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Volumn 39, Issue 3, 2014, Pages 141-149

DNA damage: RNA-binding proteins protect from near and far

Author keywords

DNA damage response; MRNA translation; Post transcriptional control of gene expression; RNA processing

Indexed keywords

LONG UNTRANSLATED RNA; RNA BINDING PROTEIN; UNTRANSLATED RNA;

EID: 84896716550     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2014.01.003     Document Type: Review
Times cited : (97)

References (90)
  • 2
    • 44449166478 scopus 로고    scopus 로고
    • RNA-binding proteins and post-transcriptional gene regulation
    • Glisovic T., et al. RNA-binding proteins and post-transcriptional gene regulation. FEBS Lett. 2008, 582:1977-1986.
    • (2008) FEBS Lett. , vol.582 , pp. 1977-1986
    • Glisovic, T.1
  • 3
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: modular design for efficient function
    • Lunde B.M., et al. RNA-binding proteins: modular design for efficient function. Nat. Rev. Mol. Cell Biol. 2007, 8:479-490.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 479-490
    • Lunde, B.M.1
  • 4
    • 84886246082 scopus 로고    scopus 로고
    • Proteome-wide identification of poly(ADP-ribosyl)ation targets in different genotoxic stress responses
    • Jungmichel S., et al. Proteome-wide identification of poly(ADP-ribosyl)ation targets in different genotoxic stress responses. Mol. Cell 2013, 52:272-285.
    • (2013) Mol. Cell , vol.52 , pp. 272-285
    • Jungmichel, S.1
  • 5
    • 34249947699 scopus 로고    scopus 로고
    • ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage
    • Matsuoka S., et al. ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science 2007, 316:1160-1166.
    • (2007) Science , vol.316 , pp. 1160-1166
    • Matsuoka, S.1
  • 6
    • 84857781943 scopus 로고    scopus 로고
    • A genome-wide homologous recombination screen identifies the RNA-binding protein RBMX as a component of the DNA-damage response
    • Adamson B., et al. A genome-wide homologous recombination screen identifies the RNA-binding protein RBMX as a component of the DNA-damage response. Nat. Cell Biol. 2012, 14:318-328.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 318-328
    • Adamson, B.1
  • 7
    • 67651119997 scopus 로고    scopus 로고
    • A genome-wide siRNA screen reveals diverse cellular processes and pathways that mediate genome stability
    • Paulsen R.D., et al. A genome-wide siRNA screen reveals diverse cellular processes and pathways that mediate genome stability. Mol. Cell 2009, 35:228-239.
    • (2009) Mol. Cell , vol.35 , pp. 228-239
    • Paulsen, R.D.1
  • 8
    • 0035831030 scopus 로고    scopus 로고
    • The BARD1-CstF-50 interaction links mRNA 3' end formation to DNA damage and tumor suppression
    • Kleiman F.E., Manley J.L. The BARD1-CstF-50 interaction links mRNA 3' end formation to DNA damage and tumor suppression. Cell 2001, 104:743-753.
    • (2001) Cell , vol.104 , pp. 743-753
    • Kleiman, F.E.1    Manley, J.L.2
  • 9
    • 41849095683 scopus 로고    scopus 로고
    • The 3' processing factor CstF functions in the DNA repair response
    • Mirkin N., et al. The 3' processing factor CstF functions in the DNA repair response. Nucleic Acids Res. 2008, 36:1792-1804.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 1792-1804
    • Mirkin, N.1
  • 10
    • 79960054172 scopus 로고    scopus 로고
    • P53 inhibits mRNA 3' processing through its interaction with the CstF/BARD1 complex
    • Nazeer F.I., et al. p53 inhibits mRNA 3' processing through its interaction with the CstF/BARD1 complex. Oncogene 2011, 30:3073-3083.
    • (2011) Oncogene , vol.30 , pp. 3073-3083
    • Nazeer, F.I.1
  • 11
    • 80052801997 scopus 로고    scopus 로고
    • The emerging role of pre-messenger RNA splicing in stress responses: sending alternative messages and silent messengers
    • Dutertre M., et al. The emerging role of pre-messenger RNA splicing in stress responses: sending alternative messages and silent messengers. RNA Biol. 2011, 8:740-747.
    • (2011) RNA Biol. , vol.8 , pp. 740-747
    • Dutertre, M.1
  • 12
    • 79952266577 scopus 로고    scopus 로고
    • Global impact of RNA polymerase II elongation inhibition on alternative splicing regulation
    • Ip J.Y., et al. Global impact of RNA polymerase II elongation inhibition on alternative splicing regulation. Genome Res. 2011, 21:390-401.
    • (2011) Genome Res. , vol.21 , pp. 390-401
    • Ip, J.Y.1
  • 13
    • 0036677451 scopus 로고    scopus 로고
    • Global analysis of stress-regulated mRNA turnover by using cDNA arrays
    • Fan J., et al. Global analysis of stress-regulated mRNA turnover by using cDNA arrays. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:10611-10616.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10611-10616
    • Fan, J.1
  • 14
    • 70350545723 scopus 로고    scopus 로고
    • Regulation of protein synthesis by ionizing radiation
    • Braunstein S., et al. Regulation of protein synthesis by ionizing radiation. Mol. Cell. Biol. 2009, 29:5645-5656.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5645-5656
    • Braunstein, S.1
  • 15
    • 84862116855 scopus 로고    scopus 로고
    • Coupled activation and degradation of eEF2K regulates protein synthesis in response to genotoxic stress
    • Kruiswijk F., et al. Coupled activation and degradation of eEF2K regulates protein synthesis in response to genotoxic stress. Sci. Signal. 2012, 5:ra40.
    • (2012) Sci. Signal. , vol.5
    • Kruiswijk, F.1
  • 16
    • 31544442938 scopus 로고    scopus 로고
    • Radiation-induced changes in gene expression involve recruitment of existing messenger RNAs to and away from polysomes
    • Lu X., et al. Radiation-induced changes in gene expression involve recruitment of existing messenger RNAs to and away from polysomes. Cancer Res. 2006, 66:1052-1061.
    • (2006) Cancer Res. , vol.66 , pp. 1052-1061
    • Lu, X.1
  • 17
    • 79952754428 scopus 로고    scopus 로고
    • Global dissociation of HuR-mRNA complexes promotes cell survival after ionizing radiation
    • Masuda K., et al. Global dissociation of HuR-mRNA complexes promotes cell survival after ionizing radiation. EMBO J. 2011, 30:1040-1053.
    • (2011) EMBO J. , vol.30 , pp. 1040-1053
    • Masuda, K.1
  • 18
    • 79951500251 scopus 로고    scopus 로고
    • The ATM kinase induces microRNA biogenesis in the DNA damage response
    • Zhang X., et al. The ATM kinase induces microRNA biogenesis in the DNA damage response. Mol. Cell 2011, 41:371-383.
    • (2011) Mol. Cell , vol.41 , pp. 371-383
    • Zhang, X.1
  • 19
    • 84869216705 scopus 로고    scopus 로고
    • DNA damage and eIF4G1 in breast cancer cells reprogram translation for survival and DNA repair mRNAs
    • Badura M., et al. DNA damage and eIF4G1 in breast cancer cells reprogram translation for survival and DNA repair mRNAs. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:18767-18772.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 18767-18772
    • Badura, M.1
  • 20
    • 45549085644 scopus 로고    scopus 로고
    • Radiation-induced gene translation profiles reveal tumor type and cancer-specific components
    • Kumaraswamy S., et al. Radiation-induced gene translation profiles reveal tumor type and cancer-specific components. Cancer Res. 2008, 68:3819-3826.
    • (2008) Cancer Res. , vol.68 , pp. 3819-3826
    • Kumaraswamy, S.1
  • 21
    • 66149137639 scopus 로고    scopus 로고
    • Translational reprogramming following UVB irradiation is mediated by DNA-PKcs and allows selective recruitment to the polysomes of mRNAs encoding DNA repair enzymes
    • Powley I.R., et al. Translational reprogramming following UVB irradiation is mediated by DNA-PKcs and allows selective recruitment to the polysomes of mRNAs encoding DNA repair enzymes. Genes Dev. 2009, 23:1207-1220.
    • (2009) Genes Dev. , vol.23 , pp. 1207-1220
    • Powley, I.R.1
  • 22
    • 79551595610 scopus 로고    scopus 로고
    • Essential role for the interaction between hnRNP H/F and a G quadruplex in maintaining p53 pre-mRNA 3'-end processing and function during DNA damage
    • Decorsiere A., et al. Essential role for the interaction between hnRNP H/F and a G quadruplex in maintaining p53 pre-mRNA 3'-end processing and function during DNA damage. Genes Dev. 2011, 25:220-225.
    • (2011) Genes Dev. , vol.25 , pp. 220-225
    • Decorsiere, A.1
  • 23
    • 51049124035 scopus 로고    scopus 로고
    • P53 mRNA controls p53 activity by managing Mdm2 functions
    • Candeias M.M., et al. P53 mRNA controls p53 activity by managing Mdm2 functions. Nat. Cell Biol. 2008, 10:1098-1105.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1098-1105
    • Candeias, M.M.1
  • 24
    • 47749090521 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein regulates IRES-mediated translation of p53 isoforms
    • Grover R., et al. Polypyrimidine tract binding protein regulates IRES-mediated translation of p53 isoforms. Cell Cycle 2008, 7:2189-2198.
    • (2008) Cell Cycle , vol.7 , pp. 2189-2198
    • Grover, R.1
  • 25
    • 0038153919 scopus 로고    scopus 로고
    • RNA-binding protein HuR enhances p53 translation in response to ultraviolet light irradiation
    • Mazan-Mamczarz K., et al. RNA-binding protein HuR enhances p53 translation in response to ultraviolet light irradiation. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:8354-8359.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 8354-8359
    • Mazan-Mamczarz, K.1
  • 26
    • 26244459242 scopus 로고    scopus 로고
    • Regulation of p53 translation and induction after DNA damage by ribosomal protein L26 and nucleolin
    • Takagi M., et al. Regulation of p53 translation and induction after DNA damage by ribosomal protein L26 and nucleolin. Cell 2005, 123:49-63.
    • (2005) Cell , vol.123 , pp. 49-63
    • Takagi, M.1
  • 27
    • 84855982133 scopus 로고    scopus 로고
    • The p53 mRNA-Mdm2 interaction controls Mdm2 nuclear trafficking and is required for p53 activation following DNA damage
    • Gajjar M., et al. The p53 mRNA-Mdm2 interaction controls Mdm2 nuclear trafficking and is required for p53 activation following DNA damage. Cancer Cell 2012, 21:25-35.
    • (2012) Cancer Cell , vol.21 , pp. 25-35
    • Gajjar, M.1
  • 28
    • 34250735674 scopus 로고    scopus 로고
    • RNA regulons: coordination of post-transcriptional events
    • Keene J.D. RNA regulons: coordination of post-transcriptional events. Nat. Rev. Genet. 2007, 8:533-543.
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 533-543
    • Keene, J.D.1
  • 29
    • 80053976182 scopus 로고    scopus 로고
    • HuR-dependent loading of miRNA RISC to the mRNA encoding the Ras-related small GTPase RhoB controls its translation during UV-induced apoptosis
    • Glorian V., et al. HuR-dependent loading of miRNA RISC to the mRNA encoding the Ras-related small GTPase RhoB controls its translation during UV-induced apoptosis. Cell Death Differ. 2011, 18:1692-1701.
    • (2011) Cell Death Differ. , vol.18 , pp. 1692-1701
    • Glorian, V.1
  • 30
    • 0033959125 scopus 로고    scopus 로고
    • HuR regulates p21 mRNA stabilization by UV light
    • Wang W., et al. HuR regulates p21 mRNA stabilization by UV light. Mol. Cell. Biol. 2000, 20:760-769.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 760-769
    • Wang, W.1
  • 31
    • 76249100558 scopus 로고    scopus 로고
    • Exon-based clustering of murine breast tumor transcriptomes reveals alternative exons whose expression is associated with metastasis
    • Dutertre M., et al. Exon-based clustering of murine breast tumor transcriptomes reveals alternative exons whose expression is associated with metastasis. Cancer Res. 2010, 70:896-905.
    • (2010) Cancer Res. , vol.70 , pp. 896-905
    • Dutertre, M.1
  • 32
    • 79960925229 scopus 로고    scopus 로고
    • The Ewing sarcoma protein regulates DNA damage-induced alternative splicing
    • Paronetto M.P., et al. The Ewing sarcoma protein regulates DNA damage-induced alternative splicing. Mol. Cell 2011, 43:353-368.
    • (2011) Mol. Cell , vol.43 , pp. 353-368
    • Paronetto, M.P.1
  • 33
    • 79954515887 scopus 로고    scopus 로고
    • SKIP counteracts p53-mediated apoptosis via selective regulation of p21Cip1 mRNA splicing
    • Chen Y., et al. SKIP counteracts p53-mediated apoptosis via selective regulation of p21Cip1 mRNA splicing. Genes Dev. 2011, 25:701-716.
    • (2011) Genes Dev. , vol.25 , pp. 701-716
    • Chen, Y.1
  • 34
    • 78549288104 scopus 로고    scopus 로고
    • Cotranscriptional exon skipping in the genotoxic stress response
    • Dutertre M., et al. Cotranscriptional exon skipping in the genotoxic stress response. Nat. Struct. Mol. Biol. 2010, 17:1358-1366.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1358-1366
    • Dutertre, M.1
  • 35
    • 46649093597 scopus 로고    scopus 로고
    • Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription
    • Wang X., et al. Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription. Nature 2008, 454:126-130.
    • (2008) Nature , vol.454 , pp. 126-130
    • Wang, X.1
  • 36
    • 77955323879 scopus 로고    scopus 로고
    • A large intergenic noncoding RNA induced by p53 mediates global gene repression in the p53 response
    • Huarte M., et al. A large intergenic noncoding RNA induced by p53 mediates global gene repression in the p53 response. Cell 2010, 142:409-419.
    • (2010) Cell , vol.142 , pp. 409-419
    • Huarte, M.1
  • 37
    • 28944446040 scopus 로고    scopus 로고
    • HnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage
    • Moumen A., et al. hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage. Cell 2005, 123:1065-1078.
    • (2005) Cell , vol.123 , pp. 1065-1078
    • Moumen, A.1
  • 38
    • 79959756263 scopus 로고    scopus 로고
    • Extensive and coordinated transcription of noncoding RNAs within cell-cycle promoters
    • Hung T., et al. Extensive and coordinated transcription of noncoding RNAs within cell-cycle promoters. Nat. Genet. 2011, 43:621-629.
    • (2011) Nat. Genet. , vol.43 , pp. 621-629
    • Hung, T.1
  • 39
    • 84860338675 scopus 로고    scopus 로고
    • R loops: from transcription byproducts to threats to genome stability
    • Aguilera A., Garcia-Muse T. R loops: from transcription byproducts to threats to genome stability. Mol. Cell 2012, 46:115-124.
    • (2012) Mol. Cell , vol.46 , pp. 115-124
    • Aguilera, A.1    Garcia-Muse, T.2
  • 40
    • 84876188716 scopus 로고    scopus 로고
    • Transcription-replication encounters, consequences and genomic instability
    • Helmrich A., et al. Transcription-replication encounters, consequences and genomic instability. Nat. Struct. Mol. Biol. 2013, 20:412-418.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 412-418
    • Helmrich, A.1
  • 41
    • 70449522304 scopus 로고    scopus 로고
    • Topoisomerase I suppresses genomic instability by preventing interference between replication and transcription
    • Tuduri S., et al. Topoisomerase I suppresses genomic instability by preventing interference between replication and transcription. Nat. Cell Biol. 2009, 11:1315-1324.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1315-1324
    • Tuduri, S.1
  • 42
    • 17444426290 scopus 로고    scopus 로고
    • Proteomic analysis of complexes formed by human topoisomerase I
    • Czubaty A., et al. Proteomic analysis of complexes formed by human topoisomerase I. Biochim. Biophys. Acta 2005, 1749:133-141.
    • (2005) Biochim. Biophys. Acta , vol.1749 , pp. 133-141
    • Czubaty, A.1
  • 43
    • 0348224064 scopus 로고    scopus 로고
    • Interaction and stimulation of human FEN-1 nuclease activities by heterogeneous nuclear ribonucleoprotein A1 in alpha-segment processing during Okazaki fragment maturation
    • Chai Q., et al. Interaction and stimulation of human FEN-1 nuclease activities by heterogeneous nuclear ribonucleoprotein A1 in alpha-segment processing during Okazaki fragment maturation. Biochemistry 2003, 42:15045-15052.
    • (2003) Biochemistry , vol.42 , pp. 15045-15052
    • Chai, Q.1
  • 44
    • 84860120619 scopus 로고    scopus 로고
    • UPF1: a leader at the end of chromosomes
    • Azzalin C.M. UPF1: a leader at the end of chromosomes. Nucleus 2012, 3:16-21.
    • (2012) Nucleus , vol.3 , pp. 16-21
    • Azzalin, C.M.1
  • 45
    • 0037148269 scopus 로고    scopus 로고
    • A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation
    • Ford L.P., et al. A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation. Oncogene 2002, 21:580-583.
    • (2002) Oncogene , vol.21 , pp. 580-583
    • Ford, L.P.1
  • 46
    • 77956687928 scopus 로고    scopus 로고
    • Functional diversity of the hnRNPs: past, present and perspectives
    • Han S.P., et al. Functional diversity of the hnRNPs: past, present and perspectives. Biochem. J. 2010, 430:379-392.
    • (2010) Biochem. J. , vol.430 , pp. 379-392
    • Han, S.P.1
  • 47
    • 84876021588 scopus 로고    scopus 로고
    • Requirement of heterogeneous nuclear ribonucleoprotein C for BRCA gene expression and homologous recombination
    • Anantha R.W., et al. Requirement of heterogeneous nuclear ribonucleoprotein C for BRCA gene expression and homologous recombination. PLoS ONE 2013, 8:e61368.
    • (2013) PLoS ONE , vol.8
    • Anantha, R.W.1
  • 48
    • 79951853518 scopus 로고    scopus 로고
    • Sequences in PSF/SFPQ mediate radioresistance and recruitment of PSF/SFPQ-containing complexes to DNA damage sites in human cells
    • Ha K., et al. Sequences in PSF/SFPQ mediate radioresistance and recruitment of PSF/SFPQ-containing complexes to DNA damage sites in human cells. DNA Repair (Amst.) 2011, 10:252-259.
    • (2011) DNA Repair (Amst.) , vol.10 , pp. 252-259
    • Ha, K.1
  • 49
    • 84875918552 scopus 로고    scopus 로고
    • The role of hnRPUL1 involved in DNA damage response is related to PARP1
    • Hong Z., et al. The role of hnRPUL1 involved in DNA damage response is related to PARP1. PLoS ONE 2013, 8:e60208.
    • (2013) PLoS ONE , vol.8
    • Hong, Z.1
  • 50
    • 84883780177 scopus 로고    scopus 로고
    • FANCD2 binds MCM proteins and controls replisome function upon activation of S phase checkpoint signaling
    • Lossaint G., et al. FANCD2 binds MCM proteins and controls replisome function upon activation of S phase checkpoint signaling. Mol. Cell 2013, 51:678-690.
    • (2013) Mol. Cell , vol.51 , pp. 678-690
    • Lossaint, G.1
  • 51
    • 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 A.S., et al. The RNA-binding protein fused in sarcoma (FUS) functions downstream of poly(ADP-ribose) polymerase (PARP) in response to DNA damage. J. Biol. Chem. 2013, 288:24731-24741.
    • (2013) J. Biol. Chem. , vol.288 , pp. 24731-24741
    • Mastrocola, A.S.1
  • 52
    • 84863415403 scopus 로고    scopus 로고
    • Regulation of DNA-end resection by hnRNPU-like proteins promotes DNA double-strand break signaling and repair
    • Polo S.E., et al. Regulation of DNA-end resection by hnRNPU-like proteins promotes DNA double-strand break signaling and repair. Mol. Cell 2012, 45:505-516.
    • (2012) Mol. Cell , vol.45 , pp. 505-516
    • Polo, S.E.1
  • 53
    • 84891793102 scopus 로고    scopus 로고
    • PARP-1 dependent recruitment of the amyotrophic lateral sclerosis-associated protein FUS/TLS to sites of oxidative DNA damage
    • Rulten S.L., et al. PARP-1 dependent recruitment of the amyotrophic lateral sclerosis-associated protein FUS/TLS to sites of oxidative DNA damage. Nucleic Acids Res. 2014, 42:307-314.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 307-314
    • Rulten, S.L.1
  • 54
    • 84864647205 scopus 로고    scopus 로고
    • Site-specific DICER and DROSHA RNA products control the DNA-damage response
    • Francia S., et al. Site-specific DICER and DROSHA RNA products control the DNA-damage response. Nature 2012, 488:231-235.
    • (2012) Nature , vol.488 , pp. 231-235
    • Francia, S.1
  • 55
    • 84862777814 scopus 로고    scopus 로고
    • A role for small RNAs in DNA double-strand break repair
    • Wei W., et al. A role for small RNAs in DNA double-strand break repair. Cell 2012, 149:101-112.
    • (2012) Cell , vol.149 , pp. 101-112
    • Wei, W.1
  • 56
    • 85027945611 scopus 로고    scopus 로고
    • YB-1 disrupts mismatch repair complex formation, interferes with MutSα recruitment on mismatch and inhibits mismatch repair through interacting with PCNA
    • Chang Y.W., et al. YB-1 disrupts mismatch repair complex formation, interferes with MutSα recruitment on mismatch and inhibits mismatch repair through interacting with PCNA. Oncogene 2013, 10.1038/onc.2013.450.
    • (2013) Oncogene
    • Chang, Y.W.1
  • 57
    • 1242342944 scopus 로고    scopus 로고
    • YB-1 promotes strand separation in vitro of duplex DNA containing either mispaired bases or cisplatin modifications, exhibits endonucleolytic activities and binds several DNA repair proteins
    • Gaudreault I., et al. YB-1 promotes strand separation in vitro of duplex DNA containing either mispaired bases or cisplatin modifications, exhibits endonucleolytic activities and binds several DNA repair proteins. Nucleic Acids Res. 2004, 32:316-327.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 316-327
    • Gaudreault, I.1
  • 58
    • 84891840119 scopus 로고    scopus 로고
    • The proteolytic YB-1 fragment interacts with DNA repair machinery and enhances survival during DNA-damaging stress
    • Kim E.R., et al. The proteolytic YB-1 fragment interacts with DNA repair machinery and enhances survival during DNA-damaging stress. Cell Cycle 2013, 12:3791-3803.
    • (2013) Cell Cycle , vol.12 , pp. 3791-3803
    • Kim, E.R.1
  • 59
    • 84859054303 scopus 로고    scopus 로고
    • Proteomic identification of PSF and p54(nrb) as TopBP1-interacting proteins
    • Kuhnert A., et al. Proteomic identification of PSF and p54(nrb) as TopBP1-interacting proteins. J. Cell. Biochem. 2012, 113:1744-1753.
    • (2012) J. Cell. Biochem. , vol.113 , pp. 1744-1753
    • Kuhnert, A.1
  • 60
    • 78651316335 scopus 로고    scopus 로고
    • The splicing-factor related protein SFPQ/PSF interacts with RAD51D and is necessary for homology-directed repair and sister chromatid cohesion
    • Rajesh C., et al. The splicing-factor related protein SFPQ/PSF interacts with RAD51D and is necessary for homology-directed repair and sister chromatid cohesion. Nucleic Acids Res. 2011, 39:132-145.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 132-145
    • Rajesh, C.1
  • 61
    • 84869024542 scopus 로고    scopus 로고
    • PARP activation regulates the RNA-binding protein NONO in the DNA damage response to DNA double-strand breaks
    • Krietsch J., et al. PARP activation regulates the RNA-binding protein NONO in the DNA damage response to DNA double-strand breaks. Nucleic Acids Res. 2012, 40:10287-10301.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 10287-10301
    • Krietsch, J.1
  • 62
    • 73349143041 scopus 로고    scopus 로고
    • Involvement of p54(nrb), a PSF partner protein, in DNA double-strand break repair and radioresistance
    • Li S., et al. Involvement of p54(nrb), a PSF partner protein, in DNA double-strand break repair and radioresistance. Nucleic Acids Res. 2009, 37:6746-6753.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6746-6753
    • Li, S.1
  • 63
    • 34247571926 scopus 로고    scopus 로고
    • P53 promotes the fidelity of DNA end-joining activity by, in part, enhancing the expression of heterogeneous nuclear ribonucleoprotein G
    • Shin K.H., et al. p53 promotes the fidelity of DNA end-joining activity by, in part, enhancing the expression of heterogeneous nuclear ribonucleoprotein G. DNA Repair (Amst.) 2007, 6:830-840.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 830-840
    • Shin, K.H.1
  • 64
    • 84860325854 scopus 로고    scopus 로고
    • Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response
    • Beli P., et al. Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response. Mol. Cell 2012, 46:212-225.
    • (2012) Mol. Cell , vol.46 , pp. 212-225
    • Beli, P.1
  • 65
    • 77953148666 scopus 로고    scopus 로고
    • Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response
    • Bennetzen M.V., et al. Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response. Mol. Cell. Proteomics 2010, 9:1314-1323.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1314-1323
    • Bennetzen, M.V.1
  • 66
    • 78649938817 scopus 로고    scopus 로고
    • ATM-dependent and -independent dynamics of the nuclear phosphoproteome after DNA damage
    • Bensimon A., et al. ATM-dependent and -independent dynamics of the nuclear phosphoproteome after DNA damage. Sci. Signal. 2010, 3:rs3.
    • (2010) Sci. Signal. , vol.3
    • Bensimon, A.1
  • 67
    • 80051793361 scopus 로고    scopus 로고
    • A phospho-proteomic screen identifies substrates of the checkpoint kinase Chk1
    • Blasius M., et al. A phospho-proteomic screen identifies substrates of the checkpoint kinase Chk1. Genome Biol. 2011, 12:R78.
    • (2011) Genome Biol. , vol.12
    • Blasius, M.1
  • 68
    • 79551602983 scopus 로고    scopus 로고
    • Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin
    • Edmond V., et al. Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin. EMBO J. 2011, 30:510-523.
    • (2011) EMBO J. , vol.30 , pp. 510-523
    • Edmond, V.1
  • 69
    • 84876161743 scopus 로고    scopus 로고
    • Paraquat modulates alternative pre-mRNA splicing by modifying the intracellular distribution of SRPK2
    • Vivarelli S., et al. Paraquat modulates alternative pre-mRNA splicing by modifying the intracellular distribution of SRPK2. PLoS ONE 2013, 8:e61980.
    • (2013) PLoS ONE , vol.8
    • Vivarelli, S.1
  • 70
    • 77957361354 scopus 로고    scopus 로고
    • DNA damage activates a spatially distinct late cytoplasmic cell-cycle checkpoint network controlled by MK2-mediated RNA stabilization
    • Reinhardt H.C., et al. DNA damage activates a spatially distinct late cytoplasmic cell-cycle checkpoint network controlled by MK2-mediated RNA stabilization. Mol. Cell 2010, 40:34-49.
    • (2010) Mol. Cell , vol.40 , pp. 34-49
    • Reinhardt, H.C.1
  • 71
    • 79952142751 scopus 로고    scopus 로고
    • ATM regulates a DNA damage response posttranscriptional RNA operon in lymphocytes
    • Mazan-Mamczarz K., et al. ATM regulates a DNA damage response posttranscriptional RNA operon in lymphocytes. Blood 2011, 117:2441-2450.
    • (2011) Blood , vol.117 , pp. 2441-2450
    • Mazan-Mamczarz, K.1
  • 72
    • 1242339684 scopus 로고    scopus 로고
    • Poly(ADP-ribose) reactivates stalled DNA topoisomerase I and induces DNA strand break resealing
    • Malanga M., Althaus F.R. Poly(ADP-ribose) reactivates stalled DNA topoisomerase I and induces DNA strand break resealing. J. Biol. Chem. 2004, 279:5244-5248.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5244-5248
    • Malanga, M.1    Althaus, F.R.2
  • 73
    • 80053986419 scopus 로고    scopus 로고
    • Regulation of HuR by DNA damage response kinases
    • Kim H.H., et al. Regulation of HuR by DNA damage response kinases. J. Nucleic Acids 2010, 2010:981487.
    • (2010) J. Nucleic Acids , vol.2010 , pp. 981487
    • Kim, H.H.1
  • 74
    • 79959330032 scopus 로고    scopus 로고
    • SR and SR-related proteins redistribute to segregated fibrillar components of nucleoli in a response to DNA damage
    • Sakashita E., Endo H. SR and SR-related proteins redistribute to segregated fibrillar components of nucleoli in a response to DNA damage. Nucleus 2010, 1:367-380.
    • (2010) Nucleus , vol.1 , pp. 367-380
    • Sakashita, E.1    Endo, H.2
  • 75
    • 0036315747 scopus 로고    scopus 로고
    • Stress-dependent nucleolin mobilization mediated by p53-nucleolin complex formation
    • Daniely Y., et al. Stress-dependent nucleolin mobilization mediated by p53-nucleolin complex formation. Mol. Cell. Biol. 2002, 22:6014-6022.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6014-6022
    • Daniely, Y.1
  • 76
    • 77953252238 scopus 로고    scopus 로고
    • Genotoxic stress causes the accumulation of the splicing regulator Sam68 in nuclear foci of transcriptionally active chromatin
    • Busa R., et al. Genotoxic stress causes the accumulation of the splicing regulator Sam68 in nuclear foci of transcriptionally active chromatin. Nucleic Acids Res. 2010, 38:3005-3018.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3005-3018
    • Busa, R.1
  • 77
    • 56149106691 scopus 로고    scopus 로고
    • Post-transcriptional control of gene expression through subcellular relocalization of mRNA binding proteins
    • Cammas A., et al. Post-transcriptional control of gene expression through subcellular relocalization of mRNA binding proteins. Biochem. Pharmacol. 2008, 76:1395-1403.
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 1395-1403
    • Cammas, A.1
  • 78
    • 37049030005 scopus 로고    scopus 로고
    • Cytoplasmic relocalization of heterogeneous nuclear ribonucleoprotein A1 controls translation initiation of specific mRNAs
    • Cammas A., et al. Cytoplasmic relocalization of heterogeneous nuclear ribonucleoprotein A1 controls translation initiation of specific mRNAs. Mol. Biol. Cell 2007, 18:5048-5059.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 5048-5059
    • Cammas, A.1
  • 79
    • 78651321770 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor p21 is regulated by RNA-binding protein PCBP4 via mRNA stability
    • Scoumanne A., et al. The cyclin-dependent kinase inhibitor p21 is regulated by RNA-binding protein PCBP4 via mRNA stability. Nucleic Acids Res. 2011, 39:213-224.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 213-224
    • Scoumanne, A.1
  • 80
    • 79960424486 scopus 로고    scopus 로고
    • Translational repression of p53 by RNPC1, a p53 target overexpressed in lymphomas
    • Zhang J., et al. Translational repression of p53 by RNPC1, a p53 target overexpressed in lymphomas. Genes Dev. 2011, 25:1528-1543.
    • (2011) Genes Dev. , vol.25 , pp. 1528-1543
    • Zhang, J.1
  • 81
    • 57349097152 scopus 로고    scopus 로고
    • Dynamic proteomics of individual cancer cells in response to a drug
    • Cohen A.A., et al. Dynamic proteomics of individual cancer cells in response to a drug. Science 2008, 322:1511-1516.
    • (2008) Science , vol.322 , pp. 1511-1516
    • Cohen, A.A.1
  • 82
    • 0037829212 scopus 로고    scopus 로고
    • The pleiotropic functions of the Y-box-binding protein, YB-1
    • Kohno K., et al. The pleiotropic functions of the Y-box-binding protein, YB-1. Bioessays 2003, 25:691-698.
    • (2003) Bioessays , vol.25 , pp. 691-698
    • Kohno, K.1
  • 83
    • 84885078620 scopus 로고    scopus 로고
    • DNA damage induces targeted, genome-wide variation of poly(A) sites in budding yeast
    • Graber J.H., et al. DNA damage induces targeted, genome-wide variation of poly(A) sites in budding yeast. Genome Res. 2013, 23:1690-1703.
    • (2013) Genome Res. , vol.23 , pp. 1690-1703
    • Graber, J.H.1
  • 84
    • 84879799948 scopus 로고    scopus 로고
    • DNA-damage-induced nuclear export of precursor microRNAs is regulated by the ATM-AKT pathway
    • Wan G., et al. DNA-damage-induced nuclear export of precursor microRNAs is regulated by the ATM-AKT pathway. Cell Rep. 2013, 3:2100-2112.
    • (2013) Cell Rep. , vol.3 , pp. 2100-2112
    • Wan, G.1
  • 85
    • 84861997955 scopus 로고    scopus 로고
    • The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts
    • Baltz A.G., et al. The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 2012, 46:674-690.
    • (2012) Mol. Cell , vol.46 , pp. 674-690
    • Baltz, A.G.1
  • 86
    • 84861969926 scopus 로고    scopus 로고
    • Insights into RNA biology from an atlas of mammalian mRNA-binding proteins
    • Castello A., et al. Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 2012, 149:1393-1406.
    • (2012) Cell , vol.149 , pp. 1393-1406
    • Castello, A.1
  • 87
    • 84876806808 scopus 로고    scopus 로고
    • RNA-binding proteins in Mendelian disease
    • Castello A., et al. RNA-binding proteins in Mendelian disease. Trends Genet. 2013, 29:318-327.
    • (2013) Trends Genet. , vol.29 , pp. 318-327
    • Castello, A.1
  • 88
    • 19444363834 scopus 로고    scopus 로고
    • 53BP1 exchanges slowly at the sites of DNA damage and appears to require RNA for its association with chromatin
    • Pryde F., et al. 53BP1 exchanges slowly at the sites of DNA damage and appears to require RNA for its association with chromatin. J. Cell Sci. 2005, 118:2043-2055.
    • (2005) J. Cell Sci. , vol.118 , pp. 2043-2055
    • Pryde, F.1
  • 89
    • 77950920903 scopus 로고    scopus 로고
    • Transcriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP
    • Hafner M., et al. Transcriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP. Cell 2010, 141:129-141.
    • (2010) Cell , vol.141 , pp. 129-141
    • Hafner, M.1
  • 90
    • 70450174321 scopus 로고    scopus 로고
    • High-throughput sequencing methods to study neuronal RNA-protein interactions
    • Ule J. High-throughput sequencing methods to study neuronal RNA-protein interactions. Biochem. Soc. Trans. 2009, 37:1278-1280.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 1278-1280
    • Ule, J.1


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