol. 282, no. 50, pp. 36444–36453, 2007. View at Publisher · View at Google Scholar · View at Scopus
  29. W. J. Friesen, A. Wyce, S. Paushkin et al., “A novel WD repeat protein component of the methylosome binds Sm proteins,” The Journal of Biological Chemistry, vol. 277, no. 10, pp. 8243–8247, 2002. View at Publisher · View at Google Scholar · View at Scopus
  30. S. Pal, S. N. Vishwanath, H. Erdjument-Bromage, P. Tempst, and S. Sif, “Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes,” Molecular and Cellular Biology, vol. 24, no. 21, pp. 9630–9645, 2004. View at Publisher · View at Google Scholar · View at Scopus
  31. T.-W. Chuang, P.-J. Peng, and W.-Y. Tarn, “The exon junction complex component Y14 modulates the activity of the methylosome in biogenesis of spliceosomal small nuclear ribonucleoproteins,” The Journal of Biological Chemistry, vol. 286, no. 11, pp. 8722–8728, 2011. View at Publisher · View at Google Scholar · View at Scopus
  32. N.-Z. Lei, X.-Y. Zhang, H.-Z. Chen et al., “A feedback regulatory loop between methyltransferase PRMT1 and orphan receptor TR3,” Nucleic Acids Research, vol. 37, no. 3, pp. 832–848, 2009. View at Publisher · View at Google Scholar · View at Scopus
  33. Y. Robin-Lespinasse, S. Sentis, C. Kolytcheff, M.-C. Rostan, L. Corbo, and M. Le Romancer, “hCAF1, a new regulator of PRMT1-dependent arginine methylation,” Journal of Cell Science, vol. 120, no. 4, pp. 638–647, 2007. View at Publisher · View at Google Scholar · View at Scopus
  34. W.-J. Lin, J. D. Gary, M. C. Yang, S. Clarke, and H. R. Herschman, “The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase,” The Journal of Biological Chemistry, vol. 271, no. 25, pp. 15034–15044, 1996. View at Publisher · View at Google Scholar · View at Scopus
  35. M. L. Pak, T. M. Lakowski, D. Thomas, M. I. Vhuiyan, K. Hüsecken, and A. Frankel, “A protein arginine N-methyltransferase 1 (PRMT1) and 2 heteromeric interaction increases PRMT1 enzymatic activity,” Biochemistry, vol. 50, no. 38, pp. 8226–8240, 2011. View at Publisher · View at Google Scholar
  36. V. Singh, T. Branscombe Miranda, W. Jiang et al., “DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo,” Oncogene, vol. 23, no. 47, pp. 7761–7771, 2004. View at Publisher · View at Google Scholar · View at Scopus
  37. P. Jelinic, J.-C. Stehle, and P. Shaw, “The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation,” PLoS Biology, vol. 4, no. 11, article e355, 2006. View at Publisher · View at Google Scholar · View at Scopus
  38. L. Wang, S. Pal, and S. Sif, “Protein arginine methyltransferase 5 suppresses the transcription of the RB family of tumor suppressors in leukemia and lymphoma cells,” Molecular and Cellular Biology, vol. 28, no. 20, pp. 6262–6277, 2008. View at Publisher · View at Google Scholar · View at Scopus
  39. M. R. Pawlak, C. A. Scherer, J. Chen, M. J. Roshon, and H. E. Ruley, “Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable,” Molecular and Cellular Biology, vol. 20, no. 13, pp. 4859–4869, 2000. View at Publisher · View at Google Scholar · View at Scopus
  40. Z. Yu, T. Chen, J. Hébert, E. Li, and S. Richard, “A mouse PRMT1 null allele defines an essential role for arginine methylation in genome maintenance and cell proliferation,” Molecular and Cellular Biology, vol. 29, no. 11, pp. 2982–2996, 2009. View at Publisher · View at Google Scholar · View at Scopus
  41. D. Kim, J. Lee, D. Cheng et al., “Enzymatic activity is required for the in vivo functions of CARM1,” The Journal of Biological Chemistry, vol. 285, no. 2, pp. 1147–1152, 2010. View at Publisher · View at Google Scholar · View at Scopus
  42. N. Yadav, J. Lee, J. Kim et al., “Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 11, pp. 6464–6468, 2003. View at Publisher · View at Google Scholar · View at Scopus
  43. W.-W. Tee, M. Pardo, T. W. Theunissen et al., “Prmt5 is essential for early mouse development and acts in the cytoplasm to maintain ES cell pluripotency,” Genes & Development, vol. 24, no. 24, pp. 2772–2777, 2010. View at Publisher · View at Google Scholar · View at Scopus
  44. M. Bezzi, S. X. Teo, J. Muller et al., “Regulation of constitutive and alternative splicing by PRMT5 reveals a role for Mdm4 pre-mRNA in sensing defects in the spliceosomal machinery,” Genes & Development, vol. 27, no. 17, pp. 1903–1916, 2013. View at Publisher · View at Google Scholar · View at Scopus
  45. M. Neault, F. A. Mallette, G. Vogel, J. Michaud-Levesque, and S. Richard, “Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor,” Nucleic Acids Research, vol. 40, no. 19, pp. 9513–9521, 2012. View at Publisher · View at Google Scholar · View at Scopus
  46. D. Cheng, J. Côté, S. Shaaban, and M. T. Bedford, “The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing,” Molecular Cell, vol. 25, no. 1, pp. 71–83, 2007. View at Publisher · View at Google Scholar · View at Scopus
  47. D. Chen, M. Ma, H. Hong et al., “Regulation of transcription by a protein methyltransferase,” Science, vol. 284, no. 5423, pp. 2174–2177, 1999. View at Publisher · View at Google Scholar · View at Scopus
  48. W. Xu, H. Chen, K. Du et al., “A transcriptional switch mediated by cofactor methylation,” Science, vol. 294, no. 5551, pp. 2507–2511, 2001. View at Publisher · View at Google Scholar · View at Scopus
  49. L. A. Hart, V. L. Krishnan, I. M. Adcock, P. J. Barnes, and K. F. Chung, “Activation and localization of transcription factor, nuclear factor-κB, in asthma,” American Journal of Respiratory and Critical Care Medicine, vol. 158, no. 5, pp. 1585–1592, 1998. View at Publisher · View at Google Scholar · View at Scopus
  50. M. F. Neurath, C. Becker, and K. Barbulescu, “Role of NF-κB in immune and inflammatory responses in the gut,” Gut, vol. 43, no. 6, pp. 856–860, 1998. View at Publisher · View at Google Scholar · View at Scopus
  51. M. Feldmann, F. M. Brennan, and R. N. Maini, “Role of cytokines in rheumatoid arthritis,” Annual Review of Immunology, vol. 14, no. 1, pp. 397–440, 1996. View at Publisher · View at Google Scholar · View at Scopus
  52. M. Karin, “The beginning of the end: IκB kinase (IKK) and NF-κB activation,” The Journal of Biological Chemistry, vol. 274, no. 39, pp. 27339–27342, 1999. View at Publisher · View at Google Scholar · View at Scopus
  53. E. Zandi, D. M. Rothwarf, M. Delhase, M. Hayakawa, and M. Karin, “The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for Iκb phosphorylation and NF-κB activation,” Cell, vol. 91, no. 2, pp. 243–252, 1997. View at Publisher · View at Google Scholar · View at Scopus
  54. U. Senftleben, Y. Cao, G. Xiao et al., “Activation by IKKα of a second, evolutionary conserved, NF-κB signaling pathway,” Science, vol. 293, no. 5534, pp. 1495–1499, 2001. View at Publisher · View at Google Scholar · View at Scopus
  55. M. Karin and Y. Ben-Neriah, “Phosphorylation meets ubiquitination: the control of NF-κB activity,” Annual Review of Immunology, vol. 18, no. 1, pp. 621–663, 2000. View at Publisher · View at Google Scholar · View at Scopus
  56. G. Bonizzi and M. Karin, “The two NF-κB activation pathways and their role in innate and adaptive immunity,” Trends in Immunology, vol. 25, no. 6, pp. 280–288, 2004. View at Publisher · View at Google Scholar · View at Scopus
  57. M. E. Gerritsen, A. J. Williams, A. S. Neish, S. Moore, Y. Shi, and T. Collins, “CREB-binding protein/p300 are transcriptional coactivators of p65,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 7, pp. 2927–2932, 1997. View at Publisher · View at Google Scholar · View at Scopus
  58. W. An, J. Kim, and R. G. Roeder, “Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53,” Cell, vol. 117, no. 6, pp. 735–748, 2004. View at Publisher · View at Google Scholar · View at Scopus
  59. M. Covic, P. O. Hassa, S. Saccani et al., “Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-κB-dependent gene expression,” The EMBO Journal, vol. 24, no. 1, pp. 85–96, 2005. View at Publisher · View at Google Scholar · View at Scopus
  60. Y.-H. Lee, S. A. Coonrod, W. L. Kraus, M. A. Jelinek, and M. R. Stallcup, “Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 10, pp. 3611–3616, 2005. View at Publisher · View at Google Scholar · View at Scopus
  61. J. Tang, A. Frankel, R. J. Cook et al., “PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells,” The Journal of Biological Chemistry, vol. 275, no. 11, pp. 7723–7730, 2000. View at Publisher · View at Google Scholar · View at Scopus
  62. H. Wang, Z.-Q. Huang, L. Xia et al., “Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor,” Science, vol. 293, no. 5531, pp. 853–857, 2001. View at Publisher · View at Google Scholar · View at Scopus
  63. S. Weber, F. Maaß, M. Schuemann, E. Krause, G. Suske, and U.-M. Bauer, “PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling,” Genes & Development, vol. 23, no. 1, pp. 118–132, 2009. View at Publisher · View at Google Scholar · View at Scopus
  64. L. Jobert, M. Argentini, and L. Tora, “PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function,” Experimental Cell Research, vol. 315, no. 7, pp. 1273–1286, 2009. View at Publisher · View at Google Scholar · View at Scopus
  65. K. Yamagata, H. Daitoku, Y. Takahashi et al., “Arginine methylation of FOXO transcription factors inhibits their phosphorylation by Akt,” Molecular Cell, vol. 32, no. 2, pp. 221–231, 2008. View at Publisher · View at Google Scholar · View at Scopus
  66. Q.-Z. Sun, F.-F. Jiao, X.-D. Yang et al., “Expression of protein arginine N-methyltransferases in E3 rat models of acute asthma,” Journal of Southern Medical University, vol. 30, no. 4, pp. 716–719, 2010. View at Google Scholar · View at Scopus
  67. M. E. Banwell, N. S. Tolley, T. J. Williams, and T. J. Mitchell, “Regulation of human eotaxin-3/CCL26 expression: modulation by cytokines and glucocorticoids,” Cytokine, vol. 17, no. 6, pp. 317–323, 2002. View at Publisher · View at Google Scholar · View at Scopus
  68. Q. Sun, X. Yang, B. Zhong et al., “Upregulated protein arginine methyltransferase 1 by IL-4 increases eotaxin-1 expression in airway epithelial cells and participates in antigen-induced pulmonary inflammation in rats,” Journal of Immunology, vol. 188, no. 7, pp. 3506–3512, 2012. View at Publisher · View at Google Scholar · View at Scopus
  69. H. Igarashi, K. Kuwahara, M. Yoshida et al., “GANP suppresses the arginine methyltransferase PRMT5 regulating IL-4-mediated STAT6-signaling to IgE production in B cells,” Molecular Immunology, vol. 46, no. 6, pp. 1031–1041, 2009. View at Publisher · View at Google Scholar · View at Scopus
  70. Q. Sun, L. Liu, M. Roth et al., “PRMT1 upregulated by epithelial proinflammatory cytokines participates in COX2 expression in fibroblasts and chronic antigen-induced pulmonary inflammation,” The Journal of Immunology, vol. 195, no. 1, pp. 298–306, 2015. View at Publisher · View at Google Scholar
  71. S. Bhattacharya, C. L. Michels, M.-K. Leung, Z. P. Arany, A. L. Kung, and D. M. Livingston, “Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1,” Genes & Development, vol. 13, no. 1, pp. 64–75, 1999. View at Publisher · View at Google Scholar · View at Scopus
  72. S. D. Bamforth, J. Bragança, J. J. Eloranta et al., “Cardiac malformations, adrenal agenesis, neural crest defects and exencephaly in mice lacking Cited2, a new Tfap2 co-activator,” Nature Genetics, vol. 29, no. 4, pp. 469–474, 2001. View at Publisher · View at Google Scholar · View at Scopus
  73. W. J. Weninger, K. L. Floro, M. B. Bennett et al., “Cited2 is required both for heart morphogenesis and establishment of the left-right axis in mouse development,” Development, vol. 132, no. 6, pp. 1337–1348, 2005. View at Publisher · View at Google Scholar · View at Scopus
  74. Z. Yin, J. Haynie, X. Yang et al., “The essential role of Cited2, a negative regulator for HIF-1α, in heart development and neurulation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 16, pp. 10488–10493, 2002. View at Publisher · View at Google Scholar · View at Scopus
  75. K. R. Kranc, H. Schepers, N. P. Rodrigues et al., “Cited2 is an essential regulator of adult hematopoietic stem cells,” Cell Stem Cell, vol. 5, no. 6, pp. 659–665, 2009. View at Publisher · View at Google Scholar · View at Scopus
  76. X. Lou, S. Sun, W. Chen et al., “Negative feedback regulation of NF-κB action by CITED2 in the nucleus,” The Journal of Immunology, vol. 186, no. 1, pp. 539–548, 2011. View at Publisher · View at Google Scholar · View at Scopus
  77. M. A. Kleinschmidt, G. Streubel, B. Samans, M. Krause, and U.-M. Bauer, “The protein arginine methyltransferases CARM1 and PRMT1 cooperate in gene regulation,” Nucleic Acids Research, vol. 36, no. 10, pp. 3202–3213, 2008. View at Publisher · View at Google Scholar · View at Scopus
  78. P. O. Hassa, M. Covic, M. T. Bedford, and M. O. Hottiger, “Protein arginine methyltransferase 1 coactivates NF-κB-dependent gene expression synergistically with CARM1 and PARP1,” Journal of Molecular Biology, vol. 377, no. 3, pp. 668–678, 2008. View at Publisher · View at Google Scholar · View at Scopus
  79. B. D. Strahl, S. D. Briggs, C. J. Brame et al., “Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1,” Current Biology, vol. 11, no. 12, pp. 996–1000, 2001. View at Publisher · View at Google Scholar · View at Scopus
  80. D. Y. Lee, I. Ianculescu, D. Purcell, X. Zhang, X. Cheng, and M. R. Stallcup, “Surface-scanning mutational analysis of protein arginine methyltransferase 1: roles of specific amino acids in methyltransferase substrate specificity, oligomerization, and coactivator function,” Molecular Endocrinology, vol. 21, no. 6, pp. 1381–1393, 2007. View at Publisher · View at Google Scholar · View at Scopus
  81. E. Guccione, C. Bassi, F. Casadio et al., “Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive,” Nature, vol. 449, no. 7164, pp. 933–937, 2007. View at Publisher · View at Google Scholar · View at Scopus
  82. A. Di Lorenzo, Y. Yang, M. Macaluso, and M. T. Bedford, “A gain-of-function mouse model identifies PRMT6 as a NF-κB coactivator,” Nucleic Acids Research, vol. 42, no. 13, Article ID gku530, pp. 8297–8309, 2014. View at Publisher · View at Google Scholar · View at Scopus
  83. M. J. Harrison, Y. H. Tang, and D. H. Dowhan, “Protein arginine methyltransferase 6 regulates multiple aspects of gene expression,” Nucleic Acids Research, vol. 38, no. 7, pp. 2201–2216, 2010. View at Publisher · View at Google Scholar · View at Scopus
  84. W. J. Frazier, J. Xue, W. A. Luce, and Y. Liu, “MAPK signaling drives inflammation in LPS-stimulated cardiomyocytes: the route of crosstalk to G-protein-coupled receptors,” PLoS ONE, vol. 7, no. 11, Article ID e50071, 2012. View at Publisher · View at Google Scholar · View at Scopus
  85. J. Huang, M. D. Cardamone, H. E. Johnson et al., “Exchange factor TBL1 and arginine methyltransferase PRMT6 cooperate in protecting G protein pathway suppressor 2 (GPS2) from proteasomal degradation,” Journal of Biological Chemistry, vol. 290, no. 31, pp. 19044–19054, 2015. View at Publisher · View at Google Scholar
  86. M. Lacroix, S. El Messaoudi, G. Rodier, A. Le Cam, C. Sardet, and E. Fabbrizio, “The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5,” EMBO Reports, vol. 9, no. 5, pp. 452–458, 2008. View at Publisher · View at Google Scholar · View at Scopus
  87. C. S. Dacwag, Y. Ohkawa, S. Pal, S. Sif, and A. N. Imbalzano, “The protein arginine methyltransferase Prmt5 is required for myogenesis because it facilitates ATP-dependent chromatin remodeling,” Molecular and Cellular Biology, vol. 27, no. 1, pp. 384–394, 2007. View at Publisher · View at Google Scholar · View at Scopus
  88. M. P. Bevilacqua, S. Stengelin, M. A. Gimbrone Jr., and B. Seed, “Endothelial leukocyte adhesion molecule 1: an inducible receptor for neutrophils related to complement regulatory proteins and lectins,” Science, vol. 243, no. 4895, pp. 1160–1165, 1989. View at Publisher · View at Google Scholar · View at Scopus
  89. L. C. Edelstein, A. Pan, and T. Collins, “Chromatin modification and the endothelial-specific activation of the E-selectin gene,” The Journal of Biological Chemistry, vol. 280, no. 12, pp. 11192–11202, 2005. View at Publisher · View at Google Scholar · View at Scopus
  90. S. Bandyopadhyay, M. Z. Ashraf, P. Daher, P. H. Howe, and P. E. DiCorleto, “HOXA9 participates in the transcriptional activation of E-selectin in endothelial cells,” Molecular and Cellular Biology, vol. 27, no. 12, pp. 4207–4216, 2007. View at Publisher · View at Google Scholar · View at Scopus
  91. U. Vijapurkar, N. Fischbach, W. Shen et al., “Protein kinase C-mediated phosphorylation of the leukemia-associated HOXA9 protein impairs its DNA binding ability and induces myeloid differentiation,” Molecular and Cellular Biology, vol. 24, no. 9, pp. 3827–3837, 2004. View at Publisher · View at Google Scholar · View at Scopus
  92. S. Bandyopadhyay, D. P. Harris, G. N. Adams et al., “HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules,” Molecular and Cellular Biology, vol. 32, no. 7, pp. 1202–1213, 2012. View at Publisher · View at Google Scholar · View at Scopus
  93. Q. Zhao, G. Rank, Y. T. Tan et al., “PRMT5-mediated methylation of histone H4R3 recruits DNMT3A, coupling histone and DNA methylation in gene silencing,” Nature Structural & Molecular Biology, vol. 16, no. 3, pp. 304–311, 2009. View at Publisher · View at Google Scholar · View at Scopus
  94. H. Tanaka, Y. Hoshikawa, T. Oh-hara et al., “PRMT5, a novel TRAIL receptor-binding protein, inhibits TRAIL-induced apoptosis via nuclear factor-κB activation,” Molecular Cancer Research, vol. 7, no. 4, pp. 557–569, 2009. View at Publisher · View at Google Scholar · View at Scopus
  95. D. Wang, D. Liu, J. Gao et al., “PRMT5 suppresses DR4-mediated CCL20 release via NF-κB pathway,” Chinese Science Bulletin, vol. 57, no. 33, pp. 4351–4355, 2012. View at Publisher · View at Google Scholar · View at Scopus
  96. H. Wei, B. Wang, M. Miyagi et al., “PRMT5 dimethylates R30 of the p65 subunit to activate NF-κB,” Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 33, pp. 13516–13521, 2013. View at Publisher · View at Google Scholar · View at Scopus
  97. D. P. Harris, S. Bandyopadhyay, T. J. Maxwell, B. Willard, and P. E. DiCorleto, “Tumor necrosis factor (TNF)-α induction of CXCL10 in endothelial cells requires protein arginine methyltransferase 5 (PRMT5)-mediated nuclear factor (NF)-κB p65 Methylation,” The Journal of Biological Chemistry, vol. 289, no. 22, pp. 15328–15339, 2014. View at Publisher · View at Google Scholar · View at Scopus
  98. Y. Yang and M. T. Bedford, “Protein arginine methyltransferases and cancer,” Nature Reviews Cancer, vol. 13, no. 1, pp. 37–50, 2013. View at Publisher · View at Google Scholar · View at Scopus
  99. R. Métivier, G. Penot, M. R. Hübner et al., “Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter,” Cell, vol. 115, no. 6, pp. 751–763, 2003. View at Publisher · View at Google Scholar · View at Scopus
  100. M. Le Romancer, I. Treilleux, N. Leconte et al., “Regulation of estrogen rapid signaling through arginine methylation by PRMT1,” Molecular Cell, vol. 31, no. 2, pp. 212–221, 2008. View at Publisher · View at Google Scholar · View at Scopus
  101. B. Chang, Y. Chen, Y. Zhao, and R. K. Bruick, “JMJD6 is a histone arginine demethylase,” Science, vol. 318, no. 5849, pp. 444–447, 2007. View at Publisher · View at Google Scholar · View at Scopus