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Volumn 84, Issue , 2015, Pages 355-379

Biochemical properties and biological functions of FET proteins

Author keywords

EWSR1; FUS; Low complexity; Neurodegeneration; RNA binding; TAF15

Indexed keywords

CELL PROTEIN; DOUBLE STRANDED DNA; FET PROTEIN; FUSED IN SARCOMA PROTEIN; MESSENGER RNA; MESSENGER RNA PRECURSOR; PROTEIN; PROTEIN SM; RNA BINDING PROTEIN EWS; RNA POLYMERASE II; SINGLE STRANDED DNA; TATA BINDING PROTEIN; TATA BOX BINDING PROTEIN 15; UNCLASSIFIED DRUG; RNA BINDING PROTEIN; TATA BINDING PROTEIN ASSOCIATED FACTOR;

EID: 84930705294     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-060614-034325     Document Type: Review
Times cited : (163)

References (151)
  • 1
    • 84904466370 scopus 로고    scopus 로고
    • Quality control of mRNP biogenesis: Networking at the transcription site
    • Eberle AB, Visa N. 2014. Quality control of mRNP biogenesis: networking at the transcription site. Semin. Cell Dev. Biol. 32C:37-46
    • (2014) Semin. Cell Dev. Biol. , vol.32 C , pp. 37-46
    • Eberle, A.B.1    Visa, N.2
  • 2
    • 19344367418 scopus 로고    scopus 로고
    • Formation of export-competent mRNP: Escaping nuclear destruction
    • Saguez C, Olesen JR, Jensen TH. 2005. Formation of export-competent mRNP: escaping nuclear destruction. Curr. Opin. Cell Biol. 17:287-93
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 287-293
    • Saguez, C.1    Olesen, J.R.2    Jensen, T.H.3
  • 3
    • 60149110358 scopus 로고    scopus 로고
    • Pre-mRNA processing reaches back to transcription and ahead to translation
    • Moore MJ, Proudfoot NJ. 2009. Pre-mRNA processing reaches back to transcription and ahead to translation. Cell 136:688-700
    • (2009) Cell , vol.136 , pp. 688-700
    • Moore, M.J.1    Proudfoot, N.J.2
  • 4
    • 0033375911 scopus 로고    scopus 로고
    • Mechanisms of mRNA surveillance in eukaryotes
    • Hilleren P, Parker R. 1999. Mechanisms of mRNA surveillance in eukaryotes. Annu. Rev. Genet. 33:229-60
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 229-260
    • Hilleren, P.1    Parker, R.2
  • 5
    • 84901033525 scopus 로고    scopus 로고
    • Principles and properties of eukaryotic mRNPs
    • Mitchell SF, Parker R. 2014. Principles and properties of eukaryotic mRNPs. Mol. Cell 54:547-58
    • (2014) Mol. Cell , vol.54 , pp. 547-558
    • Mitchell, S.F.1    Parker, R.2
  • 6
    • 84875229872 scopus 로고    scopus 로고
    • How cells get the message: Dynamic assembly and function of mRNA-protein complexes
    • Müller-McNicoll M, Neugebauer KM. 2013. How cells get the message: dynamic assembly and function of mRNA-protein complexes. Nat. Rev. Genet. 14:275-87
    • (2013) Nat. Rev. Genet. , vol.14 , pp. 275-287
    • Müller-Mcnicoll, M.1    Neugebauer, K.M.2
  • 7
    • 84861969926 scopus 로고    scopus 로고
    • Insights into RNA biology from an atlas of mammalian mRNA-binding proteins
    • Castello A, Fischer B, Eichelbaum K, Horos R, Beckmann BM, et al. 2012. Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149:1393-406
    • (2012) Cell , vol.149 , pp. 1393-1406
    • Castello, A.1    Fischer, B.2    Eichelbaum, K.3    Horos, R.4    Beckmann, B.M.5
  • 8
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Piñol-Roma S, Dreyfuss G. 1992. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 355:730-32
    • (1992) Nature , vol.355 , pp. 730-732
    • Piñol-Roma, S.1    Dreyfuss, G.2
  • 9
    • 0027411587 scopus 로고
    • HnRNP proteins: Localization and transport between the nucleus and the cytoplasm
    • Piñol-Roma S, Dreyfuss G. 1993. hnRNP proteins: localization and transport between the nucleus and the cytoplasm. Trends Cell Biol. 3:151-55
    • (1993) Trends Cell Biol. , vol.3 , pp. 151-155
    • Piñol-Roma, S.1    Dreyfuss, G.2
  • 10
    • 0034618358 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoproteins as regulators of gene expression through interactions with the human thymidine kinase promoter
    • Lau JS, Baumeister P, Kim E, Roy B, Hsieh TY, et al. 2000. Heterogeneous nuclear ribonucleoproteins as regulators of gene expression through interactions with the human thymidine kinase promoter. J. Cell Biochem. 79:395-406
    • (2000) J. Cell Biochem. , vol.79 , pp. 395-406
    • Lau, J.S.1    Baumeister, P.2    Kim, E.3    Roy, B.4    Hsieh, T.Y.5
  • 11
    • 0028905957 scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K is a DNA-binding transactivator
    • Tomonaga T, Levens D. 1995. Heterogeneous nuclear ribonucleoprotein K is a DNA-binding transactivator. J. Biol. Chem. 270:4875-81
    • (1995) J. Biol. Chem. , vol.270 , pp. 4875-4881
    • Tomonaga, T.1    Levens, D.2
  • 12
    • 0032562765 scopus 로고    scopus 로고
    • Identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a repressor of C/EBPβ-mediated gene activation
    • Miau LH, Chang CJ, Shen BJ, Tsai WH, Lee SC. 1998. Identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a repressor of C/EBPβ-mediated gene activation. J. Biol. Chem. 273:10784-91
    • (1998) J. Biol. Chem. , vol.273 , pp. 10784-10791
    • Miau, L.H.1    Chang, C.J.2    Shen, B.J.3    Tsai, W.H.4    Lee, S.C.5
  • 13
    • 34548446433 scopus 로고    scopus 로고
    • Sarcomas: Genetics, signalling, and cellular origins. Part 1: The fellowship of TET
    • Riggi N, Cironi L, Suva ML, Stamenkovic I. 2007. Sarcomas: genetics, signalling, and cellular origins. Part 1: The fellowship of TET. J. Pathol. 213:4-20
    • (2007) J. Pathol , vol.213 , pp. 4-20
    • Riggi, N.1    Cironi, L.2    Suva, M.L.3    Stamenkovic, I.4
  • 14
    • 77449136874 scopus 로고    scopus 로고
    • The TET family of proteins: Functions and roles in disease
    • Tan AY, Manley JL. 2009. The TET family of proteins: functions and roles in disease. J. Mol. Cell Biol. 1:82-92
    • (2009) J. Mol. Cell Biol. , vol.1 , pp. 82-92
    • Tan, A.Y.1    Manley, J.L.2
  • 15
    • 84860863700 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Bound RNAs identify features and components of cellular assemblies
    • Han TW, Kato M, Xie S, Wu LC, Mirzaei H, et al. 2012. Cell-free formation of RNA granules: Bound RNAs identify features and components of cellular assemblies. Cell 149:768-79
    • (2012) Cell , vol.149 , pp. 768-779
    • Han, T.W.1    Kato, M.2    Xie, S.3    Wu, L.C.4    Mirzaei, H.5
  • 16
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation ofRNAgranules: Low complexity sequence domains form dynamic fibers within hydrogels
    • Kato M, Han TW, Xie S, Shi K, Du X, et al. 2012. Cell-free formation ofRNAgranules: Low complexity sequence domains form dynamic fibers within hydrogels. Cell 149:753-67
    • (2012) Cell , vol.149 , pp. 753-767
    • Kato, M.1    Han, T.W.2    Xie, S.3    Shi, K.4    Du, X.5
  • 17
    • 84888440451 scopus 로고    scopus 로고
    • Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains
    • Kwon I, Kato M, Xiang S, Wu L, Theodoropoulos P, et al. 2013. Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains. Cell 155:1049-60
    • (2013) Cell , vol.155 , pp. 1049-1060
    • Kwon, I.1    Kato, M.2    Xiang, S.3    Wu, L.4    Theodoropoulos, P.5
  • 19
    • 79251573834 scopus 로고    scopus 로고
    • Dr. Jekyll and Mr.Hyde: The two faces of the FUS/EWS/TAF15 protein family
    • KovarH. 2011. Dr. Jekyll and Mr.Hyde: the two faces of the FUS/EWS/TAF15 protein family. Sarcoma 2011:837474
    • (2011) Sarcoma , vol.2011 , pp. 837474
    • Kovar, H.1
  • 20
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: The FUS about TDP-43
    • Lagier-Tourenne C, Cleveland DW. 2009. Rethinking ALS: the FUS about TDP-43. Cell 136:1001-4
    • (2009) Cell , vol.136 , pp. 1001-1004
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 21
    • 77956850818 scopus 로고    scopus 로고
    • TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
    • Mackenzie IR, Rademakers R, Neumann M. 2010. TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol. 9:995-1007
    • (2010) Lancet Neurol. , vol.9 , pp. 995-1007
    • Mackenzie, I.R.1    Rademakers, R.2    Neumann, M.3
  • 22
    • 0029812470 scopus 로고    scopus 로고
    • HTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II
    • Bertolotti A, Lutz Y, Heard DJ, Chambon P, Tora L. 1996. hTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II. EMBO J. 15:5022-31
    • (1996) EMBO J. , vol.15 , pp. 5022-5031
    • Bertolotti, A.1    Lutz, Y.2    Heard, D.J.3    Chambon, P.4    Tora, L.5
  • 23
    • 84871807395 scopus 로고    scopus 로고
    • The RRM domain of human fused in sarcoma protein reveals a non-canonical nucleic acid binding site
    • Liu X, Niu C, Ren J, Zhang J, Xie X, et al. 2013. The RRM domain of human fused in sarcoma protein reveals a non-canonical nucleic acid binding site. Biochim. Biophys. Acta 1832:375-85
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 375-385
    • Liu, X.1    Niu, C.2    Ren, J.3    Zhang, J.4    Xie, X.5
  • 24
    • 0031569797 scopus 로고    scopus 로고
    • Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs
    • Xu RM, Jokhan L, Cheng X, Mayeda A, Krainer AR. 1997. Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs. Structure 5:559-70
    • (1997) Structure , vol.5 , pp. 559-570
    • Xu, R.M.1    Jokhan, L.2    Cheng, X.3    Mayeda, A.4    Krainer, A.R.5
  • 25
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • Ding J, Hayashi MK, Zhang Y, Manche L, Krainer AR, Xu RM. 1999. Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. Genes Dev. 13:1102-15
    • (1999) Genes Dev. , vol.13 , pp. 1102-1115
    • Ding, J.1    Hayashi, M.K.2    Zhang, Y.3    Manche, L.4    Krainer, A.R.5    Xu, R.M.6
  • 26
    • 7244242399 scopus 로고    scopus 로고
    • Domain architectures and characterization of an RNA-binding protein, TLS
    • Iko Y, Kodama TS, Kasai N, Oyama T, Morita EH, et al. 2004. Domain architectures and characterization of an RNA-binding protein, TLS. J. Biol. Chem. 279:44834-40
    • (2004) J. Biol. Chem. , vol.279 , pp. 44834-44840
    • Iko, Y.1    Kodama, T.S.2    Kasai, N.3    Oyama, T.4    Morita, E.H.5
  • 27
    • 0031047632 scopus 로고    scopus 로고
    • Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75A° resolution
    • Shamoo Y, Krueger U, Rice LM, Williams KR, Steitz TA. 1997. Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75A° resolution. Nat. Struct. Biol. 4:215-22
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 215-222
    • Shamoo, Y.1    Krueger, U.2    Rice, L.M.3    Williams, K.R.4    Steitz, T.A.5
  • 28
    • 50249131374 scopus 로고    scopus 로고
    • A role for Q/N-rich aggregation-prone regions in P-body localization
    • Reijns MA, Alexander RD, Spiller MP, Beggs JD. 2008. A role for Q/N-rich aggregation-prone regions in P-body localization. J. Cell Sci. 121:2463-72
    • (2008) J. Cell Sci. , vol.121 , pp. 2463-2472
    • Reijns, M.A.1    Alexander, R.D.2    Spiller, M.P.3    Beggs, J.D.4
  • 29
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • Decker CJ, Teixeira D, Parker R. 2007. Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. J. Cell Biol. 179:437-49
    • (2007) J. Cell Biol. , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 30
    • 9444279617 scopus 로고    scopus 로고
    • Stress granule assembly is mediated by prion-like aggregation of TIA-1
    • Gilks N, Kedersha N, Ayodele M, Shen L, Stoecklin G, et al. 2004. Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol. Biol. Cell 15:5383-98
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5383-5398
    • Gilks, N.1    Kedersha, N.2    Ayodele, M.3    Shen, L.4    Stoecklin, G.5
  • 31
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King OD, Gitler AD, Shorter J. 2012. The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res. 1462:61-80
    • (2012) Brain Res. , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 32
    • 0029372980 scopus 로고
    • Identification of hnRNP P2 as TLS/FUS using electrospray mass spectrometry
    • Calvio C, Neubauer G, Mann M, Lamond AI. 1995. Identification of hnRNP P2 as TLS/FUS using electrospray mass spectrometry. RNA 1:724-33
    • (1995) RNA , vol.1 , pp. 724-733
    • Calvio, C.1    Neubauer, G.2    Mann, M.3    Lamond, A.I.4
  • 33
    • 79952520900 scopus 로고    scopus 로고
    • Identification of Ewing's sarcoma protein (EWS) as a G-quadruplex DNA- and RNA-binding protein
    • Takahama K, Kino K, Arai S, Kurokawa R, Oyoshi T. 2011. Identification of Ewing's sarcoma protein (EWS) as a G-quadruplex DNA- and RNA-binding protein. FEBS J. 278:988-98
    • (2011) FEBS J. , vol.278 , pp. 988-998
    • Takahama, K.1    Kino, K.2    Arai, S.3    Kurokawa, R.4    Oyoshi, T.5
  • 34
    • 84859986072 scopus 로고    scopus 로고
    • TLS/FUS (translocated in liposarcoma/ fused in sarcoma) regulates target gene transcription via single-stranded DNA response elements
    • Tan AY, Riley TR, Coady T, Bussemaker HJ, Manley JL. 2012. TLS/FUS (translocated in liposarcoma/ fused in sarcoma) regulates target gene transcription via single-stranded DNA response elements. PNAS 109:6040-35
    • (2012) PNAS , vol.109 , pp. 6040-6135
    • Tan, A.Y.1    Riley, T.R.2    Coady, T.3    Bussemaker, H.J.4    Manley, J.L.5
  • 35
    • 0030596083 scopus 로고    scopus 로고
    • Molecular cloning and subcellular localisation of the snRNP-associated protein 69KD, a structural homologue of the proto-oncoproteins TLS and EWS with RNA- and DNAbinding properties
    • Hackl W, Lührmann R. 1996. Molecular cloning and subcellular localisation of the snRNP-associated protein 69KD, a structural homologue of the proto-oncoproteins TLS and EWS with RNA- and DNAbinding properties. J. Mol. Biol. 264:843-51
    • (1996) J. Mol. Biol. , vol.264 , pp. 843-851
    • Hackl, W.1    Lührmann, R.2
  • 36
    • 0029964391 scopus 로고    scopus 로고
    • A nuclear protein regulated during the transition from active to quiescent phenotype in cultured endothelial cells
    • Alliegro MC, Alliegro MA. 1996. A nuclear protein regulated during the transition from active to quiescent phenotype in cultured endothelial cells. Dev. Biol. 174:288-97
    • (1996) Dev. Biol. , vol.174 , pp. 288-297
    • Alliegro, M.C.1    Alliegro, M.A.2
  • 38
    • 0030746523 scopus 로고    scopus 로고
    • TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling
    • Zinszner H, Sok J, Immanuel D, Yin Y, Ron D. 1997. TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling. J. Cell Sci. 110:1741-50
    • (1997) J. Cell Sci. , vol.110 , pp. 1741-1750
    • Zinszner, H.1    Sok, J.2    Immanuel, D.3    Yin, Y.4    Ron, D.5
  • 39
    • 0033858675 scopus 로고    scopus 로고
    • BCR-ABL prevents c-Junmediated and proteasome-dependent FUS (TLS) proteolysis through a protein kinase CβII-dependent pathway
    • Perrotti D, Iervolino A, Cesi V, Cirinna M, Lombardini S, et al. 2000. BCR-ABL prevents c-Junmediated and proteasome-dependent FUS (TLS) proteolysis through a protein kinase CβII-dependent pathway. Mol. Cell. Biol. 20:6159-69
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6159-6169
    • Perrotti, D.1    Iervolino, A.2    Cesi, V.3    Cirinna, M.4    Lombardini, S.5
  • 40
    • 54049138797 scopus 로고    scopus 로고
    • Identification and characterization of FUS/TLS as a new target of ATM
    • Gardiner M, Toth R, Vandermoere F, Morrice NA, Rouse J. 2008. Identification and characterization of FUS/TLS as a new target of ATM. Biochem. J. 415:297-307
    • (2008) Biochem. J. , vol.415 , pp. 297-307
    • Gardiner, M.1    Toth, R.2    Vandermoere, F.3    Morrice, N.A.4    Rouse, J.5
  • 41
    • 33845188648 scopus 로고    scopus 로고
    • An in vitro enzymatic assay coupled to proteomics analysis reveals a new DNA processing activity for Ewing sarcoma and TAF(II)68 proteins
    • Guipaud O, Guillonneau F, Labas V, Praseuth D, Rossier J, et al. 2006. An in vitro enzymatic assay coupled to proteomics analysis reveals a new DNA processing activity for Ewing sarcoma and TAF(II)68 proteins. Proteomics 6:5962-72
    • (2006) Proteomics , vol.6 , pp. 5962-5972
    • Guipaud, O.1    Guillonneau, F.2    Labas, V.3    Praseuth, D.4    Rossier, J.5
  • 42
    • 0033527059 scopus 로고    scopus 로고
    • Human POMp75 is identified as the pro-oncoprotein TLS/FUS: Both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferation
    • Bertrand P, Akhmedov AT, Delacote F, Durrbach A, Lopez BS. 1999. Human POMp75 is identified as the pro-oncoprotein TLS/FUS: Both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferation. Oncogene 18:4515-21
    • (1999) Oncogene , vol.18 , pp. 4515-4521
    • Bertrand, P.1    Akhmedov, A.T.2    Delacote, F.3    Durrbach, A.4    Lopez, B.S.5
  • 43
    • 0033607753 scopus 로고    scopus 로고
    • Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation
    • Baechtold H, Kuroda M, Sok J, Ron D, Lopez BS, Akhmedov AT. 1999. Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation. J. Biol. Chem. 274:34337-42
    • (1999) J. Biol. Chem. , vol.274 , pp. 34337-34342
    • Baechtold, H.1    Kuroda, M.2    Sok, J.3    Ron, D.4    Lopez, B.S.5    Akhmedov, A.T.6
  • 44
    • 0027227651 scopus 로고
    • Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma
    • Crozat A, Aman P, Mandahl N, Ron D. 1993. Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma. Nature 363:640-44
    • (1993) Nature , vol.363 , pp. 640-644
    • Crozat, A.1    Aman, P.2    Mandahl, N.3    Ron, D.4
  • 45
    • 0027970712 scopus 로고
    • A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP
    • Zinszner H, Albalat R, Ron D. 1994. A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP. Genes Dev. 8:2513-26
    • (1994) Genes Dev. , vol.8 , pp. 2513-2526
    • Zinszner, H.1    Albalat, R.2    Ron, D.3
  • 46
    • 0029053747 scopus 로고
    • Association of SARFH (sarcoma-associated RNA-binding fly homolog) with regions of chromatin transcribed by RNA polymerase II
    • Immanuel D, Zinszner H, Ron D. 1995. Association of SARFH (sarcoma-associated RNA-binding fly homolog) with regions of chromatin transcribed by RNA polymerase II. Mol. Cell. Biol. 15:4562-71
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4562-4571
    • Immanuel, D.1    Zinszner, H.2    Ron, D.3
  • 47
    • 0031935157 scopus 로고    scopus 로고
    • EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: Interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes
    • Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L. 1998. EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes. Mol. Cell. Biol. 18:1489-97
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1489-1497
    • Bertolotti, A.1    Melot, T.2    Acker, J.3    Vigneron, M.4    Delattre, O.5    Tora, L.6
  • 48
    • 0028074607 scopus 로고
    • The EWS gene, involved in Ewing family of tumors, malignant melanoma of soft parts and desmoplastic small round cell tumors, codes for an RNA binding protein with novel regulatory domains
    • Ohno T, Ouchida M, Lee L, Gatalica Z, Rao VN, Reddy ES. 1994. The EWS gene, involved in Ewing family of tumors, malignant melanoma of soft parts and desmoplastic small round cell tumors, codes for an RNA binding protein with novel regulatory domains. Oncogene 9:3087-97
    • (1994) Oncogene , vol.9 , pp. 3087-3097
    • Ohno, T.1    Ouchida, M.2    Lee, L.3    Gatalica, Z.4    Rao, V.N.5    Reddy, E.S.6
  • 49
    • 0028200915 scopus 로고
    • An RNA-binding protein gene, TLS/FUS, is fused to ERG in human myeloid leukemia with t(16;21) chromosomal translocation
    • Ichikawa H, Shimizu K, Hayashi Y, Ohki M. 1994. An RNA-binding protein gene, TLS/FUS, is fused to ERG in human myeloid leukemia with t(16;21) chromosomal translocation. Cancer Res. 54:2865-68
    • (1994) Cancer Res. , vol.54 , pp. 2865-2868
    • Ichikawa, H.1    Shimizu, K.2    Hayashi, Y.3    Ohki, M.4
  • 50
    • 0035794162 scopus 로고    scopus 로고
    • Identification of an RNA binding specificity for the potential splicing factor TLS
    • Lerga A, Hallier M, Delva L, Orvain C, Gallais I, et al. 2001. Identification of an RNA binding specificity for the potential splicing factor TLS. J. Biol. Chem. 276:6807-16
    • (2001) J. Biol. Chem. , vol.276 , pp. 6807-6816
    • Lerga, A.1    Hallier, M.2    Delva, L.3    Orvain, C.4    Gallais, I.5
  • 52
    • 84868153116 scopus 로고    scopus 로고
    • FUS-SMN protein interactions link the motor neuron diseases ALS and SMA
    • Yamazaki T, Chen S, Yu Y, Yan B, Haertlein TC, et al. 2012. FUS-SMN protein interactions link the motor neuron diseases ALS and SMA. Cell Rep. 2:799-806
    • (2012) Cell Rep. , vol.2 , pp. 799-806
    • Yamazaki, T.1    Chen, S.2    Yu, Y.3    Yan, B.4    Haertlein, T.C.5
  • 53
    • 46649093597 scopus 로고    scopus 로고
    • Induced ncRNAs allosterically modify RNAbinding proteins in cis to inhibit transcription
    • Wang X, Arai S, Song X, Reichart D, Du K, et al. 2008. Induced ncRNAs allosterically modify RNAbinding proteins in cis to inhibit transcription. Nature 454:126-30
    • (2008) Nature , vol.454 , pp. 126-130
    • Wang, X.1    Arai, S.2    Song, X.3    Reichart, D.4    Du, K.5
  • 54
    • 84860863883 scopus 로고    scopus 로고
    • TDP-43 and FUS RNAbinding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their posttranscriptional fate in motoneuron-like cells
    • Colombrita C, Onesto E, Megiorni F, Pizzuti A, Baralle FE, et al. 2012. TDP-43 and FUS RNAbinding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their posttranscriptional fate in motoneuron-like cells. J. Biol. Chem. 287:15636-47
    • (2012) J. Biol. Chem. , vol.287 , pp. 15636-15647
    • Colombrita, C.1    Onesto, E.2    Megiorni, F.3    Pizzuti, A.4    Baralle, F.E.5
  • 55
    • 84864448921 scopus 로고    scopus 로고
    • Position-dependent FUS-RNA interactions regulate alternative splicing events and transcriptions
    • Ishigaki S, Masuda A, Fujioka Y, Iguchi Y, Katsuno M, et al. 2012. Position-dependent FUS-RNA interactions regulate alternative splicing events and transcriptions. Sci. Rep. 2:529
    • (2012) Sci. Rep. , vol.2 , pp. 529
    • Ishigaki, S.1    Masuda, A.2    Fujioka, Y.3    Iguchi, Y.4    Katsuno, M.5
  • 56
    • 84874531814 scopus 로고    scopus 로고
    • RNA-binding ability of FUSregulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations
    • Daigle JG, Lanson NA Jr, Smith RB, Casci I, Maltare A, et al. 2013. RNA-binding ability of FUSregulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations. Hum. Mol. Genet. 22:1193-205
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 1193-1205
    • Daigle, J.G.1    Lanson, N.A.2    Smith, R.B.3    Casci, I.4    Maltare, A.5
  • 57
    • 84866126892 scopus 로고    scopus 로고
    • Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain
    • Rogelj B, Easton LE, Bogu GK, Stanton LW, Rot G, et al. 2012. Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain. Sci. Rep. 2:603
    • (2012) Sci. Rep. , vol.2 , pp. 603
    • Rogelj, B.1    Easton, L.E.2    Bogu, G.K.3    Stanton, L.W.4    Rot, G.5
  • 58
    • 84868152371 scopus 로고    scopus 로고
    • Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs
    • Lagier-Tourenne C, Polymenidou M, Hutt KR, Vu AQ, Baughn M, et al. 2012. Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs. Nat. Neurosci. 15:1488-97
    • (2012) Nat. Neurosci , vol.15 , pp. 1488-1497
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Hutt, K.R.3    Vu, A.Q.4    Baughn, M.5
  • 59
    • 84889820285 scopus 로고    scopus 로고
    • Specific binding of modified RGGdomain in TLS/FUS toG-quadruplex RNA: Tyrosines inRGGdomain recognize 2′-OH of the riboses of loops in G-quadruplex
    • Takahama K, Oyoshi T. 2013. Specific binding of modified RGGdomain in TLS/FUS toG-quadruplex RNA: Tyrosines inRGGdomain recognize 2′-OH of the riboses of loops in G-quadruplex. J. Am. Chem. Soc. 135:18016-19
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 18016-18019
    • Takahama, K.1    Oyoshi, T.2
  • 60
    • 84880427394 scopus 로고    scopus 로고
    • A compendium of RNA-binding motifs for decoding gene regulation
    • Ray D, Kazan H, Cook KB, Weirauch MT, Najafabadi HS, et al. 2013. A compendium of RNA-binding motifs for decoding gene regulation. Nature 499:172-77
    • (2013) Nature , vol.499 , pp. 172-177
    • Ray, D.1    Kazan, H.2    Cook, K.B.3    Weirauch, M.T.4    Najafabadi, H.S.5
  • 61
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • Sun Z, Diaz Z, Fang X, Hart MP, Chesi A, et al. 2011. Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLOS Biol. 9:e1000614
    • (2011) PLOS Biol. , vol.9 , pp. e1000614
    • Sun, Z.1    Diaz, Z.2    Fang, X.3    Hart, M.P.4    Chesi, A.5
  • 62
    • 44449177217 scopus 로고    scopus 로고
    • RNA-binding proteinTLS is amajor nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells
    • Doi H, Okamura K, Bauer PO, Furukawa Y, Shimizu H, et al. 2008. RNA-binding proteinTLS is amajor nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells. J. Biol. Chem. 283:6489-500
    • (2008) J. Biol. Chem. , vol.283 , pp. 6489-6500
    • Doi, H.1    Okamura, K.2    Bauer, P.O.3    Furukawa, Y.4    Shimizu, H.5
  • 63
    • 77953699543 scopus 로고    scopus 로고
    • Identification of a self-association domain in the Ewing's sarcoma protein: A novel function for arginine-glycine-glycine rich motifs?
    • Shaw DJ, Morse R, Todd AG, Eggleton P, Lorson CL, Young PJ. 2010. Identification of a self-association domain in the Ewing's sarcoma protein: a novel function for arginine-glycine-glycine rich motifs? J. Biochem. 147:885-93
    • (2010) J. Biochem. , vol.147 , pp. 885-893
    • Shaw, D.J.1    Morse, R.2    Todd, A.G.3    Eggleton, P.4    Lorson, C.L.5    Young, P.J.6
  • 64
    • 84878565260 scopus 로고    scopus 로고
    • ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules
    • Vance C, Scotter EL, Nishimura AL, Troakes C, Mitchell JC, et al. 2013. ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules. Hum. Mol. Genet. 22:2676-88
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 2676-2688
    • Vance, C.1    Scotter, E.L.2    Nishimura, A.L.3    Troakes, C.4    Mitchell, J.C.5
  • 65
    • 84869005887 scopus 로고    scopus 로고
    • The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS
    • Yamaguchi A, Kitajo K. 2012. The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS. PLOS ONE 7:e49267
    • (2012) PLOS ONE , vol.7 , pp. e49267
    • Yamaguchi, A.1    Kitajo, K.2
  • 67
    • 77957867303 scopus 로고    scopus 로고
    • Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules
    • Bosco DA, Lemay N, Ko HK, Zhou H, Burke C, et al. 2010. Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum. Mol. Genet. 19:4160-75
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4160-4175
    • Bosco, D.A.1    Lemay, N.2    Ko, H.K.3    Zhou, H.4    Burke, C.5
  • 68
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C, Rogelj B, Hortobagyi T, De Vos KJ, Nishimura AL, et al. 2009. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323:1208-11
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3    De Vos, K.J.4    Nishimura, A.L.5
  • 69
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski TJ Jr, Bosco DA, Leclerc AL, Tamrazian E, Vanderburg CR, et al. 2009. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323:1205-8
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski, T.J.1    Bosco, D.A.2    Leclerc, A.L.3    Tamrazian, E.4    Vanderburg, C.R.5
  • 70
    • 79955495201 scopus 로고    scopus 로고
    • A yeast model of FUS/TLS-dependent cytotoxicity
    • Ju S, Tardiff DF, Han H, Divya K, Zhong Q, et al. 2011. A yeast model of FUS/TLS-dependent cytotoxicity. PLOS Biol. 9:e1001052
    • (2011) PLOS Biol. , vol.9 , pp. e1001052
    • Ju, S.1    Tardiff, D.F.2    Han, H.3    Divya, K.4    Zhong, Q.5
  • 72
    • 84884907673 scopus 로고    scopus 로고
    • TAF15 is important for cellular proliferation and regulates the expression of a subset of cell cycle genes through miRNAs
    • Ballarino M, Jobert L, Dembele D, de la Grange P, Auboeuf D, Tora L. 2013. TAF15 is important for cellular proliferation and regulates the expression of a subset of cell cycle genes through miRNAs. Oncogene 32:4646-55
    • (2013) Oncogene , vol.32 , pp. 4646-4655
    • Ballarino, M.1    Jobert, L.2    Dembele, D.3    De La Grange, P.4    Auboeuf, D.5    Tora, L.6
  • 73
    • 84871002507 scopus 로고    scopus 로고
    • FUS stimulates microRNA biogenesis by facilitating co-transcriptional Drosha recruitment
    • Morlando M, Dini Modigliani S, Torrelli G, Rosa A, Di Carlo V, et al. 2012. FUS stimulates microRNA biogenesis by facilitating co-transcriptional Drosha recruitment. EMBO J. 31:4502-10
    • (2012) EMBO J. , vol.31 , pp. 4502-4510
    • Morlando, M.1    Dini Modigliani, S.2    Torrelli, G.3    Rosa, A.4    Di Carlo, V.5
  • 74
    • 84890521089 scopus 로고    scopus 로고
    • A conserved N-terminal motif is required for complex formation between FUS, EWSR1, TAF15 and their oncogenic fusion proteins
    • Thomsen C, Grundevik P, Elias P, Stahlberg A, Aman P. 2013. A conserved N-terminal motif is required for complex formation between FUS, EWSR1, TAF15 and their oncogenic fusion proteins. FASEB J. 27:4965-74
    • (2013) FASEB J. , vol.27 , pp. 4965-4974
    • Thomsen, C.1    Grundevik, P.2    Elias, P.3    Stahlberg, A.4    Aman, P.5
  • 75
    • 59649111087 scopus 로고    scopus 로고
    • The unfolded protein response signals through high-order assembly of Ire1
    • Korennykh AV, Egea PF, Korostelev AA, Finer-Moore J, Zhang C, et al. 2009. The unfolded protein response signals through high-order assembly of Ire1. Nature 457:687-93
    • (2009) Nature , vol.457 , pp. 687-693
    • Korennykh, A.V.1    Egea, P.F.2    Korostelev, A.A.3    Finer-Moore, J.4    Zhang, C.5
  • 76
    • 84885411813 scopus 로고    scopus 로고
    • Allosteric regulation of DNA cleavage and sequence-specificity through run-on oligomerization
    • Lyumkis D, Talley H, Stewart A, Shah S, Park CK, et al. 2013. Allosteric regulation of DNA cleavage and sequence-specificity through run-on oligomerization. Structure 21:1848-58
    • (2013) Structure , vol.21 , pp. 1848-1858
    • Lyumkis, D.1    Talley, H.2    Stewart, A.3    Shah, S.4    Park, C.K.5
  • 77
    • 0038662666 scopus 로고    scopus 로고
    • Cooperative interaction of EWS with CREB-binding protein selectively activates hepatocyte nuclear factor 4-mediated transcription
    • Araya N, Hirota K, Shimamoto Y, Miyagishi M, Yoshida E, et al. 2003. Cooperative interaction of EWS with CREB-binding protein selectively activates hepatocyte nuclear factor 4-mediated transcription. J. Biol. Chem. 278:5427-32
    • (2003) J. Biol. Chem. , vol.278 , pp. 5427-5432
    • Araya, N.1    Hirota, K.2    Shimamoto, Y.3    Miyagishi, M.4    Yoshida, E.5
  • 78
    • 20344371441 scopus 로고    scopus 로고
    • Stimulation of Oct-4 activity by Ewing's sarcoma protein
    • Lee J, Rhee BK, Bae GY, Han YM, Kim J. 2005. Stimulation of Oct-4 activity by Ewing's sarcoma protein. Stem Cells 23:738-51
    • (2005) Stem Cells , vol.23 , pp. 738-751
    • Lee, J.1    Rhee, B.K.2    Bae, G.Y.3    Han, Y.M.4    Kim, J.5
  • 79
    • 73549089900 scopus 로고    scopus 로고
    • TLS inhibits RNA polymerase III transcription
    • Tan AY, Manley JL. 2010. TLS inhibits RNA polymerase III transcription. Mol. Cell. Biol. 30:186-96
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 186-196
    • Tan, A.Y.1    Manley, J.L.2
  • 80
    • 0034053964 scopus 로고    scopus 로고
    • TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins
    • Yang L, Embree LJ, Hickstein DD. 2000. TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins. Mol. Cell. Biol. 20:3345-54
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3345-3354
    • Yang, L.1    Embree, L.J.2    Hickstein, D.D.3
  • 81
    • 0035328667 scopus 로고    scopus 로고
    • Oncogenic TLS/ERG and EWS/FLI-1 fusion proteins inhibit RNA splicing mediated by YB-1 protein
    • Chansky HA, Hu M, Hickstein DD, Yang L. 2001. Oncogenic TLS/ERG and EWS/FLI-1 fusion proteins inhibit RNA splicing mediated by YB-1 protein. Cancer Res. 61:3586-90
    • (2001) Cancer Res. , vol.61 , pp. 3586-3590
    • Chansky, H.A.1    Hu, M.2    Hickstein, D.D.3    Yang, L.4
  • 82
    • 34250363024 scopus 로고    scopus 로고
    • SR proteins function in coupling RNAP II transcription to pre-mRNA splicing
    • Das R, Yu J, Zhang Z, Gygi MP, Krainer AR, et al. 2007. SR proteins function in coupling RNAP II transcription to pre-mRNA splicing. Mol. Cell 26:867-81
    • (2007) Mol. Cell , vol.26 , pp. 867-881
    • Das, R.1    Yu, J.2    Zhang, Z.3    Gygi, M.P.4    Krainer, A.R.5
  • 83
    • 0027276357 scopus 로고
    • Fusion of the dominant negative transcription regulator CHOP with a novel gene FUS by translocation t(12;16) in malignant liposarcoma
    • Rabbitts TH, Forster A, Larson R, Nathan P. 1993. Fusion of the dominant negative transcription regulator CHOP with a novel gene FUS by translocation t(12;16) in malignant liposarcoma. Nat. Genet. 4:175-80
    • (1993) Nat. Genet. , vol.4 , pp. 175-180
    • Rabbitts, T.H.1    Forster, A.2    Larson, R.3    Nathan, P.4
  • 85
    • 33745945163 scopus 로고    scopus 로고
    • TLS, EWS and TAF15: A model for transcriptional integration of gene expression
    • Law WJ, Cann KL, Hicks GG. 2006. TLS, EWS and TAF15: a model for transcriptional integration of gene expression. Brief Funct. Genomics Proteomics 5:8-14
    • (2006) Brief Funct. Genomics Proteomics , vol.5 , pp. 8-14
    • Law, W.J.1    Cann, K.L.2    Hicks, G.G.3
  • 86
    • 0032541042 scopus 로고    scopus 로고
    • The transcriptional repressor ZFM1 interacts with and modulates the ability of EWS to activate transcription
    • Zhang D, Paley AJ, Childs G. 1998. The transcriptional repressor ZFM1 interacts with and modulates the ability of EWS to activate transcription. J. Biol. Chem. 273:18086-91
    • (1998) J. Biol. Chem. , vol.273 , pp. 18086-18091
    • Zhang, D.1    Paley, A.J.2    Childs, G.3
  • 87
    • 0027362619 scopus 로고
    • The Ewing's sarcoma EWS/FLI-1 fusion gene encodes a more potent transcriptional activator and is a more powerful transforming gene than FLI-1
    • May WA, Lessnick SL, Braun BS, Klemsz M, Lewis BC, et al. 1993. The Ewing's sarcoma EWS/FLI-1 fusion gene encodes a more potent transcriptional activator and is a more powerful transforming gene than FLI-1. Mol. Cell. Biol. 13:7393-98
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7393-7398
    • May, W.A.1    Lessnick, S.L.2    Braun, B.S.3    Klemsz, M.4    Lewis, B.C.5
  • 88
    • 0033598946 scopus 로고    scopus 로고
    • The N-terminal domain of human TAFII68 displays transactivation and oncogenic properties
    • Bertolotti A, Bell B, Tora L. 1999. The N-terminal domain of human TAFII68 displays transactivation and oncogenic properties. Oncogene 18:8000-10
    • (1999) Oncogene , vol.18 , pp. 8000-8010
    • Bertolotti, A.1    Bell, B.2    Tora, L.3
  • 89
    • 40549086265 scopus 로고    scopus 로고
    • A transcriptional profiling meta-analysis reveals a core EWS-FLI gene expression signature
    • Hancock JD, Lessnick SL. 2008. A transcriptional profiling meta-analysis reveals a core EWS-FLI gene expression signature. Cell Cycle 7:250-56
    • (2008) Cell Cycle , vol.7 , pp. 250-256
    • Hancock, J.D.1    Lessnick, S.L.2
  • 90
    • 21744461721 scopus 로고    scopus 로고
    • The oncogenic TLS-ERG fusion protein exerts different effects in hematopoietic cells and fibroblasts
    • Zou J, Ichikawa H, Blackburn ML, Hu HM, Zielinska-Kwiatkowska A, et al. 2005. The oncogenic TLS-ERG fusion protein exerts different effects in hematopoietic cells and fibroblasts. Mol. Cell. Biol. 25:6235-46
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6235-6246
    • Zou, J.1    Ichikawa, H.2    Blackburn, M.L.3    Hu, H.M.4    Zielinska-Kwiatkowska, A.5
  • 91
    • 0034142209 scopus 로고    scopus 로고
    • Male sterility and enhanced radiation sensitivity in TLS-/-mice
    • Kuroda M, Sok J, Webb L, Baechtold H, Urano F, et al. 2000. Male sterility and enhanced radiation sensitivity in TLS-/-mice. EMBO J. 19:453-62
    • (2000) EMBO J. , vol.19 , pp. 453-462
    • Kuroda, M.1    Sok, J.2    Webb, L.3    Baechtold, H.4    Urano, F.5
  • 92
    • 0031915988 scopus 로고    scopus 로고
    • TLS (translocated-in-liposarcoma) is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors
    • Powers CA, Mathur M, Raaka BM, Ron D, Samuels HH. 1998. TLS (translocated-in-liposarcoma) is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors. Mol. Endocrinol. 12:4-18
    • (1998) Mol. Endocrinol. , vol.12 , pp. 4-18
    • Powers, C.A.1    Mathur, M.2    Raaka, B.M.3    Ron, D.4    Samuels, H.H.5
  • 93
    • 0032479980 scopus 로고    scopus 로고
    • TLS/FUS, a pro-oncogene involved in multiple chromosomal translocations, is a novel regulator of BCR/ABL-mediated leukemogenesis
    • Perrotti D, Bonatti S, Trotta R, Martinez R, Skorski T, et al. 1998. TLS/FUS, a pro-oncogene involved in multiple chromosomal translocations, is a novel regulator of BCR/ABL-mediated leukemogenesis. EMBO J. 17:4442-55
    • (1998) EMBO J. , vol.17 , pp. 4442-4455
    • Perrotti, D.1    Bonatti, S.2    Trotta, R.3    Martinez, R.4    Skorski, T.5
  • 94
    • 0030774839 scopus 로고    scopus 로고
    • The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain
    • Deloulme JC, Prichard L, Delattre O, Storm DR. 1997. The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain. J. Biol. Chem. 272:27369-77
    • (1997) J. Biol. Chem. , vol.272 , pp. 27369-27377
    • Deloulme, J.C.1    Prichard, L.2    Delattre, O.3    Storm, D.R.4
  • 95
    • 62049084331 scopus 로고    scopus 로고
    • O-GlcNAcylation is involved in the transcriptional activity of EWS-FLI1 in Ewing's sarcoma
    • Bachmaier R, Aryee DN, Jug G, Kauer M, Kreppel M, et al. 2009. O-GlcNAcylation is involved in the transcriptional activity of EWS-FLI1 in Ewing's sarcoma. Oncogene 28:1280-84
    • (2009) Oncogene , vol.28 , pp. 1280-1284
    • Bachmaier, R.1    Aryee, D.N.2    Jug, G.3    Kauer, M.4    Kreppel, M.5
  • 96
    • 63049100536 scopus 로고    scopus 로고
    • PRMT1mediated methylation ofTAF15 is required for its positive gene regulatory function
    • Jobert L, Argentini M, Tora L. 2009. PRMT1mediated methylation ofTAF15 is required for its positive gene regulatory function. Exp. Cell Res. 315:1273-86
    • (2009) Exp. Cell Res. , vol.315 , pp. 1273-1286
    • Jobert, L.1    Argentini, M.2    Tora, L.3
  • 98
    • 0042063647 scopus 로고    scopus 로고
    • Expression and subcellular localization of Ewing sarcoma (EWS) protein is affected by the methylation process
    • Belyanskaya LL, Delattre O, Gehring H. 2003. Expression and subcellular localization of Ewing sarcoma (EWS) protein is affected by the methylation process. Exp. Cell Res. 288:374-81
    • (2003) Exp. Cell Res. , vol.288 , pp. 374-381
    • Belyanskaya, L.L.1    Delattre, O.2    Gehring, H.3
  • 99
    • 0034353182 scopus 로고    scopus 로고
    • EWS.Fli1 fusion protein interactswith hyperphosphorylated RNA polymerase II and interferes with serine-arginine protein-mediated RNA splicing
    • Yang L, Chansky HA, Hickstein DD. 2000. EWS.Fli1 fusion protein interactswith hyperphosphorylated RNA polymerase II and interferes with serine-arginine protein-mediated RNA splicing. J. Biol. Chem. 275:37612-18
    • (2000) J. Biol. Chem. , vol.275 , pp. 37612-37618
    • Yang, L.1    Chansky, H.A.2    Hickstein, D.D.3
  • 100
    • 0032570707 scopus 로고    scopus 로고
    • The transcription factor Spi- 1/PU.1 interacts with the potential splicing factor TLS
    • Hallier M, Lerga A, Barnache S, Tavitian A, Moreau-Gachelin F. 1998. The transcription factor Spi- 1/PU.1 interacts with the potential splicing factor TLS. J. Biol. Chem. 273:4838-42
    • (1998) J. Biol. Chem. , vol.273 , pp. 4838-4842
    • Hallier, M.1    Lerga, A.2    Barnache, S.3    Tavitian, A.4    Moreau-Gachelin, F.5
  • 101
    • 0035918291 scopus 로고    scopus 로고
    • Involvement of the prooncoprotein TLS (translocated in liposarcoma) in nuclear factor κb p65-mediated transcription as a coactivator
    • Uranishi H, Tetsuka T, Yamashita M, Asamitsu K, Shimizu M, et al. 2001. Involvement of the prooncoprotein TLS (translocated in liposarcoma) in nuclear factor κB p65-mediated transcription as a coactivator. J. Biol. Chem. 276:13395-401
    • (2001) J. Biol. Chem. , vol.276 , pp. 13395-13401
    • Uranishi, H.1    Tetsuka, T.2    Yamashita, M.3    Asamitsu, K.4    Shimizu, M.5
  • 102
    • 0034619768 scopus 로고    scopus 로고
    • Liposarcoma initiated by FUS/TLS-CHOP: The FUS/TLS domain plays a critical role in the pathogenesis of liposarcoma
    • Pérez-Losada J, Sánchez-Martín M, Rodríguez-García MA, Pérez-Mancera PA, Pintado B, et al. 2000. Liposarcoma initiated by FUS/TLS-CHOP: The FUS/TLS domain plays a critical role in the pathogenesis of liposarcoma. Oncogene 19:6015-22
    • (2000) Oncogene , vol.19 , pp. 6015-6022
    • Pérez-Losada, J.1    Sánchez-Martín, M.2    Rodríguez-García, M.A.3    Pérez-Mancera, P.A.4    Pintado, B.5
  • 103
    • 0032694087 scopus 로고    scopus 로고
    • Dual transforming activities of the FUS (TLS)-ERG leukemia fusion protein conferred by two N-terminal domains of FUS (TLS)
    • Ichikawa H, Shimizu K, Katsu R, Ohki M. 1999. Dual transforming activities of the FUS (TLS)-ERG leukemia fusion protein conferred by two N-terminal domains of FUS (TLS). Mol. Cell. Biol. 19:7639-50
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7639-7650
    • Ichikawa, H.1    Shimizu, K.2    Katsu, R.3    Ohki, M.4
  • 104
    • 0027948152 scopus 로고
    • TLS/FUS fusion domain of TLS/FUS-erg chimeric protein resulting from the t(16;21) chromosomal translocation in human myeloid leukemia functions as a transcriptional activation domain
    • Prasad DD, Ouchida M, Lee L, Rao VN, Reddy ES. 1994. TLS/FUS fusion domain of TLS/FUS-erg chimeric protein resulting from the t(16;21) chromosomal translocation in human myeloid leukemia functions as a transcriptional activation domain. Oncogene 9:3717-29
    • (1994) Oncogene , vol.9 , pp. 3717-3729
    • Prasad, D.D.1    Ouchida, M.2    Lee, L.3    Rao, V.N.4    Reddy, E.S.5
  • 105
    • 0036791118 scopus 로고    scopus 로고
    • Recurrent rearrangement of the Ewing's sarcoma gene, EWSR1, or its homologue, TAF15, with the transcription factor CIZ/NMP4 in acute leukemia
    • Martini A, La Starza R, Janssen H, Bilhou-Nabera C, Corveleyn A, et al. 2002. Recurrent rearrangement of the Ewing's sarcoma gene, EWSR1, or its homologue, TAF15, with the transcription factor CIZ/NMP4 in acute leukemia. Cancer Res. 62:5408-12
    • (2002) Cancer Res. , vol.62 , pp. 5408-5412
    • Martini, A.1    La Starza, R.2    Janssen, H.3    Bilhou-Nabera, C.4    Corveleyn, A.5
  • 106
    • 13044289315 scopus 로고    scopus 로고
    • Induction of a secreted protein by the myxoid liposarcoma oncogene
    • Kuroda M, Wang X, Sok J, Yin Y, Chung P, et al. 1999. Induction of a secreted protein by the myxoid liposarcoma oncogene. PNAS 96:5025-30
    • (1999) PNAS , vol.96 , pp. 5025-5030
    • Kuroda, M.1    Wang, X.2    Sok, J.3    Yin, Y.4    Chung, P.5
  • 107
    • 0029004567 scopus 로고
    • Identification of target genes for the Ewing's sarcoma EWS/FLI fusion protein by representational difference analysis
    • Braun BS, Frieden R, Lessnick SL, May WA, Denny CT. 1995. Identification of target genes for the Ewing's sarcoma EWS/FLI fusion protein by representational difference analysis. Mol. Cell. Biol. 15:4623-30
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4623-4630
    • Braun, B.S.1    Frieden, R.2    Lessnick, S.L.3    May, W.A.4    Denny, C.T.5
  • 108
    • 79960925229 scopus 로고    scopus 로고
    • TheEwing sarcoma protein regulatesDNA damage-induced alternative splicing
    • Paronetto MP, Minana B, Valcarcel J. 2011. TheEwing sarcoma protein regulatesDNA damage-induced alternative splicing. Mol. Cell 43:353-68
    • (2011) Mol. Cell , vol.43 , pp. 353-368
    • Paronetto, M.P.1    Minana, B.2    Valcarcel, J.3
  • 109
    • 0344407006 scopus 로고    scopus 로고
    • Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRM160, and SR proteins
    • Meissner M, Lopato S, Gotzmann J, Sauermann G, Barta A. 2003. Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRM160, and SR proteins. Exp. Cell Res. 283:184-95
    • (2003) Exp. Cell Res. , vol.283 , pp. 184-195
    • Meissner, M.1    Lopato, S.2    Gotzmann, J.3    Sauermann, G.4    Barta, A.5
  • 110
    • 65549147264 scopus 로고    scopus 로고
    • DNA damage regulates alternative splicing through inhibition of RNA polymerase II elongation
    • Muñoz MJ, Pérez-Santangelo MS, Paronetto MP, de la Mata M, Pelisch F, et al. 2009. DNA damage regulates alternative splicing through inhibition of RNA polymerase II elongation. Cell 137:708-20
    • (2009) Cell , vol.137 , pp. 708-720
    • Muñoz, M.J.1    Pérez-Santangelo, M.S.2    Paronetto, M.P.3    De La Mata, M.4    Pelisch, F.5
  • 111
    • 80055038803 scopus 로고    scopus 로고
    • A fraction of the transcription factor TAF15 participates in interactions with a subset of the spliceosomal U1 snRNP complex
    • Leichter M, Marko M, Ganou V, Patrinou-Georgoula M, Tora L, Guialis A. 2011. A fraction of the transcription factor TAF15 participates in interactions with a subset of the spliceosomal U1 snRNP complex. Biochim. Biophys. Acta 1814:1812-24
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 1812-1824
    • Leichter, M.1    Marko, M.2    Ganou, V.3    Patrinou-Georgoula, M.4    Tora, L.5    Guialis, A.6
  • 112
    • 2542477014 scopus 로고    scopus 로고
    • RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers
    • de Hoog CL, Foster LJ, Mann M. 2004. RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers. Cell 117:649-62
    • (2004) Cell , vol.117 , pp. 649-662
    • De Hoog, C.L.1    Foster, L.J.2    Mann, M.3
  • 114
    • 77954214646 scopus 로고    scopus 로고
    • Analysis of SMN-neurite granules: Core Cajal body components are absent from SMN-cytoplasmic complexes
    • Todd AG, Morse R, Shaw DJ, Stebbings H, Young PJ. 2010. Analysis of SMN-neurite granules: Core Cajal body components are absent from SMN-cytoplasmic complexes. Biochem. Biophys. Res. Commun. 397:479-85
    • (2010) Biochem. Biophys. Res. Commun. , vol.397 , pp. 479-485
    • Todd, A.G.1    Morse, R.2    Shaw, D.J.3    Stebbings, H.4    Young, P.J.5
  • 115
    • 84873314088 scopus 로고    scopus 로고
    • Spliceosome integrity is defective in the motor neuron diseases ALS and SMA
    • Tsuiji H, Iguchi Y, Furuya A, Kataoka A, Hatsuta H, et al. 2013. Spliceosome integrity is defective in the motor neuron diseases ALS and SMA. EMBO Mol. Med. 5:221-34
    • (2013) EMBO Mol. Med. , vol.5 , pp. 221-234
    • Tsuiji, H.1    Iguchi, Y.2    Furuya, A.3    Kataoka, A.4    Hatsuta, H.5
  • 116
    • 84862149527 scopus 로고    scopus 로고
    • FET proteins in frontotemporal dementia and amyotrophic lateral sclerosis
    • Mackenzie IR, Neumann M. 2012. FET proteins in frontotemporal dementia and amyotrophic lateral sclerosis. Brain Res. 1462:40-43
    • (2012) Brain Res. , vol.1462 , pp. 40-43
    • Mackenzie, I.R.1    Neumann, M.2
  • 117
    • 80052959701 scopus 로고    scopus 로고
    • FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations
    • Neumann M, Bentmann E, Dormann D, Jawaid A, DeJesus-Hernandez M, et al. 2011. FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations. Brain 134:2595-609
    • (2011) Brain , vol.134 , pp. 2595-2609
    • Neumann, M.1    Bentmann, E.2    Dormann, D.3    Jawaid, A.4    Dejesus-Hernandez, M.5
  • 118
    • 79959354904 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in the C-terminal nuclear localization and retention signal (C-NLS) of the EWSprotein
    • Leemann-Zakaryan RP, Pahlich S, Grossenbacher D, Gehring H. 2011. Tyrosine phosphorylation in the C-terminal nuclear localization and retention signal (C-NLS) of the EWSprotein. Sarcoma 2011:218483
    • (2011) Sarcoma , vol.2011 , pp. 218483
    • Leemann-Zakaryan, R.P.1    Pahlich, S.2    Grossenbacher, D.3    Gehring, H.4
  • 119
    • 84864366184 scopus 로고    scopus 로고
    • Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)
    • Zhang ZC, Chook YM. 2012. Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS). PNAS 109:12017-21
    • (2012) PNAS , vol.109 , pp. 12017-12021
    • Zhang, Z.C.1    Chook, Y.M.2
  • 120
    • 84869237956 scopus 로고    scopus 로고
    • Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS
    • Dormann D, Madl T, Valori CF, Bentmann E, Tahirovic S, et al. 2012. Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS. EMBO J. 31:4258-75
    • (2012) EMBO J. , vol.31 , pp. 4258-4275
    • Dormann, D.1    Madl, T.2    Valori, C.F.3    Bentmann, E.4    Tahirovic, S.5
  • 121
    • 84876437828 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo
    • Scaramuzzino C, Monaghan J, Milioto C, Lanson NA Jr, Maltare A, et al. 2013. Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo. PLOS ONE 8:e61576
    • (2013) PLOS ONE , vol.8 , pp. e61576
    • Scaramuzzino, C.1    Monaghan, J.2    Milioto, C.3    Lanson, N.A.4    Maltare, A.5
  • 122
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • Tradewell ML, Yu Z, Tibshirani M, Boulanger MC, Durham HD, Richard S. 2012. Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations. Hum. Mol. Genet. 21:136-49
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.2    Tibshirani, M.3    Boulanger, M.C.4    Durham, H.D.5    Richard, S.6
  • 123
    • 0035378344 scopus 로고    scopus 로고
    • Exposure on cell surface and extensive arginine methylation of Ewing sarcoma (EWS) protein
    • Belyanskaya LL, Gehrig PM, Gehring H. 2001. Exposure on cell surface and extensive arginine methylation of Ewing sarcoma (EWS) protein. J. Biol. Chem. 276:18681-87
    • (2001) J. Biol. Chem. , vol.276 , pp. 18681-18687
    • Belyanskaya, L.L.1    Gehrig, P.M.2    Gehring, H.3
  • 125
    • 30544448358 scopus 로고    scopus 로고
    • TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines
    • Fujii R, Takumi T. 2005. TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines. J. Cell Sci. 118:5755-65
    • (2005) J. Cell Sci. , vol.118 , pp. 5755-5765
    • Fujii, R.1    Takumi, T.2
  • 126
    • 15744378126 scopus 로고    scopus 로고
    • The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology
    • Fujii R, Okabe S, Urushido T, Inoue K, Yoshimura A, et al. 2005. The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology. Curr. Biol. 15:587-93
    • (2005) Curr. Biol. , vol.15 , pp. 587-593
    • Fujii, R.1    Okabe, S.2    Urushido, T.3    Inoue, K.4    Yoshimura, A.5
  • 127
    • 48249083430 scopus 로고    scopus 로고
    • The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response
    • Andersson MK, Stahlberg A, Arvidsson Y, Olofsson A, Semb H, et al. 2008. The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response. BMC Cell Biol. 9:37
    • (2008) BMC Cell Biol. , vol.9 , pp. 37
    • Andersson, M.K.1    Stahlberg, A.2    Arvidsson, Y.3    Olofsson, A.4    Semb, H.5
  • 128
    • 84890819735 scopus 로고    scopus 로고
    • The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules
    • Yasuda K, Zhang H, Loiselle D, Haystead T, Macara IG, Mili S. 2013. The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules. J. Cell Biol. 203:737-46
    • (2013) J. Cell Biol. , vol.203 , pp. 737-746
    • Yasuda, K.1    Zhang, H.2    Loiselle, D.3    Haystead, T.4    Macara, I.G.5    Mili, S.6
  • 129
    • 84881220788 scopus 로고    scopus 로고
    • FUS/TLS assembles into stress granules and is a prosurvival factor during hyperosmolar stress
    • Sama RR, Ward CL, Kaushansky LJ, Lemay N, Ishigaki S, et al. 2013. FUS/TLS assembles into stress granules and is a prosurvival factor during hyperosmolar stress. J. Cell Physiol. 228:2222-31
    • (2013) J. Cell Physiol. , vol.228 , pp. 2222-2231
    • Sama, R.R.1    Ward, C.L.2    Kaushansky, L.J.3    Lemay, N.4    Ishigaki, S.5
  • 130
  • 131
    • 84882801549 scopus 로고    scopus 로고
    • Altered ribostasis: RNA-protein granules in degenerative disorders
    • Ramaswami M, Taylor JP, Parker R. 2013. Altered ribostasis: RNA-protein granules in degenerative disorders. Cell 154:727-36
    • (2013) Cell , vol.154 , pp. 727-736
    • Ramaswami, M.1    Taylor, J.P.2    Parker, R.3
  • 135
    • 79952585425 scopus 로고    scopus 로고
    • Mutational analysis reveals the FUS homolog TAF15 as a candidate gene for familial amyotrophic lateral sclerosis
    • Ticozzi N, Vance C, Leclerc AL, Keagle P, Glass JD, et al. 2011. Mutational analysis reveals the FUS homolog TAF15 as a candidate gene for familial amyotrophic lateral sclerosis. Am. J. Med. Genet. B 156:285-90
    • (2011) Am. J. Med. Genet. B , vol.156 , pp. 285-290
    • Ticozzi, N.1    Vance, C.2    Leclerc, A.L.3    Keagle, P.4    Glass, J.D.5
  • 136
    • 84907489769 scopus 로고    scopus 로고
    • Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms
    • Shelkovnikova TA, Robinson HK, Southcombe JA, Ninkina N, Buchman VL. 2014. Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms. Hum. Mol. Genet. 23:2511-26
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 2511-2526
    • Shelkovnikova, T.A.1    Robinson, H.K.2    Southcombe, J.A.3    Ninkina, N.4    Buchman, V.L.5
  • 137
    • 84883149037 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-linked FUS/TLS alters stress granule assembly and dynamics
    • Baron DM, Kaushansky LJ, Ward CL, Sama RR, Chian RJ, et al. 2013. Amyotrophic lateral sclerosis-linked FUS/TLS alters stress granule assembly and dynamics. Mol. Neurodegener. 8:30
    • (2013) Mol. Neurodegener , vol.8 , pp. 30
    • Baron, D.M.1    Kaushansky, L.J.2    Ward, C.L.3    Sama, R.R.4    Chian, R.J.5
  • 138
    • 84902291718 scopus 로고    scopus 로고
    • The role of FUS gene variants in neurodegenerative diseases
    • Deng H, Gao K, Jankovic J. 2014. The role of FUS gene variants in neurodegenerative diseases. Nat. Rev. Neurol. 10:337-48
    • (2014) Nat. Rev. Neurol. , vol.10 , pp. 337-348
    • Deng, H.1    Gao, K.2    Jankovic, J.3
  • 139
    • 70350156915 scopus 로고    scopus 로고
    • Analysis of FUS gene mutation in familial amyotrophic lateral sclerosis within an Italian cohort
    • Ticozzi N, Silani V, LeClerc AL, Keagle P, Gellera C, et al. 2009. Analysis of FUS gene mutation in familial amyotrophic lateral sclerosis within an Italian cohort. Neurology 73:1180-85
    • (2009) Neurology , vol.73 , pp. 1180-1185
    • Ticozzi, N.1    Silani, V.2    Leclerc, A.L.3    Keagle, P.4    Gellera, C.5
  • 140
    • 79551472601 scopus 로고    scopus 로고
    • Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS
    • Ito D, Seki M, Tsunoda Y, Uchiyama H, Suzuki N. 2010. Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS. Ann. Neurol. 69:152-62
    • (2010) Ann. Neurol. , vol.69 , pp. 152-162
    • Ito, D.1    Seki, M.2    Tsunoda, Y.3    Uchiyama, H.4    Suzuki, N.5
  • 142
    • 80052374038 scopus 로고    scopus 로고
    • FUS and TARDBP but not SOD1 interact in genetic models of amyotrophic lateral sclerosis
    • Kabashi E, Bercier V, Lissouba A, Liao M, Brustein E, et al. 2011. FUS and TARDBP but not SOD1 interact in genetic models of amyotrophic lateral sclerosis. PLOS Genet. 7:e1002214
    • (2011) PLOS Genet. , vol.7 , pp. e1002214
    • Kabashi, E.1    Bercier, V.2    Lissouba, A.3    Liao, M.4    Brustein, E.5
  • 143
    • 84896799718 scopus 로고    scopus 로고
    • ALS-associated mutation FUS-R521C causes DNA damage and RNA splicing defects
    • Qiu H, Lee S, Shang Y, Wang WY, Au KF, et al. 2014. ALS-associated mutation FUS-R521C causes DNA damage and RNA splicing defects. J. Clin. Investig. 124:981-99
    • (2014) J. Clin. Investig. , vol.124 , pp. 981-999
    • Qiu, H.1    Lee, S.2    Shang, Y.3    Wang, W.Y.4    Au, K.F.5
  • 144
    • 84884902129 scopus 로고    scopus 로고
    • Interaction of FUS and HDAC1 regulates DNA damage response and repair in neurons
    • Wang WY, Pan L, Su SC, Quinn EJ, Sasaki M, et al. 2013. Interaction of FUS and HDAC1 regulates DNA damage response and repair in neurons. Nat. Neurosci. 16:1383-91
    • (2013) Nat. Neurosci. , vol.16 , pp. 1383-1391
    • Wang, W.Y.1    Pan, L.2    Su, S.C.3    Quinn, E.J.4    Sasaki, M.5
  • 145
    • 84883136968 scopus 로고    scopus 로고
    • The RNA-binding protein fused in sarcoma (FUS) functions downstream of poly(ADP-ribose) polymerase (PARP) in response to DNA damage
    • Mastrocola AS, Kim SH, Trinh AT, Rodenkirch LA, Tibbetts RS. 2013. The RNA-binding protein fused in sarcoma (FUS) functions downstream of poly(ADP-ribose) polymerase (PARP) in response to DNA damage. J. Biol. Chem. 288:24731-41
    • (2013) J. Biol. Chem. , vol.288 , pp. 24731-24741
    • Mastrocola, A.S.1    Kim, S.H.2    Trinh, A.T.3    Rodenkirch, L.A.4    Tibbetts, R.S.5
  • 146
    • 84887435150 scopus 로고    scopus 로고
    • Combining PARP-1 inhibition and radiation in Ewing sarcoma results in lethal DNA damage
    • Lee HJ, Yoon C, Schmidt B, Park DJ, Zhang AY, et al. 2013. Combining PARP-1 inhibition and radiation in Ewing sarcoma results in lethal DNA damage. Mol. Cancer Ther. 12:2591-600
    • (2013) Mol. Cancer Ther. , vol.12 , pp. 2591-2600
    • Lee, H.J.1    Yoon, C.2    Schmidt, B.3    Park, D.J.4    Zhang, A.Y.5
  • 147
    • 34248203558 scopus 로고    scopus 로고
    • Ewing sarcoma gene EWS is essential for meiosis and B lymphocyte development
    • Li H, Watford W, Li C, Parmelee A, Bryant MA, et al. 2007. Ewing sarcoma gene EWS is essential for meiosis and B lymphocyte development. J. Clin. Investig. 117:1314-23
    • (2007) J. Clin. Investig. , vol.117 , pp. 1314-1323
    • Li, H.1    Watford, W.2    Li, C.3    Parmelee, A.4    Bryant, M.A.5
  • 148
    • 0033968408 scopus 로고    scopus 로고
    • Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death
    • Hicks GG, Singh N, Nashabi A, Mai S, Bozek G, et al. 2000. Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death. Nat. Genet. 24:175-79
    • (2000) Nat. Genet. , vol.24 , pp. 175-179
    • Hicks, G.G.1    Singh, N.2    Nashabi, A.3    Mai, S.4    Bozek, G.5
  • 149
    • 77954485095 scopus 로고    scopus 로고
    • FET family proto-oncogene Fus contributes to self-renewal of hematopoietic stem cells
    • Sugawara T, Oguro H, Negishi M, Morita Y, Ichikawa H, et al. 2010. FET family proto-oncogene Fus contributes to self-renewal of hematopoietic stem cells. Exp. Hematol. 38:696-706
    • (2010) Exp. Hematol. , vol.38 , pp. 696-706
    • Sugawara, T.1    Oguro, H.2    Negishi, M.3    Morita, Y.4    Ichikawa, H.5
  • 150
    • 84859391984 scopus 로고    scopus 로고
    • PARP-1 inhibition as a targeted strategy to treat Ewing's sarcoma
    • Brenner JC, Feng FY, Han S, Patel S, Goyal SV, et al. 2012. PARP-1 inhibition as a targeted strategy to treat Ewing's sarcoma. Cancer Res. 72:1608-13
    • (2012) Cancer Res. , vol.72 , pp. 1608-1613
    • Brenner, J.C.1    Feng, F.Y.2    Han, S.3    Patel, S.4    Goyal, S.V.5
  • 151
    • 46049090743 scopus 로고    scopus 로고
    • Nuclear trafficking of pro-apoptotic kinases in response to DNA damage
    • Yoshida K. 2008. Nuclear trafficking of pro-apoptotic kinases in response to DNA damage. Trends Mol. Med. 14:305-13
    • (2008) Trends Mol. Med. , vol.14 , pp. 305-313
    • Yoshida, K.1


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