메뉴 건너뛰기




Volumn 39, Issue 5, 2012, Pages 195-208

Plant PRMTs Broaden the Scope of Arginine Methylation

Author keywords

Arginine methylation; Post translational modifications; PRMTs

Indexed keywords

6 N,N' DIMETHYLARGININE; ARGININE; JANUS KINASE 2; METHIONINE; N(G),N(G) DIMETHYLARGININE; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 1; PROTEIN ARGININE METHYLTRANSFERASE 10; PROTEIN ARGININE METHYLTRANSFERASE 11; PROTEIN ARGININE METHYLTRANSFERASE 2; PROTEIN ARGININE METHYLTRANSFERASE 3; PROTEIN ARGININE METHYLTRANSFERASE 4; PROTEIN ARGININE METHYLTRANSFERASE 6; PROTEIN ARGININE METHYLTRANSFERASE 7; PROTEIN ARGININE METHYLTRANSFERASE 8; PROTEIN ARGININE METHYLTRANSFERASE 9; SMAD1 PROTEIN; SMAD3 PROTEIN; UNCLASSIFIED DRUG;

EID: 84861343081     PISSN: 16738527     EISSN: 18735533     Source Type: Journal    
DOI: 10.1016/j.jgg.2012.04.001     Document Type: Review
Times cited : (50)

References (123)
  • 1
    • 77955152008 scopus 로고    scopus 로고
    • Decoding the epigenetic language of plant development
    • Ahmad A., Zhang Y., Cao X.F. Decoding the epigenetic language of plant development. Mol. Plant 2010, 3:719-728.
    • (2010) Mol. Plant , vol.3 , pp. 719-728
    • Ahmad, A.1    Zhang, Y.2    Cao, X.F.3
  • 2
    • 80051636584 scopus 로고    scopus 로고
    • Characterization of the PRMT gene family in rice reveals conservation of arginine methylation
    • Ahmad A., Dong Y., Cao X. Characterization of the PRMT gene family in rice reveals conservation of arginine methylation. PloS One 2011, 6:e22664.
    • (2011) PloS One , vol.6
    • Ahmad, A.1    Dong, Y.2    Cao, X.3
  • 3
    • 77956206633 scopus 로고    scopus 로고
    • Arginine methylation of SmB is required for Drosophila germ cell development
    • Anne J. Arginine methylation of SmB is required for Drosophila germ cell development. Development 2010, 137:2819-2828.
    • (2010) Development , vol.137 , pp. 2819-2828
    • Anne, J.1
  • 4
    • 3342936604 scopus 로고    scopus 로고
    • PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits
    • Bachand F., Silver P.A. PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits. EMBO J. 2004, 23:2641-2650.
    • (2004) EMBO J. , vol.23 , pp. 2641-2650
    • Bachand, F.1    Silver, P.A.2
  • 5
    • 34250859489 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: from unicellular eukaryotes to humans
    • Bachand F. Protein arginine methyltransferases: from unicellular eukaryotes to humans. Eukaryot. Cell 2007, 6:889-898.
    • (2007) Eukaryot. Cell , vol.6 , pp. 889-898
    • Bachand, F.1
  • 6
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister A.J., Kouzarides T. Regulation of chromatin by histone modifications. Cell Res. 2011, 21:381-395.
    • (2011) Cell Res. , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 8
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: who, what, and why
    • Bedford M.T., Clarke S.G. Protein arginine methylation in mammals: who, what, and why. Mol. Cell 2009, 33:1-13.
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 9
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation: an emerging regulator of protein function
    • Bedford M.T., Richard S. Arginine methylation: an emerging regulator of protein function. Mol. Cell 2005, 18:263-272.
    • (2005) Mol. Cell , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 10
    • 84857195774 scopus 로고    scopus 로고
    • Arginine methylation of RNA-binding proteins regulates cell function and differentiation
    • Blackwell E., Ceman S. Arginine methylation of RNA-binding proteins regulates cell function and differentiation. Mol. Reprod. Dev. 2011, 79:163-175.
    • (2011) Mol. Reprod. Dev. , vol.79 , pp. 163-175
    • Blackwell, E.1    Ceman, S.2
  • 11
    • 77955587632 scopus 로고    scopus 로고
    • [Beta]-catenin primes organizer gene expression by recruiting a histone H3 arginine 8 methyltransferase, Prmt2
    • Blythe S.A., Cha S.W., Tadjuidje E., Heasman J., Klein P.S. [Beta]-catenin primes organizer gene expression by recruiting a histone H3 arginine 8 methyltransferase, Prmt2. Dev. Cell 2010, 19:220-231.
    • (2010) Dev. Cell , vol.19 , pp. 220-231
    • Blythe, S.A.1    Cha, S.W.2    Tadjuidje, E.3    Heasman, J.4    Klein, P.S.5
  • 12
    • 0035980018 scopus 로고    scopus 로고
    • PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
    • Branscombe T.L., Frankel A., Lee J.H., Cook J.R., Yang Z., Pestka S., Clarke S. PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. J. Biol. Chem. 2001, 276:32971-32976.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32971-32976
    • Branscombe, T.L.1    Frankel, A.2    Lee, J.H.3    Cook, J.R.4    Yang, Z.5    Pestka, S.6    Clarke, S.7
  • 14
    • 69449093950 scopus 로고    scopus 로고
    • A role for the ribosome in development
    • Byrne M.E. A role for the ribosome in development. Trends Plant Sci. 2009, 14:512-519.
    • (2009) Trends Plant Sci. , vol.14 , pp. 512-519
    • Byrne, M.E.1
  • 16
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 is a histone arginine demethylase
    • Chang B., Chen Y., Zhao Y., Bruick R.K. JMJD6 is a histone arginine demethylase. Science 2007, 318:444-447.
    • (2007) Science , vol.318 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 19
    • 20544461679 scopus 로고    scopus 로고
    • Structural and sequence motifs of protein (histone) methylation enzymes. Annu. Rev. Biophy. Biomol
    • Cheng X., Collins R.E., Zhang X. Structural and sequence motifs of protein (histone) methylation enzymes. Annu. Rev. Biophy. Biomol. Struct 2005, 34:267-294.
    • (2005) Struct , vol.34 , pp. 267-294
    • Cheng, X.1    Collins, R.E.2    Zhang, X.3
  • 20
    • 33846001366 scopus 로고    scopus 로고
    • The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing
    • Cheng D., Cote J., Shaaban S., Bedford M.T. The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing. Mol. Cell 2007, 25:71-83.
    • (2007) Mol. Cell , vol.25 , pp. 71-83
    • Cheng, D.1    Cote, J.2    Shaaban, S.3    Bedford, M.T.4
  • 21
    • 81055156654 scopus 로고    scopus 로고
    • Crystal structure of the plant epigenetic protein arginine methyltransferase 10
    • Cheng Y., Frazier M., Lu F., Cao X., Redinbo M.R. Crystal structure of the plant epigenetic protein arginine methyltransferase 10. J. Mol. Biol. 2011, 414:106-122.
    • (2011) J. Mol. Biol. , vol.414 , pp. 106-122
    • Cheng, Y.1    Frazier, M.2    Lu, F.3    Cao, X.4    Redinbo, M.R.5
  • 22
    • 0037107417 scopus 로고    scopus 로고
    • Control of CBP co-activating activity by arginine methylation
    • Chevillard-Briet M., Trouche D., Vandel L. Control of CBP co-activating activity by arginine methylation. EMBO J. 2002, 21:5457-5466.
    • (2002) EMBO J. , vol.21 , pp. 5457-5466
    • Chevillard-Briet, M.1    Trouche, D.2    Vandel, L.3
  • 23
    • 47049083398 scopus 로고    scopus 로고
    • PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex
    • Choi S., Jung C.R., Kim J.Y., Im D.S. PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex. Biochim. Biophys. Acta 2008, 1780:1062-1069.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1062-1069
    • Choi, S.1    Jung, C.R.2    Kim, J.Y.3    Im, D.S.4
  • 26
    • 80555154796 scopus 로고    scopus 로고
    • Prmt2 regulates the lipopolysaccharide-induced responses in lungs and macrophages
    • Dalloneau E., Pereira P.L., Brault V., Nabel E.G., Hérault Y. Prmt2 regulates the lipopolysaccharide-induced responses in lungs and macrophages. J. Immunol. 2011, 187:4826-4834.
    • (2011) J. Immunol. , vol.187 , pp. 4826-4834
    • Dalloneau, E.1    Pereira, P.L.2    Brault, V.3    Nabel, E.G.4    Hérault, Y.5
  • 27
    • 78650488766 scopus 로고    scopus 로고
    • Arginine methylation mediated by the Arabidopsis homolog of PRMT5 is essential for proper pre-mRNA splicing
    • Deng X., Gu L., Liu C., Lu T., Lu F., Lu Z., Cui P., Pei Y., Wang B., Hu S. Arginine methylation mediated by the Arabidopsis homolog of PRMT5 is essential for proper pre-mRNA splicing. Proc. Natl. Acad. Sci. USA 2010, 107:19114-19119.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 19114-19119
    • Deng, X.1    Gu, L.2    Liu, C.3    Lu, T.4    Lu, F.5    Lu, Z.6    Cui, P.7    Pei, Y.8    Wang, B.9    Hu, S.10
  • 28
    • 79959829510 scopus 로고    scopus 로고
    • Histone arginine methylation
    • Di Lorenzo A., Bedford M.T. Histone arginine methylation. FEBS Lett. 2010, 585:2024-2031.
    • (2010) FEBS Lett. , vol.585 , pp. 2024-2031
    • Di Lorenzo, A.1    Bedford, M.T.2
  • 30
    • 84859222354 scopus 로고    scopus 로고
    • The methylproteome and the intracellular methylation network
    • Erce M.A., Pang C.N.I., Hart-Smith G., Wilkins M.R. The methylproteome and the intracellular methylation network. Proteomics 2012, 12:1-23.
    • (2012) Proteomics , vol.12 , pp. 1-23
    • Erce, M.A.1    Pang, C.N.I.2    Hart-Smith, G.3    Wilkins, M.R.4
  • 33
    • 0036479327 scopus 로고    scopus 로고
    • The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
    • Frankel A., Yadav N., Lee J., Branscombe T.L., Clarke S., Bedford M.T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 2002, 277:3537-3543.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3537-3543
    • Frankel, A.1    Yadav, N.2    Lee, J.3    Branscombe, T.L.4    Clarke, S.5    Bedford, M.T.6
  • 34
    • 0035947239 scopus 로고    scopus 로고
    • SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets
    • Friesen W.J., Massenet S., Paushkin S., Wyce A., Dreyfuss G. SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol. Cell 2001, 7:1111-1117.
    • (2001) Mol. Cell , vol.7 , pp. 1111-1117
    • Friesen, W.J.1    Massenet, S.2    Paushkin, S.3    Wyce, A.4    Dreyfuss, G.5
  • 37
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein arginine methylation
    • Gary J.D., Clarke S. RNA and protein interactions modulated by protein arginine methylation. Prog. Nucleic Acid Res. Mol. Biol. 1998, 61:65-131.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 38
    • 34548356376 scopus 로고    scopus 로고
    • Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins
    • Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.M., Lamond A.I., Matera A.G. Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J. Biol. Chem. 2007, 178:733-740.
    • (2007) J. Biol. Chem. , vol.178 , pp. 733-740
    • Gonsalvez, G.B.1    Tian, L.2    Ospina, J.K.3    Boisvert, F.M.4    Lamond, A.I.5    Matera, A.G.6
  • 41
    • 77956271553 scopus 로고    scopus 로고
    • Structural basis for methylarginine-dependent recognition of Aubergine by Tudor
    • Haiping L., Wang J.Y.S., Huang Y., Li Z., Gong W., Lehmann R., Xu R.M. Structural basis for methylarginine-dependent recognition of Aubergine by Tudor. Genes Dev. 2010, 24:1876-1881.
    • (2010) Genes Dev. , vol.24 , pp. 1876-1881
    • Haiping, L.1    Wang, J.Y.S.2    Huang, Y.3    Li, Z.4    Gong, W.5    Lehmann, R.6    Xu, R.M.7
  • 42
    • 78649764498 scopus 로고    scopus 로고
    • Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)
    • Handrkova H., Petrak J., Halada P., Pospisilova D., Cmejla R. Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3). Biochim. Biophys. Acta 2011, 1814:277-282.
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 277-282
    • Handrkova, H.1    Petrak, J.2    Halada, P.3    Pospisilova, D.4    Cmejla, R.5
  • 43
    • 77952310684 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 6 regulates multiple aspects of gene expression
    • Harrison M.J., Tang Y.H., Dowhan D.H. Protein arginine methyltransferase 6 regulates multiple aspects of gene expression. Nucleic Acids Res. 2010, 38:2201-2216.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 2201-2216
    • Harrison, M.J.1    Tang, Y.H.2    Dowhan, D.H.3
  • 44
    • 27844433569 scopus 로고    scopus 로고
    • Dynamics of human protein arginine methyltransferase 1 (PRMT1) in vivo
    • Herrmann F., Lee J., Bedford M.T., Fackelmayer F.O. Dynamics of human protein arginine methyltransferase 1 (PRMT1) in vivo. J. Biol. Chem. 2005, 280:38005-38010.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38005-38010
    • Herrmann, F.1    Lee, J.2    Bedford, M.T.3    Fackelmayer, F.O.4
  • 45
    • 66149108467 scopus 로고    scopus 로고
    • Human protein arginine methyltransferases in vivo-distinct properties of eight canonical members of the PRMT family
    • Herrmann F., Pably P., Eckerich C., Bedford M.T., Fackelmayer F.O. Human protein arginine methyltransferases in vivo-distinct properties of eight canonical members of the PRMT family. J. Cell Sci. 2009, 122:667-677.
    • (2009) J. Cell Sci. , vol.122 , pp. 667-677
    • Herrmann, F.1    Pably, P.2    Eckerich, C.3    Bedford, M.T.4    Fackelmayer, F.O.5
  • 46
    • 78650446132 scopus 로고    scopus 로고
    • Type II protein arginine methyltransferase 5 (PRMT5) is required for circadian period determination in Arabidopsis thaliana
    • Hong S., Song H.R., Lutz K., Kerstetter R.A., Michael T.P., McClung C.R. Type II protein arginine methyltransferase 5 (PRMT5) is required for circadian period determination in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 2010, 107:21211-21216.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 21211-21216
    • Hong, S.1    Song, H.R.2    Lutz, K.3    Kerstetter, R.A.4    Michael, T.P.5    McClung, C.R.6
  • 48
    • 33846708629 scopus 로고    scopus 로고
    • PRMT6 diminishes HIV-1 Rev binding to and export of viral RNA
    • Invernizzi C., Xie B., Richard S., Wainberg M. PRMT6 diminishes HIV-1 Rev binding to and export of viral RNA. Retrovirology 2006, 3:93.
    • (2006) Retrovirology , vol.3 , pp. 93
    • Invernizzi, C.1    Xie, B.2    Richard, S.3    Wainberg, M.4
  • 50
    • 77958471611 scopus 로고    scopus 로고
    • Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation
    • Iwasaki H., Kovacic J.C., Olive M., Beers J.K., Yoshimoto T., Crook M.F., Tonelli L.H., Nabel E.G. Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation. Circ. Res. 2010, 107:992-1001.
    • (2010) Circ. Res. , vol.107 , pp. 992-1001
    • Iwasaki, H.1    Kovacic, J.C.2    Olive, M.3    Beers, J.K.4    Yoshimoto, T.5    Crook, M.F.6    Tonelli, L.H.7    Nabel, E.G.8
  • 51
    • 33751029979 scopus 로고    scopus 로고
    • The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation
    • Jelinic P., Stehle J.C., Shaw P. The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation. PLoS Biol. 2006, 4:e355.
    • (2006) PLoS Biol. , vol.4
    • Jelinic, P.1    Stehle, J.C.2    Shaw, P.3
  • 52
    • 53049097189 scopus 로고    scopus 로고
    • EWS is a substrate of type I protein arginine methyltransferase, PRMT8
    • Kim J.D., Kako K., Kakiuchi M., Park G.G., Fukamizu A. EWS is a substrate of type I protein arginine methyltransferase, PRMT8. Int. J. Mol. Med. 2008, 22:309-315.
    • (2008) Int. J. Mol. Med. , vol.22 , pp. 309-315
    • Kim, J.D.1    Kako, K.2    Kakiuchi, M.3    Park, G.G.4    Fukamizu, A.5
  • 54
    • 33845896853 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential
    • Krause C.D., Yang Z.H., Kim Y.S., Lee J.H., Cook J.R., Pestka S. Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential. Pharmacol. Ther. 2007, 113:50-87.
    • (2007) Pharmacol. Ther. , vol.113 , pp. 50-87
    • Krause, C.D.1    Yang, Z.H.2    Kim, Y.S.3    Lee, J.H.4    Cook, J.R.5    Pestka, S.6
  • 55
    • 79954611535 scopus 로고    scopus 로고
    • Automethylation of CARM1 allows coupling of transcription and mRNA splicing
    • Kuhn P., Chumanov R., Wang Y., Ge Y., Burgess R.R., Xu W. Automethylation of CARM1 allows coupling of transcription and mRNA splicing. Nucleic Acids Res. 2011, 39:2717-2726.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2717-2726
    • Kuhn, P.1    Chumanov, R.2    Wang, Y.3    Ge, Y.4    Burgess, R.R.5    Xu, W.6
  • 56
    • 0037623333 scopus 로고    scopus 로고
    • Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties
    • Kwak Y.T., Guo J., Prajapati S., Park K.J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B. Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Mol. Cell 2003, 11:1055-1066.
    • (2003) Mol. Cell , vol.11 , pp. 1055-1066
    • Kwak, Y.T.1    Guo, J.2    Prajapati, S.3    Park, K.J.4    Surabhi, R.M.5    Miller, B.6    Gehrig, P.7    Gaynor, R.B.8
  • 58
    • 34147095806 scopus 로고    scopus 로고
    • Protein methylation and DNA repair
    • Lake A.N., Bedford M.T. Protein methylation and DNA repair. Mutat. Res. 2007, 618:91-101.
    • (2007) Mutat. Res. , vol.618 , pp. 91-101
    • Lake, A.N.1    Bedford, M.T.2
  • 59
    • 25444463928 scopus 로고    scopus 로고
    • PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family
    • Lee J., Sayegh J., Daniel J., Clarke S., Bedford M.T. PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J. Biol. Chem. 2005, 280:32890-32896.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32890-32896
    • Lee, J.1    Sayegh, J.2    Daniel, J.3    Clarke, S.4    Bedford, M.T.5
  • 60
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
    • Lin W.J., Gary J.D., Yang M.C., Clarke S., Herschman H.R. The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J. Biol. Chem. 1996, 271:15034-15044.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15034-15044
    • Lin, W.J.1    Gary, J.D.2    Yang, M.C.3    Clarke, S.4    Herschman, H.R.5
  • 63
    • 80053064868 scopus 로고    scopus 로고
    • Conserved arginine residue in the membrane-spanning domain of HIV-1 gp41 is required for efficient membrane fusion
    • Long Y., Meng F., Kondo N., Iwamoto A., Matsuda Z. Conserved arginine residue in the membrane-spanning domain of HIV-1 gp41 is required for efficient membrane fusion. Protein Cell 2011, 2:369-376.
    • (2011) Protein Cell , vol.2 , pp. 369-376
    • Long, Y.1    Meng, F.2    Kondo, N.3    Iwamoto, A.4    Matsuda, Z.5
  • 64
    • 0034634395 scopus 로고    scopus 로고
    • The evolutionary fate and consequences of duplicate genes
    • Lynch M., Conery J.S. The evolutionary fate and consequences of duplicate genes. Science 2000, 290:1151-1155.
    • (2000) Science , vol.290 , pp. 1151-1155
    • Lynch, M.1    Conery, J.S.2
  • 66
    • 0036845335 scopus 로고    scopus 로고
    • Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs
    • Meister G., Fischer U. Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs. EMBO J. 2002, 21:5853-5863.
    • (2002) EMBO J. , vol.21 , pp. 5853-5863
    • Meister, G.1    Fischer, U.2
  • 67
    • 34548452082 scopus 로고    scopus 로고
    • PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor
    • Meyer R., Wolf S.S., Obendorf M. PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor. J. Steroid Biochem. Mol. Biol. 2007, 107:1-14.
    • (2007) J. Steroid Biochem. Mol. Biol. , vol.107 , pp. 1-14
    • Meyer, R.1    Wolf, S.S.2    Obendorf, M.3
  • 68
    • 0033133554 scopus 로고    scopus 로고
    • FLOWERING LOCUS C encodes a novel MADS domain protein that acts as a repressor of flowering
    • Michaels S.D., Amasino R.M. FLOWERING LOCUS C encodes a novel MADS domain protein that acts as a repressor of flowering. Plant Cell 1999, 11:949-956.
    • (1999) Plant Cell , vol.11 , pp. 949-956
    • Michaels, S.D.1    Amasino, R.M.2
  • 69
    • 2542429259 scopus 로고    scopus 로고
    • PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity
    • Miranda T.B., Miranda M., Frankel A., Clarke S. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J. Biol. Chem. 2004, 279:22902-22907.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22902-22907
    • Miranda, T.B.1    Miranda, M.2    Frankel, A.3    Clarke, S.4
  • 70
    • 4344629701 scopus 로고    scopus 로고
    • Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes
    • Mowen K.A., Schurter B.T., Fathman J.W., David M., Glimcher L.H. Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes. Mol. Cell 2004, 15:559-571.
    • (2004) Mol. Cell , vol.15 , pp. 559-571
    • Mowen, K.A.1    Schurter, B.T.2    Fathman, J.W.3    David, M.4    Glimcher, L.H.5
  • 72
    • 36749068882 scopus 로고    scopus 로고
    • Regulation of flowering time by the protein arginine methyltransferase AtPRMT10
    • Niu L., Lu F., Pei Y., Liu C., Cao X. Regulation of flowering time by the protein arginine methyltransferase AtPRMT10. EMBO Rep. 2007, 8:1190-1195.
    • (2007) EMBO Rep. , vol.8 , pp. 1190-1195
    • Niu, L.1    Lu, F.2    Pei, Y.3    Liu, C.4    Cao, X.5
  • 73
    • 55549123195 scopus 로고    scopus 로고
    • Redundant requirement for a pair of PROTEIN ARGININE METHYLTRANSFERASE4 homologs for the proper regulation of Arabidopsis flowering time
    • Niu L., Zhang Y., Pei Y., Liu C., Cao X. Redundant requirement for a pair of PROTEIN ARGININE METHYLTRANSFERASE4 homologs for the proper regulation of Arabidopsis flowering time. Plant Physiol. 2008, 148:490-503.
    • (2008) Plant Physiol. , vol.148 , pp. 490-503
    • Niu, L.1    Zhang, Y.2    Pei, Y.3    Liu, C.4    Cao, X.5
  • 75
    • 23844435269 scopus 로고    scopus 로고
    • Coactivator-associated arginine methyltransferase 1, CARM1, affects pre-mRNA splicing in an isoform-specific manner
    • Ohkura N., Takahashi M., Yaguchi H., Nagamura Y., Tsukada T. Coactivator-associated arginine methyltransferase 1, CARM1, affects pre-mRNA splicing in an isoform-specific manner. J. Biol. Chem. 2005, 280:28927-28935.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28927-28935
    • Ohkura, N.1    Takahashi, M.2    Yaguchi, H.3    Nagamura, Y.4    Tsukada, T.5
  • 76
    • 33845418030 scopus 로고    scopus 로고
    • Protein arginine methylation: cellular functions and methods of analysis
    • Pahlich S., Zakaryan R.P., Gehring H. Protein arginine methylation: cellular functions and methods of analysis. Biochim. Biophys. Acta 2006, 1764:1890-1903.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1890-1903
    • Pahlich, S.1    Zakaryan, R.P.2    Gehring, H.3
  • 77
    • 51349117212 scopus 로고    scopus 로고
    • Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state
    • Pahlich S., Zakaryan R.P., Gehring H. Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state. Proteins 2008, 72:1125-1137.
    • (2008) Proteins , vol.72 , pp. 1125-1137
    • Pahlich, S.1    Zakaryan, R.P.2    Gehring, H.3
  • 78
    • 33847678615 scopus 로고    scopus 로고
    • Historical review: the field of protein methylation
    • Paik W.K., Paik D.C., Kim S. Historical review: the field of protein methylation. Trends Biochem. Sci. 2007, 32:146-152.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 146-152
    • Paik, W.K.1    Paik, D.C.2    Kim, S.3
  • 79
    • 80053009662 scopus 로고    scopus 로고
    • A protein arginine N-methyltransferase 1 and 2 heteromeric interaction increases PRMT1 enzymatic activity
    • Pak M.L., Lakowski T.M., Thomas D., Vhuiyan M.I., Hüsecken K., Frankel A. A protein arginine N-methyltransferase 1 and 2 heteromeric interaction increases PRMT1 enzymatic activity. Biochemistry 2011, 50:8226-8240.
    • (2011) Biochemistry , vol.50 , pp. 8226-8240
    • Pak, M.L.1    Lakowski, T.M.2    Thomas, D.3    Vhuiyan, M.I.4    Hüsecken, K.5    Frankel, A.6
  • 80
    • 6344222803 scopus 로고    scopus 로고
    • Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes
    • Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S. Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol. Cell. Biol. 2004, 24:9630-9645.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9630-9645
    • Pal, S.1    Vishwanath, S.N.2    Erdjument-Bromage, H.3    Tempst, P.4    Sif, S.5
  • 81
    • 0034045559 scopus 로고    scopus 로고
    • Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable
    • Pawlak M.R., Scherer C.A., Chen J., Roshon M.J., Ruley H.E. Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable. Mol. Cell. Biol. 2000, 20:4859-4869.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4859-4869
    • Pawlak, M.R.1    Scherer, C.A.2    Chen, J.3    Roshon, M.J.4    Ruley, H.E.5
  • 82
    • 34547881914 scopus 로고    scopus 로고
    • Mutations in the Type II protein arginine methyltransferase AtPRMT5 result in pleiotropic developmental defects in Arabidopsis
    • Pei Y., Niu L., Lu F., Liu C., Zhai J., Kong X., Cao X. Mutations in the Type II protein arginine methyltransferase AtPRMT5 result in pleiotropic developmental defects in Arabidopsis. Plant Physiol. 2007, 144:1913-1923.
    • (2007) Plant Physiol. , vol.144 , pp. 1913-1923
    • Pei, Y.1    Niu, L.2    Lu, F.3    Liu, C.4    Zhai, J.5    Kong, X.6    Cao, X.7
  • 83
    • 67649359948 scopus 로고    scopus 로고
    • A methyltransferase-independent function for Rmt3 in ribosomal subunit homeostasis
    • Perreault A., Gascon S., D'Amours A., Aletta J.M., Bachand F. A methyltransferase-independent function for Rmt3 in ribosomal subunit homeostasis. J. Biol. Chem. 2009, 284:15026-15037.
    • (2009) J. Biol. Chem. , vol.284 , pp. 15026-15037
    • Perreault, A.1    Gascon, S.2    D'Amours, A.3    Aletta, J.M.4    Bachand, F.5
  • 84
    • 0033615656 scopus 로고    scopus 로고
    • The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity
    • Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S. The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. J. Biol. Chem. 1999, 274:31531-31542.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31531-31542
    • Pollack, B.P.1    Kotenko, S.V.2    He, W.3    Izotova, L.S.4    Barnoski, B.L.5    Pestka, S.6
  • 85
    • 0037047399 scopus 로고    scopus 로고
    • Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor α
    • Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.J. Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor α. J. Biol. Chem. 2002, 277:28624-28630.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28624-28630
    • Qi, C.1    Chang, J.2    Zhu, Y.3    Yeldandi, A.V.4    Rao, S.M.5    Zhu, Y.J.6
  • 87
    • 77951217870 scopus 로고    scopus 로고
    • Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis
    • Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z. Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis. J. Biol. Chem. 2010, 285:12695-12705.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12695-12705
    • Ren, J.1    Wang, Y.2    Liang, Y.3    Zhang, Y.4    Bao, S.5    Xu, Z.6
  • 88
    • 34548636476 scopus 로고    scopus 로고
    • Arginine methylation of Sam68 and SLM proteins negatively regulates their poly (U) RNA binding activity
    • Rho J., Choi S., Jung C.R., Im D.S. Arginine methylation of Sam68 and SLM proteins negatively regulates their poly (U) RNA binding activity. Arch. Biochem. Biophys. 2007, 466:49-57.
    • (2007) Arch. Biochem. Biophys. , vol.466 , pp. 49-57
    • Rho, J.1    Choi, S.2    Jung, C.R.3    Im, D.S.4
  • 90
    • 37549043199 scopus 로고    scopus 로고
    • Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain
    • Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G. Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain. J. Biol. Chem. 2007, 282:36444-36453.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36444-36453
    • Sayegh, J.1    Webb, K.2    Cheng, D.3    Bedford, M.T.4    Clarke, S.G.5
  • 91
    • 35148851963 scopus 로고    scopus 로고
    • PRMT11: a new Arabidopsis MBD7 protein partner with arginine methyltransferase activity
    • Scebba F., De Bastiani M., Bernacchia G., Andreucci A., Galli A., Pitto L. PRMT11: a new Arabidopsis MBD7 protein partner with arginine methyltransferase activity. Plant J. 2007, 52:210-222.
    • (2007) Plant J. , vol.52 , pp. 210-222
    • Scebba, F.1    De Bastiani, M.2    Bernacchia, G.3    Andreucci, A.4    Galli, A.5    Pitto, L.6
  • 93
    • 0032521176 scopus 로고    scopus 로고
    • Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)
    • Scott H.S., Antonarakis S.E., Lalioti M.D., Rossier C., Silver P.A., Henry M.F. Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2). Genomics 1998, 48:330-340.
    • (1998) Genomics , vol.48 , pp. 330-340
    • Scott, H.S.1    Antonarakis, S.E.2    Lalioti, M.D.3    Rossier, C.4    Silver, P.A.5    Henry, M.F.6
  • 97
    • 2542476990 scopus 로고    scopus 로고
    • Arginine methylation of RNA helicase a determines its subcellular localization
    • Smith W.A., Schurter B.T., Wong-Staal F., David M. Arginine methylation of RNA helicase a determines its subcellular localization. J. Biol. Chem. 2004, 279:22795-22798.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22795-22798
    • Smith, W.A.1    Schurter, B.T.2    Wong-Staal, F.3    David, M.4
  • 99
    • 14244255860 scopus 로고    scopus 로고
    • Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)
    • Swiercz R., Person M.D., Bedford M.T. Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3). Biochem. J. 2005, 386:85-91.
    • (2005) Biochem. J. , vol.386 , pp. 85-91
    • Swiercz, R.1    Person, M.D.2    Bedford, M.T.3
  • 100
    • 34447119527 scopus 로고    scopus 로고
    • Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice
    • Swiercz R., Cheng D., Kim D., Bedford M.T. Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice. J. Biol. Chem. 2007, 282:16917-16923.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16917-16923
    • Swiercz, R.1    Cheng, D.2    Kim, D.3    Bedford, M.T.4
  • 101
    • 33749188072 scopus 로고    scopus 로고
    • Control of the DNA methylation system component MBD2 by protein arginine methylation
    • Tan C.P., Nakielny S. Control of the DNA methylation system component MBD2 by protein arginine methylation. Mol. Cell. Biol. 2006, 26:7224-7235.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7224-7235
    • Tan, C.P.1    Nakielny, S.2
  • 102
    • 0032479171 scopus 로고    scopus 로고
    • PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation
    • Tang J., Gary J.D., Clarke S., Herschman H.R. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J. Biol. Chem. 1998, 273:16935-16945.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16935-16945
    • Tang, J.1    Gary, J.D.2    Clarke, S.3    Herschman, H.R.4
  • 103
    • 58149229504 scopus 로고    scopus 로고
    • Gene expression meta-analysis identifies chromosomal regions and candidate genes involved in breast cancer metastasis
    • Thomassen M., Tan Q., Kruse T.A. Gene expression meta-analysis identifies chromosomal regions and candidate genes involved in breast cancer metastasis. Breast Cancer Res. Treat. 2009, 113:239-249.
    • (2009) Breast Cancer Res. Treat. , vol.113 , pp. 239-249
    • Thomassen, M.1    Tan, Q.2    Kruse, T.A.3
  • 104
    • 33846226977 scopus 로고    scopus 로고
    • Histone arginine methylation regulates pluripotency in the early mouse embryo
    • Torres-Padilla M.E., Parfitt D.E., Kouzarides T., Zernicka-Goetz M. Histone arginine methylation regulates pluripotency in the early mouse embryo. Nature 2007, 445:214-218.
    • (2007) Nature , vol.445 , pp. 214-218
    • Torres-Padilla, M.E.1    Parfitt, D.E.2    Kouzarides, T.3    Zernicka-Goetz, M.4
  • 107
    • 34247221117 scopus 로고    scopus 로고
    • SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis
    • Wang X., Zhang Y., Ma Q., Zhang Z., Xue Y., Bao S., Chong K. SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis. EMBO J. 2007, 26:1934-1941.
    • (2007) EMBO J. , vol.26 , pp. 1934-1941
    • Wang, X.1    Zhang, Y.2    Ma, Q.3    Zhang, Z.4    Xue, Y.5    Bao, S.6    Chong, K.7
  • 109
    • 34247158278 scopus 로고    scopus 로고
    • 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
    • Xie B., Invernizzi C.F., Richard S., Wainberg M.A. 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. 2007, 81:4226-4234.
    • (2007) J. Virol. , vol.81 , pp. 4226-4234
    • Xie, B.1    Invernizzi, C.F.2    Richard, S.3    Wainberg, M.A.4
  • 110
    • 36348965898 scopus 로고    scopus 로고
    • Identification and characterization of two closely related histone H4 arginine 3 methyltransferases in Arabidopsis thaliana
    • Yan D., Zhang Y., Niu L., Yuan Y., Cao X. Identification and characterization of two closely related histone H4 arginine 3 methyltransferases in Arabidopsis thaliana. Biochem. J. 2007, 408:113-121.
    • (2007) Biochem. J. , vol.408 , pp. 113-121
    • Yan, D.1    Zhang, Y.2    Niu, L.3    Yuan, Y.4    Cao, X.5
  • 111
    • 78650233514 scopus 로고    scopus 로고
    • TDRD3 is an effector molecule for arginine-methylated histone marks
    • Yang Y., Lu Y., Espejo A., Wu J., Xu W., Liang S., Bedford M.T. TDRD3 is an effector molecule for arginine-methylated histone marks. Mol. Cell 2010, 40:1016-1023.
    • (2010) Mol. Cell , vol.40 , pp. 1016-1023
    • Yang, Y.1    Lu, Y.2    Espejo, A.3    Wu, J.4    Xu, W.5    Liang, S.6    Bedford, M.T.7
  • 112
    • 84862907702 scopus 로고    scopus 로고
    • Tudor domain-containing proteins of Drosophila melanogaster
    • Ying M., Chen D. Tudor domain-containing proteins of Drosophila melanogaster. Dev. Growth Dif 2012, 54:32-43.
    • (2012) Dev. Growth Dif , vol.54 , pp. 32-43
    • Ying, M.1    Chen, D.2
  • 114
    • 72949121026 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 1 regulates herpes simplex virus replication through ICP27 RGG-box methylation
    • Yu J., Shin B., Park E.S., Yang S., Choi S., Kang M., Rho J. Protein arginine methyltransferase 1 regulates herpes simplex virus replication through ICP27 RGG-box methylation. Biochem. Biophys. Res. Commun. 2010, 391:322-328.
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 322-328
    • Yu, J.1    Shin, B.2    Park, E.S.3    Yang, S.4    Choi, S.5    Kang, M.6    Rho, J.7
  • 115
    • 84859223099 scopus 로고    scopus 로고
    • The role of protein arginine methylation in mRNP dynamics
    • Yu M.C. The role of protein arginine methylation in mRNP dynamics. Mol. Cell. Biol. 2011, 2011:1-10.
    • (2011) Mol. Cell. Biol. , vol.2011 , pp. 1-10
    • Yu, M.C.1
  • 116
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides
    • Zhang X., Cheng X. Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Structure 2003, 11:509-520.
    • (2003) Structure , vol.11 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 117
    • 79952288503 scopus 로고    scopus 로고
    • Arabidopsis floral initiator SKB1 confers high salt tolerance by regulating transcription and pre-mRNA splicing through altering histone H4R3 and small nuclear ribonucleoprotein LSM4 methylation
    • Zhang Z., Zhang S., Zhang Y., Wang X., Li D., Li Q., Yue M., Xu Y. Arabidopsis floral initiator SKB1 confers high salt tolerance by regulating transcription and pre-mRNA splicing through altering histone H4R3 and small nuclear ribonucleoprotein LSM4 methylation. Plant Cell 2011, 23:396-411.
    • (2011) Plant Cell , vol.23 , pp. 396-411
    • Zhang, Z.1    Zhang, S.2    Zhang, Y.3    Wang, X.4    Li, D.5    Li, Q.6    Yue, M.7    Xu, Y.8
  • 122
  • 123
    • 84858040000 scopus 로고    scopus 로고
    • Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues
    • Zurita-Lopez C.I., Sandberg T., Kelly R., Clarke S.G. Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues. J. Biol. Chem. 2012, 287:7859-7870.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7859-7870
    • Zurita-Lopez, C.I.1    Sandberg, T.2    Kelly, R.3    Clarke, S.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.