36. Jeong S-J et al (2006) Coactivator-associated arginine methyltransferase 1 enhances transcriptional activity of the human T-cell Lymphotropic virus type 1 long terminal repeat through
direct interaction with tax. J Virol 80:10036–10044
37. Xie B et al (2007) Arginine methylation of the human immunodeficiency virus type 1 tat
protein by PRMT6 negatively affects tat interactions with both cyclin T1 and the tat
transactivation region. J Virol 81:4226–4234
38. Alinari L et al (2015) Selective inhibition of protein arginine methyltransferase 5 blocks
initiation and maintenance of B-cell transformation. Blood 125:2530–2543
39. Cheng D et al (2004) Small molecule regulators of protein arginine methyltransferases. J Biol
Chem 279:23892–23899
40. Peng C, Wong CC (2017) The story of protein arginine methylation: characterization, regulation, and function. Expert Rev Proteomics 14:157–170
41. Kaniskan HÜ et al (2017) Inhibitors of protein methyltransferases and demethylases. Chem
Rev 118:989–1068
42. Blanc RS, Richard S (2017) Arginine methylation: the coming of age. Mol Cell 65:8–24
43. Morettin A et al (2015) Arginine methyltransferases as novel therapeutic targets for breast
cancer. Mutagenesis 30:177–189
44. Boriack-Sjodin PA, Swinger KK (2016) Protein methyltransferases: a distinct, diverse, and
dynamic family of enzymes. Biochemistry 55:1557–1569
45. Schapira M, Ferreira de Freitas R (2014) Structural biology and chemistry of protein arginine
methyltransferases. Med Chem Commun 5:1779–1788
46. Scheer S et al (2019) A chemical biology toolbox to study protein methyltransferases and
epigenetic signaling. Nat Commun 10:19
47. Kryukov GV et al (2016) MTAP deletion confers enhanced dependency on the PRMT5
arginine methyltransferase in cancer cells. Science 351:1214–1218
48. Marjon K et al (2016) MTAP deletions in cancer create vulnerability to targeting of the
MAT2A/PRMT5/RIOK1 axis. Cell Rep 15:574–587
49. Mavrakis KJ et al (2016) Disordered methionine metabolism in MTAP/CDKN2A-deleted
cancers leads to dependence on PRMT5. Science 351:1208–1213
50. Eram MS et al (2016) A potent, selective, and cell-active inhibitor of human type I protein
arginine methyltransferases. ACS Chem Biol 11:772–781
51. Tang J et al (2000) Protein-arginine methyltransferase I, the predominant protein-arginine
methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding
factor 3. J Biol Chem 275:19866–19876
52. Tang J et al (2000) PRMT1 is the predominant type I protein arginine methyltransferase in
mammalian cells. J Biol Chem 275:7723–7730
53. Goulet I et al (2007) Alternative splicing yields protein arginine methyltransferase 1 isoforms
with distinct activity, substrate specificity, and subcellular localization. J Biol Chem
282:33009–33021
54. Dhar S et al (2013) Loss of the major type I arginine methyltransferase PRMT1 causes
substrate scavenging by other PRMTs. Sci Rep 3:1311
55. Wooderchak WL et al (2008) Substrate profiling of PRMT1 reveals amino acid sequences that
extend beyond the “RGG” paradigm. Biochemistry 47:9456–9466
56. Wei H et al (2014) Protein arginine methylation of non-histone proteins and its role in diseases.
Cell Cycle 13:32–41
57. Baldwin RM et al (2012) Alternatively spliced protein arginine methyltransferase 1 isoform
PRMT1v2 promotes the survival and invasiveness of breast cancer cells. Cell Cycle
11:4597–4612
58. Seligson DB et al (2005) Global histone modification patterns predict risk of prostate cancer
recurrence. Nature 435:1262–1266
59. Avasarala S et al (2015) PRMT1 is a novel regulator of epithelial-mesenchymal-transition in
non-small cell lung cancer. J Biol Chem 290:13479–13489
190
M. J. van Haren and N. I. Martin
direct interaction with tax. J Virol 80:10036–10044
37. Xie B et al (2007) Arginine methylation of the human immunodeficiency virus type 1 tat
protein by PRMT6 negatively affects tat interactions with both cyclin T1 and the tat
transactivation region. J Virol 81:4226–4234
38. Alinari L et al (2015) Selective inhibition of protein arginine methyltransferase 5 blocks
initiation and maintenance of B-cell transformation. Blood 125:2530–2543
39. Cheng D et al (2004) Small molecule regulators of protein arginine methyltransferases. J Biol
Chem 279:23892–23899
40. Peng C, Wong CC (2017) The story of protein arginine methylation: characterization, regulation, and function. Expert Rev Proteomics 14:157–170
41. Kaniskan HÜ et al (2017) Inhibitors of protein methyltransferases and demethylases. Chem
Rev 118:989–1068
42. Blanc RS, Richard S (2017) Arginine methylation: the coming of age. Mol Cell 65:8–24
43. Morettin A et al (2015) Arginine methyltransferases as novel therapeutic targets for breast
cancer. Mutagenesis 30:177–189
44. Boriack-Sjodin PA, Swinger KK (2016) Protein methyltransferases: a distinct, diverse, and
dynamic family of enzymes. Biochemistry 55:1557–1569
45. Schapira M, Ferreira de Freitas R (2014) Structural biology and chemistry of protein arginine
methyltransferases. Med Chem Commun 5:1779–1788
46. Scheer S et al (2019) A chemical biology toolbox to study protein methyltransferases and
epigenetic signaling. Nat Commun 10:19
47. Kryukov GV et al (2016) MTAP deletion confers enhanced dependency on the PRMT5
arginine methyltransferase in cancer cells. Science 351:1214–1218
48. Marjon K et al (2016) MTAP deletions in cancer create vulnerability to targeting of the
MAT2A/PRMT5/RIOK1 axis. Cell Rep 15:574–587
49. Mavrakis KJ et al (2016) Disordered methionine metabolism in MTAP/CDKN2A-deleted
cancers leads to dependence on PRMT5. Science 351:1208–1213
50. Eram MS et al (2016) A potent, selective, and cell-active inhibitor of human type I protein
arginine methyltransferases. ACS Chem Biol 11:772–781
51. Tang J et al (2000) Protein-arginine methyltransferase I, the predominant protein-arginine
methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding
factor 3. J Biol Chem 275:19866–19876
52. Tang J et al (2000) PRMT1 is the predominant type I protein arginine methyltransferase in
mammalian cells. J Biol Chem 275:7723–7730
53. Goulet I et al (2007) Alternative splicing yields protein arginine methyltransferase 1 isoforms
with distinct activity, substrate specificity, and subcellular localization. J Biol Chem
282:33009–33021
54. Dhar S et al (2013) Loss of the major type I arginine methyltransferase PRMT1 causes
substrate scavenging by other PRMTs. Sci Rep 3:1311
55. Wooderchak WL et al (2008) Substrate profiling of PRMT1 reveals amino acid sequences that
extend beyond the “RGG” paradigm. Biochemistry 47:9456–9466
56. Wei H et al (2014) Protein arginine methylation of non-histone proteins and its role in diseases.
Cell Cycle 13:32–41
57. Baldwin RM et al (2012) Alternatively spliced protein arginine methyltransferase 1 isoform
PRMT1v2 promotes the survival and invasiveness of breast cancer cells. Cell Cycle
11:4597–4612
58. Seligson DB et al (2005) Global histone modification patterns predict risk of prostate cancer
recurrence. Nature 435:1262–1266
59. Avasarala S et al (2015) PRMT1 is a novel regulator of epithelial-mesenchymal-transition in
non-small cell lung cancer. J Biol Chem 290:13479–13489
190
M. J. van Haren and N. I. Martin