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Volumn 12, Issue 10, 2011, Pages 629-642

Deciphering arginine methylation: Tudor tells the tale

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ARGININE; BINDING PROTEIN; DROSOPHILA PROTEIN; N(G),N(G) DIMETHYLARGININE; PIWI INTERACTING RNA; PIWI PROTEIN; PROTEIN TUDOR; REGULATOR PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 80053132089     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3185     Document Type: Review
Times cited : (238)

References (102)
  • 1
    • 33745813187 scopus 로고    scopus 로고
    • Reading protein modifications with interaction domains
    • DOI 10.1038/nrm1960, PII NRM1960
    • Seet, B. T., Dikic, I., Zhou, M. M. & Pawson, T. Reading protein modifications with interaction domains. Nature Rev. Mol. Cell Biol. 7, 473-483 (2006). (Pubitemid 44036453)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.7 , pp. 473-483
    • Seet, B.T.1    Dikic, I.2    Zhou, M.-M.3    Pawson, T.4
  • 2
    • 0022400587 scopus 로고
    • Tudor, a gene required for assembly of the germ plasma in Drosophila melanogaster
    • Boswell, R. E. & Mahowald, A. P. Tudor, a gene required for assembly of the germ plasm in Drosophila melanogaster. Cell 43, 97-104 (1985). (Pubitemid 16199699)
    • (1985) Cell , vol.43 , Issue.1 , pp. 97-104
    • Boswell, R.E.1    Mahowald, A.P.2
  • 3
    • 0031081575 scopus 로고    scopus 로고
    • Tudor domains in proteins that interact with RNA
    • DOI 10.1016/S0968-0004(96)30049-2, PII S0968000496300492
    • Ponting, C. P. Tudor domains in proteins that interact with RNA. Trends Biochem. Sci. 22, 51-52 (1997). (Pubitemid 27076805)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.2 , pp. 51-52
    • Ponting, C.P.1
  • 4
    • 0031027360 scopus 로고    scopus 로고
    • The human EBNA-2 coactivator p100: Multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development
    • Callebaut, I. & Mornon, J. P. The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the Tudor protein involved in Drosophila melanogaster development. Biochem. J. 321, 125-132 (1997). (Pubitemid 27032578)
    • (1997) Biochemical Journal , vol.321 , Issue.1 , pp. 125-132
    • Callebaut, I.1    Mornon, J.P.2
  • 5
    • 0242683460 scopus 로고    scopus 로고
    • Essential role for the Tudor domain of SMN in spliceosomal U snRNP assembly: Implications for spinal muscular atrophy
    • Buhler, D., Raker, V., Luhrmann, R. & Fischer, U. Essential role for the Tudor domain of SMN in spliceosomal U snRNP assembly: implications for spinal muscular atrophy. Hum. Mol. Genet. 8, 2351-2357 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2351-2357
    • Buhler, D.1    Raker, V.2    Luhrmann, R.3    Fischer, U.4
  • 7
    • 0035947239 scopus 로고    scopus 로고
    • SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets
    • DOI 10.1016/S1097-2765(01)00244-1
    • 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 7, 1111-1117 (2001). (Pubitemid 32525757)
    • (2001) Molecular Cell , vol.7 , Issue.5 , pp. 1111-1117
    • Friesen, W.J.1    Massenet, S.2    Paushkin, S.3    Wyce, A.4    Dreyfuss, G.5
  • 8
    • 0037459239 scopus 로고    scopus 로고
    • High-resolution X-ray and NMR structures of the SMN Tudor domain: Conformational variation in the binding site for symmetrically dimethylated arginine residues
    • DOI 10.1016/S0022-2836(03)00148-7
    • Sprangers, R., Groves, M. R., Sinning, I. & Sattler, M. High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues. J. Mol. Biol. 327, 507-520 (2003). (Pubitemid 36298718)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.2 , pp. 507-520
    • Sprangers, R.1    Groves, M.R.2    Sinning, I.3    Sattler, M.4
  • 10
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers
    • DOI 10.1038/nsmb1338, PII NSMB1338
    • Taverna, S. D., Li, H., Ruthenburg, A. J., Allis, C. D. & Patel, D. J. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nature Struct. Mol. Biol. 14, 1025-1040 (2007). (Pubitemid 350060344)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.11 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 11
    • 65249151919 scopus 로고    scopus 로고
    • Structure and function of histone methylation binding proteins
    • Adams-Cioaba, M. A. & Min, J. Structure and function of histone methylation binding proteins. Biochem. Cell Biol. 87, 93-105 (2009).
    • (2009) Biochem. Cell Biol. , vol.87 , pp. 93-105
    • Adams-Cioaba, M.A.1    Min, J.2
  • 12
    • 78549287139 scopus 로고    scopus 로고
    • Keeping it in the family: Diverse histone recognition by conserved structural folds
    • Yap, K. L. & Zhou, M. M. Keeping it in the family: diverse histone recognition by conserved structural folds. Crit. Rev. Biochem. Mol. Biol. 45, 488-505 (2010).
    • (2010) Crit. Rev. Biochem. Mol. Biol. , vol.45 , pp. 488-505
    • Yap, K.L.1    Zhou, M.M.2
  • 13
    • 33645502395 scopus 로고    scopus 로고
    • Tudor MBT and chromo domains gauge the degree of lysine methylation
    • Kim, J. et al. Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep. 7, 397-403 (2006).
    • (2006) EMBO Rep. , vol.7 , pp. 397-403
    • Kim, J.1
  • 14
    • 36448949026 scopus 로고    scopus 로고
    • Multivalent engagement of chromatin modifications by linked binding modules
    • DOI 10.1038/nrm2298, PII NRM2298
    • Ruthenburg, A. J., Li, H., Patel, D. J. & Allis, C. D. Multivalent engagement of chromatin modifications by linked binding modules. Nature Rev. Mol. Cell Biol. 8, 983-994 (2007). (Pubitemid 350174643)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.12 , pp. 983-994
    • Ruthenburg, A.J.1    Li, H.2    Patel, D.J.3    David Allis, C.4
  • 15
    • 75549086174 scopus 로고    scopus 로고
    • Eukaryotic protein domains as functional units of cellular evolution
    • Jin, J. et al. Eukaryotic protein domains as functional units of cellular evolution. Sci. Signal. 2, ra76 (2009).
    • (2009) Sci. Signal. , vol.2
    • Jin, J.1
  • 16
    • 77950488501 scopus 로고    scopus 로고
    • How does the royal family of Tudor rule the PIWI-interacting RNA pathway?
    • Siomi, M. C., Mannen, T. & Siomi, H. How does the royal family of Tudor rule the PIWI-interacting RNA pathway? Genes Dev. 24, 636-646 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 636-646
    • Siomi, M.C.1    Mannen, T.2    Siomi, H.3
  • 18
    • 33845666681 scopus 로고    scopus 로고
    • Structural Basis for the Methylation State-Specific Recognition of Histone H4-K20 by 53BP1 and Crb2 in DNA Repair
    • DOI 10.1016/j.cell.2006.10.043, PII S009286740601525X
    • Botuyan, M. V. et al. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127, 1361-1373 (2006). (Pubitemid 44960409)
    • (2006) Cell , vol.127 , Issue.7 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.-E.4    Thompson, J.R.5    Chen, J.6    Mer, G.7
  • 19
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double Tudor domain of JMJD2A
    • Huang, Y., Fang, J., Bedford, M. T., Zhang, Y. & Xu, R. M. Recognition of histone H3 lysine-4 methylation by the double Tudor domain of JMJD2A. Science 312, 748-751 (2006).
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 20
    • 77956271553 scopus 로고    scopus 로고
    • Structural basis for methylarginine-dependent recognition of Aubergine by Tudor
    • Liu, H. et al. Structural basis for methylarginine-dependent recognition of Aubergine by Tudor. Genes Dev. 24, 1876-1881 (2010).
    • (2010) Genes Dev , vol.24 , pp. 1876-1881
    • Liu, H.1
  • 21
    • 78649842259 scopus 로고    scopus 로고
    • Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain
    • Liu, K. et al. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proc. Natl Acad. Sci. USA 107, 18398-18403 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 18398-18403
    • Liu, K.1
  • 23
    • 46349107531 scopus 로고    scopus 로고
    • Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing
    • DOI 10.1093/nar/gkn236
    • Li, C. L., Yang, W. Z., Chen, Y. P. & Yuan, H. S. Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing. Nucleic Acids Res. 36, 3579-3589 (2008). (Pubitemid 351917522)
    • (2008) Nucleic Acids Research , vol.36 , Issue.11 , pp. 3579-3589
    • Li, C.-L.1    Yang, W.-Z.2    Chen, Y.-P.3    Yuan, H.S.4
  • 24
    • 62649142373 scopus 로고    scopus 로고
    • Structure and ligand binding of the extended Tudor domain of D. melanogaster Tudor-SN
    • Friberg, A., Corsini, L., Mourao, A. & Sattler, M. Structure and ligand binding of the extended Tudor domain of D. melanogaster Tudor-SN. J. Mol. Biol. 387, 921-934 (2009).
    • (2009) J. Mol. Biol. , vol.387 , pp. 921-934
    • Friberg, A.1    Corsini, L.2    Mourao, A.3    Sattler, M.4
  • 25
    • 33845418030 scopus 로고    scopus 로고
    • Protein arginine methylation: Cellular functions and methods of analysis
    • DOI 10.1016/j.bbapap.2006.08.008, PII S1570963906002810, Posttranslational Modifications in Proteomics
    • Pahlich, S., Zakaryan, R. P. & Gehring, H. Protein arginine methylation: cellular functions and methods of analysis. Biochim. Biophys. Acta 1764, 1890-1903 (2006). (Pubitemid 44895022)
    • (2006) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1764 , Issue.12 , pp. 1890-1903
    • Pahlich, S.1    Zakaryan, R.P.2    Gehring, H.3
  • 26
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein
    • DOI 10.1017/S135583820101442X
    • Brahms, H., Meheus, L., de Brabandere, V., Fischer, U. & Luhrmann, R. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA 7, 1531-1542 (2001). (Pubitemid 33078929)
    • (2001) RNA , vol.7 , Issue.11 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    De Brabandere, V.3    Fischer, U.4    Luhrmann, R.5
  • 27
    • 23344444863 scopus 로고    scopus 로고
    • Tudor domains bind symmetrical dimethylated arginines
    • DOI 10.1074/jbc.M414328200
    • Cote, J. & Richard, S. Tudor domains bind symmetrical dimethylated arginines. J. Biol. Chem. 280, 28476-28483 (2005). (Pubitemid 41105747)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.31 , pp. 28476-28483
    • Cote, J.1    Richard, S.2
  • 28
    • 0034714380 scopus 로고    scopus 로고
    • Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN)
    • Friesen, W. J. & Dreyfuss, G. Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN). J. Biol. Chem. 275, 26370-26375 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26370-26375
    • Friesen, W.J.1    Dreyfuss, G.2
  • 29
    • 0034595798 scopus 로고    scopus 로고
    • The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies
    • DOI 10.1074/jbc.M000300200
    • Brahms, H. et al. The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies. J. Biol. Chem. 275, 17122-17129 (2000). (Pubitemid 30398957)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 17122-17129
    • Brahms, H.1    Raymackers, J.2    Union, A.3    De Keyser, F.4    Meheus, L.5    Luhrmann, R.6
  • 30
    • 0031759799 scopus 로고    scopus 로고
    • Characterization of a gene encoding Survival Motor Neuron (SMN)-related protein, a constituent of the spliceosome complex
    • Talbot, K., Miguel-Aliaga, I., Mohaghegh, P., Ponting, C. P. & Davies, K. E. Characterization of a gene encoding survival motor neuron (SMN)-related protein, a constituent of the spliceosome complex. Hum. Mol. Genet. 7, 2149-2156 (1998). (Pubitemid 28546426)
    • (1998) Human Molecular Genetics , vol.7 , Issue.13 , pp. 2149-2156
    • Talbot, K.1    Miguel-Aliaga, I.2    Mohaghegh, P.3    Ponting, C.P.4    Davies, K.E.5
  • 31
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
    • DOI 10.1016/S0960-9822(01)00592-9
    • Meister, G. et al. Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr. Biol. 11, 1990-1994 (2001). (Pubitemid 33146428)
    • (2001) Current Biology , vol.11 , Issue.24 , pp. 1990-1994
    • Meister, G.1    Eggert, C.2    Buhler, D.3    Brahms, H.4    Kambach, C.5    Fischer, U.6
  • 32
    • 0035903086 scopus 로고    scopus 로고
    • SPF30 is an essential human splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome
    • Rappsilber, J., Ajuh, P., Lamond, A. I. & Mann, M. SPF30 is an essential human splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. J. Biol. Chem. 276, 31142-31150 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 31142-31150
    • Rappsilber, J.1    Ajuh, P.2    Lamond, A.I.3    Mann, M.4
  • 33
    • 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 137, 2819-2828 (2010).
    • (2010) Development , vol.137 , pp. 2819-2828
    • Anne, J.1
  • 34
    • 33846001366 scopus 로고    scopus 로고
    • The Arginine Methyltransferase CARM1 Regulates the Coupling of Transcription and mRNA Processing
    • DOI 10.1016/j.molcel.2006.11.019, PII S1097276506007908
    • Cheng, D., Cote, J., Shaaban, S. & Bedford, M. T. The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing. Mol. Cell 25, 71-83 (2007). (Pubitemid 46049059)
    • (2007) Molecular Cell , vol.25 , Issue.1 , pp. 71-83
    • Cheng, D.1    Cote, J.2    Shaaban, S.3    Bedford, M.T.4
  • 35
    • 78650233514 scopus 로고    scopus 로고
    • TDRD3 is an effector molecule for arginine-methylated histone marks
    • Yang, Y. et al. TDRD3 is an effector molecule for arginine-methylated histone marks. Mol. Cell 40, 1016-1023 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 1016-1023
    • Yang, Y.1
  • 36
    • 79953288782 scopus 로고    scopus 로고
    • The C-terminal domain of RNA polymerase II is modified by site-specific methylation
    • Sims, R. J., et al. The C-terminal domain of RNA polymerase II is modified by site-specific methylation. Science 332, 99-103 (2011).
    • (2011) Science , vol.332 , pp. 99-103
    • Sims, R.J.1
  • 37
    • 53349096773 scopus 로고    scopus 로고
    • Tdrd3 is a novel stress granule-associated protein interacting with the Fragile-X syndrome protein FMRP
    • Linder, B. et al. Tdrd3 is a novel stress granule-associated protein interacting with the Fragile-X syndrome protein FMRP. Hum. Mol. Genet. 17, 3236-3246 (2008).
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3236-3246
    • Linder, B.1
  • 38
    • 52949122554 scopus 로고    scopus 로고
    • TDRD3 a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules
    • Goulet, I., Boisvenue, S., Mokas, S., Mazroui, R. & Cote, J. TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules. Hum. Mol. Genet. 17, 3055-3074 (2008).
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3055-3074
    • Goulet, I.1    Boisvenue, S.2    Mokas, S.3    Mazroui, R.4    Cote, J.5
  • 39
    • 73949084329 scopus 로고    scopus 로고
    • Mouse Piwi interactome identifies binding mechanism of Tdrkh Tudor domain to arginine methylated Miwi
    • Chen, C. et al. Mouse Piwi interactome identifies binding mechanism of Tdrkh Tudor domain to arginine methylated Miwi. Proc. Natl Acad. Sci. USA 106, 20336-20341 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 20336-20341
    • Chen, C.1
  • 40
    • 67349281394 scopus 로고    scopus 로고
    • Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for Ago3 and Aub stability
    • Kirino, Y. et al. Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for Ago3 and Aub stability. Nature Cell Biol. 11, 652-658 (2009).
    • (2009) Nature Cell Biol , vol.11 , pp. 652-658
    • Kirino, Y.1
  • 41
    • 70349981885 scopus 로고    scopus 로고
    • Associations between PIWI proteins and TDRD1/MTR-1 are critical for integrated subcellular localization in murine male germ cells
    • Kojima, K. et al. Associations between PIWI proteins and TDRD1/MTR-1 are critical for integrated subcellular localization in murine male germ cells. Genes Cells 14, 1155-1165 (2009).
    • (2009) Genes Cells , vol.14 , pp. 1155-1165
    • Kojima, K.1
  • 42
    • 72449147419 scopus 로고    scopus 로고
    • Functional involvement of Tudor and dPRMT5 in the piRNA processing pathway in drosophila germlines
    • Nishida, K. M. et al. Functional involvement of Tudor and dPRMT5 in the piRNA processing pathway in Drosophila germlines. EMBO J. 28, 3820-3831 (2009).
    • (2009) EMBO J. , vol.28 , pp. 3820-3831
    • Nishida, K.M.1
  • 43
    • 67349141725 scopus 로고    scopus 로고
    • Loss of the mili-interacting tudor domain-containing protein-1 activates transposons and alters the Mili-associated small RNA profile
    • Reuter, M. et al. Loss of the Mili-interacting Tudor domain-containing protein-1 activates transposons and alters the Mili-associated small RNA profile. Nature Struct. Mol. Biol. 16, 639-646 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 639-646
    • Reuter, M.1
  • 44
    • 68149164399 scopus 로고    scopus 로고
    • Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members
    • Vagin, V. V. et al. Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members. Genes Dev. 23, 1749-1762 (2009).
    • (2009) Genes Dev. , vol.23 , pp. 1749-1762
    • Vagin, V.V.1
  • 45
    • 65049088735 scopus 로고    scopus 로고
    • Mili interacts with Tudor domain-containing protein 1 in regulating spermatogenesis
    • Wang, J., Saxe, J. P., Tanaka, T., Chuma, S. & Lin, H. Mili interacts with Tudor domain-containing protein 1 in regulating spermatogenesis. Curr. Biol. 19, 640-644 (2009).
    • (2009) Curr. Biol. , vol.19 , pp. 640-644
    • Wang, J.1    Saxe, J.P.2    Tanaka, T.3    Chuma, S.4    Lin, H.5
  • 46
    • 75649132891 scopus 로고    scopus 로고
    • Arginine methylation of aubergine mediates tudor binding and germ plasm localization
    • Kirino, Y. et al. Arginine methylation of Aubergine mediates Tudor binding and germ plasm localization. RNA 16, 70-78 (2010).
    • (2010) RNA , vol.16 , pp. 70-78
    • Kirino, Y.1
  • 47
    • 33744506571 scopus 로고    scopus 로고
    • The Sm-protein methyltransferase, Dart5, is essential for germ-cell specification and maintenance
    • DOI 10.1016/j.cub.2006.04.037, PII S0960982206014989
    • Gonsalvez, G. B., Rajendra, T. K., Tian, L. & Matera, A. G. The Sm-protein methyltransferase, dart5, is essential for germ-cell specification and maintenance. Curr. Biol. 16, 1077-1089 (2006). (Pubitemid 43815752)
    • (2006) Current Biology , vol.16 , Issue.11 , pp. 1077-1089
    • Gonsalvez, G.B.1    Rajendra, T.K.2    Tian, L.3    Matera, A.G.4
  • 48
    • 33846517786 scopus 로고    scopus 로고
    • Arginine methyltransferase Capsuléen is essential for methylation of spliceosomal Sm proteins and germ cell formation in Drosophila
    • DOI 10.1242/dev.02687
    • Anne, J., Ollo, R., Ephrussi, A. & Mechler, B. M. Arginine methyltransferase Capsuleen is essential for methylation of spliceosomal Sm proteins and germ cell formation in Drosophila. Development 134, 137-146 (2007). (Pubitemid 46152714)
    • (2007) Development , vol.134 , Issue.1 , pp. 137-146
    • Anne, J.1    Ollo, R.2    Ephrussi, A.3    Mechler, B.M.4
  • 49
    • 77950895342 scopus 로고    scopus 로고
    • Arginine methylation of Vasa protein is conserved across phyla
    • Kirino, Y. et al. Arginine methylation of Vasa protein is conserved across phyla. J. Biol. Chem. 285, 8148-8154 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 8148-8154
    • Kirino, Y.1
  • 50
    • 77955339860 scopus 로고    scopus 로고
    • Building RNA-protein granules: Insight from the germline
    • Arkov, A. L. & Ramos, A. Building RNA-protein granules: insight from the germline. Trends Cell Biol. 20, 482-490 (2010).
    • (2010) Trends Cell Biol , vol.20 , pp. 482-490
    • Arkov, A.L.1    Ramos, A.2
  • 51
    • 74249101368 scopus 로고    scopus 로고
    • Cytoplasmic compartmentalization of the fetal piRNA pathway in mice
    • Aravin, A. A. et al. Cytoplasmic compartmentalization of the fetal piRNA pathway in mice. PLoS Genet. 5, e1000764 (2009).
    • (2009) PLoS Genet. , vol.5
    • Aravin, A.A.1
  • 52
    • 24344456467 scopus 로고    scopus 로고
    • Tudor and its domains: Germ cell formation from a Tudor perspective
    • DOI 10.1038/sj.cr.7290297
    • Thomson, T. & Lasko, P. Tudor and its domains: germ cell formation from a Tudor perspective. Cell Res. 15, 281-291 (2005). (Pubitemid 41642884)
    • (2005) Cell Research , vol.15 , Issue.4 , pp. 281-291
    • Thomson, T.1    Lasko, P.2
  • 53
    • 33751027628 scopus 로고    scopus 로고
    • The role of Tudor domains in germline development and polar granule architecture
    • DOI 10.1242/dev.02572
    • Arkov, A. L., Wang, J. Y., Ramos, A. & Lehmann, R. The role of Tudor domains in germline development and polar granule architecture. Development 133, 4053-4062 (2006). (Pubitemid 44756198)
    • (2006) Development , vol.133 , Issue.20 , pp. 4053-4062
    • Arkov, A.L.1    Wang, J.-Y.S.2    Ramos, A.3    Lehmann, R.4
  • 54
    • 0035838369 scopus 로고    scopus 로고
    • Double-stranded RNA-mediated silencing of genomic tandem repeats and transposable elements in the D. melanogaster germline
    • DOI 10.1016/S0960-9822(01)00299-8
    • Aravin, A. A. et al. Double-stranded RNA-mediated silencing of genomic tandem repeats and transposable elements in the D. melanogaster germline. Curr. Biol. 11, 1017-1027 (2001). (Pubitemid 32632716)
    • (2001) Current Biology , vol.11 , Issue.13 , pp. 1017-1027
    • Aravin, A.A.1    Naumova, N.M.2    Tulin, A.V.3    Vagin, V.V.4    Rozovsky, Y.M.5    Gvozdev, V.A.6
  • 55
    • 85061111209 scopus 로고    scopus 로고
    • The RNA interference proteins and vasa locus are involved in the silencing of retrotransposons in the female germline of Drosophila melanogaster
    • Vagin, V. V. et al. The RNA interference proteins and vasa locus are involved in the silencing of retrotransposons in the female germline of Drosophila melanogaster. RNA Biol. 1, 54-58 (2004).
    • (2004) RNA Biol , vol.1 , pp. 54-58
    • Vagin, V.V.1
  • 56
    • 34249849029 scopus 로고    scopus 로고
    • Unique germ-line organelle, nuage, functions to repress selfish genetic elements in Drosophila melanogaster
    • DOI 10.1073/pnas.0701920104
    • Lim, A. K. & Kai, T. Unique germ-line organelle, nuage, functions to repress selfish genetic elements in Drosophila melanogaster. Proc. Natl Acad. Sci. USA 104, 6714-6719 (2007). (Pubitemid 47175566)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.16 , pp. 6714-6719
    • Ai, K.L.1    Kai, T.2
  • 57
    • 65549105694 scopus 로고    scopus 로고
    • Specialized piRNA pathways act in germline and somatic tissues of the Drosophila ovary
    • Malone, C. D. et al. Specialized piRNA pathways act in germline and somatic tissues of the Drosophila ovary. Cell 137, 522-535 (2009).
    • (2009) Cell , vol.137 , pp. 522-535
    • Malone, C.D.1
  • 58
    • 77951288138 scopus 로고    scopus 로고
    • Repression of retroelements in Drosophila germline via piRNA pathway by the Tudor domain protein Tejas
    • Patil, V. S. & Kai, T. Repression of retroelements in Drosophila germline via piRNA pathway by the Tudor domain protein Tejas. Curr. Biol. 20, 724-730 (2010).
    • (2010) Curr. Biol. , vol.20 , pp. 724-730
    • Patil, V.S.1    Kai, T.2
  • 59
    • 79955366604 scopus 로고    scopus 로고
    • PAPI a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition
    • Liu, L., Qi, H., Wang, J. & Lin, H. PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition. Development 138, 1863-1873 (2011).
    • (2011) Development , vol.138 , pp. 1863-1873
    • Liu, L.1    Qi, H.2    Wang, J.3    Lin, H.4
  • 60
    • 66149145780 scopus 로고    scopus 로고
    • The Yb protein defines a novel organelle and regulates male germline stem cell self-renewal in Drosophila melanogaster
    • Szakmary, A., Reedy, M., Qi, H. & Lin, H. The Yb protein defines a novel organelle and regulates male germline stem cell self-renewal in Drosophila melanogaster. J. Cell Biol. 185, 613-627 (2009).
    • (2009) J. Cell Biol. , vol.185 , pp. 613-627
    • Szakmary, A.1    Reedy, M.2    Qi, H.3    Lin, H.4
  • 61
    • 77957793321 scopus 로고    scopus 로고
    • An in vivo RNAi assay identifies major genetic and cellular requirements for primary piRNA biogenesis in Drosophila
    • Olivieri, D., Sykora, M. M., Sachidanandam, R., Mechtler, K. & Brennecke, J. An in vivo RNAi assay identifies major genetic and cellular requirements for primary piRNA biogenesis in Drosophila. EMBO J. 29, 3301-3317 (2010).
    • (2010) EMBO J. , vol.29 , pp. 3301-3317
    • Olivieri, D.1    Sykora, M.M.2    Sachidanandam, R.3    Mechtler, K.4    Brennecke, J.5
  • 62
    • 78149478349 scopus 로고    scopus 로고
    • Roles for the Yb body components Armitage and Yb in primary piRNA biogenesis in Drosophila
    • Saito, K. et al. Roles for the Yb body components Armitage and Yb in primary piRNA biogenesis in Drosophila. Genes Dev. 24, 2493-2498 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 2493-2498
    • Saito, K.1
  • 63
    • 79952792594 scopus 로고    scopus 로고
    • The Yb body, a major site for Piwi-associated RNA biogenesis and a gateway for Piwi expression and transport to the nucleus in somatic cells
    • Qi, H. et al. The Yb body, a major site for Piwi-associated RNA biogenesis and a gateway for Piwi expression and transport to the nucleus in somatic cells. J. Biol. Chem. 286, 3789-3797 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 3789-3797
    • Qi, H.1
  • 67
    • 27144461786 scopus 로고    scopus 로고
    • RNF17, a component of the mammalian germ cell nuage, is essential for spermiogenesis
    • DOI 10.1242/dev.02003
    • Pan, J. et al. RNF17, a component of the mammalian germ cell nuage, is essential for spermiogenesis. Development 132, 4029-4039 (2005). (Pubitemid 41488853)
    • (2005) Development , vol.132 , Issue.18 , pp. 4029-4039
    • Pan, J.1    Goodheart, M.2    Chuma, S.3    Nakatsuji, N.4    Page, D.C.5    Wang, P.J.6
  • 68
    • 65049090424 scopus 로고    scopus 로고
    • Tdrd6 is required for spermiogenesis, chromatoid body architecture, and regulation of miRNA expression
    • Vasileva, A., Tiedau, D., Firooznia, A., Muller-Reichert, T. & Jessberger, R. Tdrd6 is required for spermiogenesis, chromatoid body architecture, and regulation of miRNA expression. Curr. Biol. 19, 630-639 (2009).
    • (2009) Curr. Biol. , vol.19 , pp. 630-639
    • Vasileva, A.1    Tiedau, D.2    Firooznia, A.3    Muller-Reichert, T.4    Jessberger, R.5
  • 69
    • 79953147369 scopus 로고    scopus 로고
    • Mutations in the RNA granule component TDRD7 cause cataract and glaucoma
    • Lachke, S. A. et al. Mutations in the RNA granule component TDRD7 cause cataract and glaucoma. Science 331, 1571-1576 (2011).
    • (2011) Science , vol.331 , pp. 1571-1576
    • Lachke, S.A.1
  • 70
    • 79960572781 scopus 로고    scopus 로고
    • Tudor domain containing 7 (Tdrd7) is essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis
    • Tanaka, T. et al. Tudor domain containing 7 (Tdrd7) is essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis. Proc. Natl Acad. Sci. USA 108, 10579-10584 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 10579-10584
    • Tanaka, T.1
  • 71
    • 0036083480 scopus 로고    scopus 로고
    • Miwi, a murine homolog of piwi, encodes a cytoplasmic protein essential for spermatogenesis
    • DOI 10.1016/S1534-5807(02)00165-X
    • Deng, W. & Lin, H. miwi, a murine homolog of piwi, encodes a cytoplasmic protein essential for spermatogenesis. Dev. Cell 2, 819-830 (2002). (Pubitemid 34650077)
    • (2002) Developmental Cell , vol.2 , Issue.6 , pp. 819-830
    • Deng, W.1    Lin, H.2
  • 72
    • 33845609223 scopus 로고    scopus 로고
    • Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: Domain composition, intracellular localization, and function in male germ cells in mice
    • DOI 10.1016/j.ydbio.2006.10.046, PII S0012160606013406
    • Hosokawa, M. et al. Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain composition, intracellular localization, and function in male germ cells in mice. Dev. Biol. 301, 38-52 (2007). (Pubitemid 44958404)
    • (2007) Developmental Biology , vol.301 , Issue.1 , pp. 38-52
    • Hosokawa, M.1    Shoji, M.2    Kitamura, K.3    Tanaka, T.4    Noce, T.5    Chuma, S.6    Nakatsuji, N.7
  • 73
    • 79952375230 scopus 로고    scopus 로고
    • TDRD5 is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis in mice
    • Yabuta, Y. et al. TDRD5 is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis in mice. J. Cell Biol. 192, 781-795 (2011).
    • (2011) J. Cell Biol , vol.192 , pp. 781-795
    • Yabuta, Y.1
  • 74
    • 71649101009 scopus 로고    scopus 로고
    • The TDRD9-MIWI2 complex is essential for piRNA-mediated retrotransposon silencing in the mouse male germline
    • Shoji, M. et al. The TDRD9-MIWI2 complex is essential for piRNA-mediated retrotransposon silencing in the mouse male germline. Dev. Cell 17, 775-787 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 775-787
    • Shoji, M.1
  • 75
    • 78650212707 scopus 로고    scopus 로고
    • Prmt5 is essential for early mouse development and acts in the cytoplasm to maintain ES cell pluripotency
    • Tee, W. W. et al. Prmt5 is essential for early mouse development and acts in the cytoplasm to maintain ES cell pluripotency. Genes Dev. 24, 2772-2777 (2010).
    • (2010) Genes Dev , vol.24 , pp. 2772-2777
    • Tee, W.W.1
  • 76
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • DOI 10.1126/science.278.5346.2075
    • Pawson, T. & Scott, J. D. Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075-2080 (1997). (Pubitemid 28028310)
    • (1997) Science , vol.278 , Issue.5346 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 77
    • 33847718707 scopus 로고    scopus 로고
    • Dynamic control of signaling by modular adaptor proteins
    • DOI 10.1016/j.ceb.2007.02.013, PII S0955067407000270
    • Pawson, T. Dynamic control of signaling by modular adaptor proteins. Curr. Opin. Cell Biol. 19, 112-116 (2007). (Pubitemid 46386409)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.2 , pp. 112-116
    • Pawson, T.1
  • 79
    • 62049086288 scopus 로고    scopus 로고
    • PRMT5-mediated methylation of histone H4R3 recruits DNMT3A, coupling histone and DNA methylation in gene silencing
    • Zhao, Q. et al. PRMT5-mediated methylation of histone H4R3 recruits DNMT3A, coupling histone and DNA methylation in gene silencing. Nature Struct. Mol. Biol. 16, 304-311 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 304-311
    • Zhao, Q.1
  • 80
    • 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. 61, 65-131 (1998).
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 81
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation: An emerging regulator of protein function
    • DOI 10.1016/j.molcel.2005.04.003, PII S1097276505012475
    • Bedford, M. T. & Richard, S. Arginine methylation an emerging regulator of protein function. Mol. Cell 18, 263-272 (2005). (Pubitemid 41350532)
    • (2005) Molecular Cell , vol.18 , Issue.3 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 82
    • 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 33, 1-13 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 83
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 is a histone arginine demethylase
    • DOI 10.1126/science.1145801
    • Chang, B., Chen, Y., Zhao, Y. & Bruick, R. K. JMJD6 is a histone arginine demethylase. Science 318, 444-447 (2007). (Pubitemid 47614528)
    • (2007) Science , vol.318 , Issue.5849 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 84
    • 67650072604 scopus 로고    scopus 로고
    • Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing
    • Webby, C. J. et al. Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science 325, 90-93 (2009).
    • (2009) Science , vol.325 , pp. 90-93
    • Webby, C.J.1
  • 87
    • 37549014207 scopus 로고    scopus 로고
    • Argonaute proteins: Key players in RNA silencing
    • Hutvagner, G. & Simard, M. J. Argonaute proteins: key players in RNA silencing. Nature Rev. Mol. Cell Biol. 9, 22-32 (2008).
    • (2008) Nature Rev. Mol. Cell Biol. , vol.9 , pp. 22-32
    • Hutvagner, G.1    Simard, M.J.2
  • 89
    • 33745621037 scopus 로고    scopus 로고
    • A novel class of small RNAs in mouse spermatogenic cells
    • DOI 10.1101/gad.1434406
    • Grivna, S. T., Beyret, E., Wang, Z. & Lin, H. A novel class of small RNAs in mouse spermatogenic cells. Genes Dev. 20, 1709-1714 (2006). (Pubitemid 43992878)
    • (2006) Genes and Development , vol.20 , Issue.13 , pp. 1709-1714
    • Grivna, S.T.1    Beyret, E.2    Wang, Z.3    Lin, H.4
  • 90
    • 33745336617 scopus 로고    scopus 로고
    • A germline-specific class of small RNAs binds mammalian Piwi proteins
    • DOI 10.1038/nature04917, PII NATURE04917
    • Girard, A., Sachidanandam, R., Hannon, G. J. & Carmell, M. A. A germline-specific class of small RNAs binds mammalian Piwi proteins. Nature 442, 199-202 (2006). (Pubitemid 44086566)
    • (2006) Nature , vol.442 , Issue.7099 , pp. 199-202
    • Girard, A.1    Sachidanandam, R.2    Hannon, G.J.3    Carmell, M.A.4
  • 92
    • 33745599586 scopus 로고    scopus 로고
    • Identification and characterization of two novel classes of small RNAs in the mouse germline: Retrotransposon-derived siRNAs in oocytes and germline small RNAs in testes
    • DOI 10.1101/gad.1425706
    • Watanabe, T. et al. Identification and characterization of two novel classes of small RNAs in the mouse germline: retrotransposon-derived siRNAs in oocytes and germline small RNAs in testes. Genes Dev. 20, 1732-1743 (2006). (Pubitemid 43992882)
    • (2006) Genes and Development , vol.20 , Issue.13 , pp. 1732-1743
    • Watanabe, T.1    Takeda, A.2    Tsukiyama, T.3    Mise, K.4    Okuno, T.5    Sasaki, H.6    Minami, N.7    Imai, H.8
  • 94
    • 36749037521 scopus 로고    scopus 로고
    • The Piwi-piRNA pathway provides an adaptive defense in the transposon arms race
    • DOI 10.1126/science.1146484
    • Aravin, A. A., Hannon, G. J. & Brennecke, J. The Piwi-piRNA pathway provides an adaptive defense in the transposon arms race. Science 318, 761-764 (2007). (Pubitemid 351411762)
    • (2007) Science , vol.318 , Issue.5851 , pp. 761-764
    • Aravin, A.A.1    Hannon, G.J.2    Brennecke, J.3
  • 95
    • 33947273235 scopus 로고    scopus 로고
    • Discrete Small RNA-Generating Loci as Master Regulators of Transposon Activity in Drosophila
    • DOI 10.1016/j.cell.2007.01.043, PII S0092867407002577
    • Brennecke, J. et al. Discrete small RNA-generating loci as master regulators of transposon activity in Drosophila. Cell 128, 1089-1103 (2007). (Pubitemid 46427877)
    • (2007) Cell , vol.128 , Issue.6 , pp. 1089-1103
    • Brennecke, J.1    Aravin, A.A.2    Stark, A.3    Dus, M.4    Kellis, M.5    Sachidanandam, R.6    Hannon, G.J.7
  • 97
    • 74849115776 scopus 로고    scopus 로고
    • Arginine methylation as a molecular signature of the Piwi small RNA pathway
    • Vagin, V. V., Hannon, G. J. & Aravin, A. A. Arginine methylation as a molecular signature of the Piwi small RNA pathway. Cell Cycle 8, 4003-4004 (2009).
    • (2009) Cell Cycle , vol.8 , pp. 4003-4004
    • Vagin, V.V.1    Hannon, G.J.2    Aravin, A.A.3
  • 98
    • 77954381767 scopus 로고    scopus 로고
    • Small RNAs in the animal gonad: Guarding genomes and guiding development
    • Lau, N. C. Small RNAs in the animal gonad: guarding genomes and guiding development. Int. J. Biochem. Cell Biol. 42, 1334-1347 (2010).
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 1334-1347
    • Lau, N.C.1
  • 99
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • DOI 10.1126/science.1069473
    • Jacobs, S. A. & Khorasanizadeh, S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295, 2080-2083 (2002). (Pubitemid 34229471)
    • (2002) Science , vol.295 , Issue.5562 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 101
    • 77951977878 scopus 로고    scopus 로고
    • Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1
    • Vezzoli, A. et al. Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1. Nature Struct. Mol. Biol. 17, 617-619 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 617-619
    • Vezzoli, A.1
  • 102
    • 33644799748 scopus 로고    scopus 로고
    • The structure of the N-terminal domain of the fragile X mental retardation protein: A platform for protein-protein interaction
    • DOI 10.1016/j.str.2005.09.018, PII S0969212605003989
    • Ramos, A. et al. The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction. Structure 14, 21-31 (2006). (Pubitemid 43350070)
    • (2006) Structure , vol.14 , Issue.1 , pp. 21-31
    • Ramos, A.1    Hollingworth, D.2    Adinolfi, S.3    Castets, M.4    Kelly, G.5    Frenkiel, T.A.6    Bardoni, B.7    Pastore, A.8


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