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Volumn 5, Issue , 2014, Pages

The splicing activator DAZAP1 integrates splicing control into MEK/Erk-regulated cell proliferation and migration

Author keywords

[No Author keywords available]

Indexed keywords

DAZ ASSOCIATED PROTEIN 1; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A2; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN DL; MESSENGER RNA; MESSENGER RNA PRECURSOR; MITOGEN ACTIVATED PROTEIN KINASE; RNA; RNA BINDING PROTEIN; UNCLASSIFIED DRUG; DAZAP1 PROTEIN, HUMAN; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE;

EID: 84899632097     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4078     Document Type: Article
Times cited : (55)

References (61)
  • 1
    • 75849145292 scopus 로고    scopus 로고
    • Expansion of the eukaryotic proteome by alternative splicing
    • Nilsen, T. W., Graveley, B. R. Expansion of the eukaryotic proteome by alternative splicing. Nature 463, 457-463 (2010).
    • (2010) Nature , vol.463 , pp. 457-463
    • Nilsen, T.W.1    Graveley, B.R.2
  • 2
    • 33745899048 scopus 로고    scopus 로고
    • Alternative splicing: New insights from global analyses
    • Blencowe, B. J. Alternative splicing: new insights from global analyses. Cell 126, 37-47 (2006).
    • (2006) Cell , vol.126 , pp. 37-47
    • Blencowe, B.J.1
  • 3
    • 56549101959 scopus 로고    scopus 로고
    • Alternative isoform regulation in human tissue transcriptomes
    • Wang, E. T. et al. Alternative isoform regulation in human tissue transcriptomes. Nature 456, 470-476 (2008).
    • (2008) Nature , vol.456 , pp. 470-476
    • Wang, E.T.1
  • 4
    • 56749098074 scopus 로고    scopus 로고
    • Deep surveying of alternative splicing complexity in the human transcriptome by highthroughput sequencing
    • Pan, Q., Shai, O., Lee, L. J., Frey, B. J., Blencowe, B. J. Deep surveying of alternative splicing complexity in the human transcriptome by highthroughput sequencing. Nat. Genet. 40, 1413-1415 (2008).
    • (2008) Nat. Genet. , vol.40 , pp. 1413-1415
    • Pan, Q.1    Shai, O.2    Lee, L.J.3    Frey, B.J.4    Blencowe, B.J.5
  • 5
    • 42449098125 scopus 로고    scopus 로고
    • Splicing regulation: From a parts list of regulatory elements to an integrated splicing code
    • Wang, Z., Burge, C. B. Splicing regulation: from a parts list of regulatory elements to an integrated splicing code. RNA 14, 802-813 (2008).
    • (2008) RNA , vol.14 , pp. 802-813
    • Wang, Z.1    Burge, C.B.2
  • 6
    • 18344364099 scopus 로고    scopus 로고
    • Understanding alternative splicing: Towards a cellular code
    • Matlin, A. J., Clark, F., Smith, C. W. Understanding alternative splicing: towards a cellular code. Nat. Rev. Mol. Cell Biol. 6, 386-398 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 386-398
    • Matlin, A.J.1    Clark, F.2    Smith, C.W.3
  • 7
    • 0032038213 scopus 로고    scopus 로고
    • Arginine/serine-rich domains of SR proteins can function as activators of pre-mRNA splicing
    • Graveley, B. R., Maniatis, T. Arginine/serine-rich domains of SR proteins can function as activators of pre-mRNA splicing. Mol. Cell 1, 765-771 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 765-771
    • Graveley, B.R.1    Maniatis, T.2
  • 8
    • 0032962535 scopus 로고    scopus 로고
    • HNRNP A1 recruited to an exon in vivo can function as an exon splicing silencer
    • Del Gatto-Konczak, F., Olive, M., Gesnel, M. C., Breathnach, R. hnRNP A1 recruited to an exon in vivo can function as an exon splicing silencer. Mol. Cell Biol. 19, 251-260 (1999).
    • (1999) Mol. Cell Biol. , vol.19 , pp. 251-260
    • Del Gatto-Konczak, F.1    Olive, M.2    Gesnel, M.C.3    Breathnach, R.4
  • 10
    • 84872017252 scopus 로고    scopus 로고
    • A complex network of factors with overlapping affinities represses splicing through intronic elements
    • Wang, Y. et al. A complex network of factors with overlapping affinities represses splicing through intronic elements. Nat. Struct. Mol. Biol. 20, 36-45 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 36-45
    • Wang, Y.1
  • 11
    • 84871401549 scopus 로고    scopus 로고
    • Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms
    • Erkelenz, S. et al. Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms. RNA 19, 96-102 (2013).
    • (2013) RNA , vol.19 , pp. 96-102
    • Erkelenz, S.1
  • 12
    • 4444272979 scopus 로고    scopus 로고
    • Cell signalling and the control of pre-mRNA splicing
    • Shin, C., Manley, J. L. Cell signalling and the control of pre-mRNA splicing. Nat. Rev. Mol. Cell Biol. 5, 727-738 (2004).
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 727-738
    • Shin, C.1    Manley, J.L.2
  • 13
    • 34547209343 scopus 로고    scopus 로고
    • Roles of the Raf/MEK/ERK pathway in cell growth, malignant transformation and drug resistance
    • McCubrey, J. A. et al. Roles of the Raf/MEK/ERK pathway in cell growth, malignant transformation and drug resistance. Biochim. Biophys. Acta 1773, 1263-1284 (2007).
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1263-1284
    • McCubrey, J.A.1
  • 14
    • 0032747134 scopus 로고    scopus 로고
    • Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase
    • Scheid, M. P., Schubert, K. M., Duronio, V. Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase. J. Biol. Chem. 274, 31108-31113 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31108-31113
    • Scheid, M.P.1    Schubert, K.M.2    Duronio, V.3
  • 15
    • 0035421277 scopus 로고    scopus 로고
    • Regulation of alternative pre-mRNA splicing by the ERK MAP-kinase pathway
    • Weg-Remers, S., Ponta, H., Herrlich, P., Konig, H. Regulation of alternative pre-mRNA splicing by the ERK MAP-kinase pathway. EMBO J. 20, 4194-4203 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4194-4203
    • Weg-Remers, S.1    Ponta, H.2    Herrlich, P.3    Konig, H.4
  • 16
    • 79951813692 scopus 로고    scopus 로고
    • TGF-beta regulates isoform switching of FGF receptors and epithelial-mesenchymal transition
    • Shirakihara, T. et al. TGF-beta regulates isoform switching of FGF receptors and epithelial-mesenchymal transition. EMBO J. 30, 783-795 (2011).
    • (2011) EMBO J. , vol.30 , pp. 783-795
    • Shirakihara, T.1
  • 17
    • 0037069651 scopus 로고    scopus 로고
    • Signal-dependent regulation of splicing via phosphorylation of Sam68
    • Matter, N., Herrlich, P., Konig, H. Signal-dependent regulation of splicing via phosphorylation of Sam68. Nature 420, 691-695 (2002).
    • (2002) Nature , vol.420 , pp. 691-695
    • Matter, N.1    Herrlich, P.2    Konig, H.3
  • 18
    • 33745606029 scopus 로고    scopus 로고
    • A positive feedback loop couples Ras activation and CD44 alternative splicing
    • Cheng, C., Yaffe, M. B., Sharp, P. A. A positive feedback loop couples Ras activation and CD44 alternative splicing. Genes Dev. 20, 1715-1720 (2006).
    • (2006) Genes Dev. , vol.20 , pp. 1715-1720
    • Cheng, C.1    Yaffe, M.B.2    Sharp, P.A.3
  • 19
    • 84864910082 scopus 로고    scopus 로고
    • The Akt-SRPK-SR axis constitutes a major pathway in transducing EGF signaling to regulate alternative splicing in the nucleus
    • Zhou, Z. et al. The Akt-SRPK-SR axis constitutes a major pathway in transducing EGF signaling to regulate alternative splicing in the nucleus. Mol. Cell 47, 422-433 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 422-433
    • Zhou, Z.1
  • 20
    • 13444301185 scopus 로고    scopus 로고
    • Dynamic changes in intranuclear and subcellular localizations of mouse Prrp/DAZAP1 during spermatogenesis: The necessity of the C-terminal proline-rich region for nuclear import and localization
    • Kurihara, Y. et al. Dynamic changes in intranuclear and subcellular localizations of mouse Prrp/DAZAP1 during spermatogenesis: the necessity of the C-terminal proline-rich region for nuclear import and localization. Arch. Histol. Cytol. 67, 325-333 (2004).
    • (2004) Arch. Histol. Cytol. , vol.67 , pp. 325-333
    • Kurihara, Y.1
  • 21
    • 0034192841 scopus 로고    scopus 로고
    • Identification of two novel proteins that interact with germ-cellspecific RNA-binding proteins DAZ and DAZL1
    • Tsui, S. et al. Identification of two novel proteins that interact with germ-cellspecific RNA-binding proteins DAZ and DAZL1. Genomics 65, 266-273 (2000).
    • (2000) Genomics , vol.65 , pp. 266-273
    • Tsui, S.1
  • 22
    • 12444329819 scopus 로고    scopus 로고
    • Vertebrate 2xRBD hnRNP proteins: A comparative analysis of genome, mRNA and protein sequences
    • Akindahunsi, A. A., Bandiera, A., Manzini, G. Vertebrate 2xRBD hnRNP proteins: a comparative analysis of genome, mRNA and protein sequences. Comput. Biol. Chem. 29, 13-23 (2005).
    • (2005) Comput. Biol. Chem. , vol.29 , pp. 13-23
    • Akindahunsi, A.A.1    Bandiera, A.2    Manzini, G.3
  • 23
    • 13744252668 scopus 로고    scopus 로고
    • The RNA ligands for mouse proline-rich RNA-binding protein (mouse Prrp) contain two consensus sequences in separate loop structure
    • Hori, T., Taguchi, Y., Uesugi, S., Kurihara, Y. The RNA ligands for mouse proline-rich RNA-binding protein (mouse Prrp) contain two consensus sequences in separate loop structure. Nucleic Acids Res. 33, 190-200 (2005).
    • (2005) Nucleic Acids Res. , vol.33 , pp. 190-200
    • Hori, T.1    Taguchi, Y.2    Uesugi, S.3    Kurihara, Y.4
  • 24
    • 0035341466 scopus 로고    scopus 로고
    • A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization
    • Zhao, W. M., Jiang, C., Kroll, T. T., Huber, P. W. A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization. EMBO J. 20, 2315-2325 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2315-2325
    • Zhao, W.M.1    Jiang, C.2    Kroll, T.T.3    Huber, P.W.4
  • 25
    • 0036708422 scopus 로고    scopus 로고
    • Deleted in azoospermia associated protein 1 shuttles between nucleus and cytoplasm during normal germ cell maturation
    • Vera, Y. et al. Deleted in azoospermia associated protein 1 shuttles between nucleus and cytoplasm during normal germ cell maturation. J. Androl. 23, 622-628 (2002).
    • (2002) J. Androl. , vol.23 , pp. 622-628
    • Vera, Y.1
  • 26
    • 50649104843 scopus 로고    scopus 로고
    • DAZAP1, an hnRNP protein, is required for normal growth and spermatogenesis in mice
    • Hsu, L. C. et al. DAZAP1, an hnRNP protein, is required for normal growth and spermatogenesis in mice. RNA 14, 1814-1822 (2008).
    • (2008) RNA , vol.14 , pp. 1814-1822
    • Hsu, L.C.1
  • 27
    • 33746565898 scopus 로고    scopus 로고
    • A novel nucleocytoplasmic shuttling sequence of DAZAP1, a testis-abundant RNA-binding protein
    • Lin, Y. T., Yen, P. H. A novel nucleocytoplasmic shuttling sequence of DAZAP1, a testis-abundant RNA-binding protein. RNA 12, 1486-1493 (2006).
    • (2006) RNA , vol.12 , pp. 1486-1493
    • Lin, Y.T.1    Yen, P.H.2
  • 28
    • 84867234474 scopus 로고    scopus 로고
    • Intronic splicing enhancers, cognate splicing factors and context-dependent regulation rules
    • Wang, Y., Ma, M., Xiao, X., Wang, Z. Intronic splicing enhancers, cognate splicing factors and context-dependent regulation rules. Nat. Struct. Mol. Biol. 19, 1044-1052 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 1044-1052
    • Wang, Y.1    Ma, M.2    Xiao, X.3    Wang, Z.4
  • 29
    • 79959294504 scopus 로고    scopus 로고
    • DAZAP1, an RNA-binding protein required for development and spermatogenesis, can regulate mRNA translation
    • Smith, R. W. et al. DAZAP1, an RNA-binding protein required for development and spermatogenesis, can regulate mRNA translation. RNA 17, 1282-1295 (2011).
    • (2011) RNA , vol.17 , pp. 1282-1295
    • Smith, R.W.1
  • 30
    • 44349135730 scopus 로고    scopus 로고
    • Binding of DAZAP1 and hnRNPA1/A2 to an exonic splicing silencer in a natural BRCA1 exon 18 mutant
    • Goina, E., Skoko, N., Pagani, F. Binding of DAZAP1 and hnRNPA1/A2 to an exonic splicing silencer in a natural BRCA1 exon 18 mutant. Mol. Cell Biol. 28, 3850-3860 (2008).
    • (2008) Mol. Cell Biol. , vol.28 , pp. 3850-3860
    • Goina, E.1    Skoko, N.2    Pagani, F.3
  • 31
    • 79961187651 scopus 로고    scopus 로고
    • Interaction of hnRNPA1/A2 and DAZAP1 with an Alu-derived intronic splicing enhancer regulates ATM aberrant splicing
    • Pastor, T., Pagani, F. Interaction of hnRNPA1/A2 and DAZAP1 with an Alu-derived intronic splicing enhancer regulates ATM aberrant splicing. PLoS One 6, e23349 (2011).
    • (2011) PLoS One , vol.6 , pp. e23349
    • Pastor, T.1    Pagani, F.2
  • 32
    • 0028215301 scopus 로고
    • RNA binding specificity of hnRNP A1: Significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing
    • Burd, C. G., Dreyfuss, G. RNA binding specificity of hnRNP A1: significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing. EMBO J. 13, 1197-1204 (1994).
    • (1994) EMBO J. , vol.13 , pp. 1197-1204
    • Burd, C.G.1    Dreyfuss, G.2
  • 33
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • Ding, J. et al. Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. Genes Dev. 13, 1102-1115 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1102-1115
    • Ding, J.1
  • 34
    • 84873059804 scopus 로고    scopus 로고
    • Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: How the relative orientation between RRMs influences the nucleic acid binding topology
    • Barraud, P., Allain, F. H. Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology. J. Biomol. NMR 55, 119-138 (2013).
    • (2013) J. Biomol. NMR , vol.55 , pp. 119-138
    • Barraud, P.1    Allain, F.H.2
  • 35
    • 0034426852 scopus 로고    scopus 로고
    • Experimental design for analysis of complex kinetics using surface plasmon resonance
    • Lipschultz, C. A., Li, Y., Smith-Gill, S. Experimental design for analysis of complex kinetics using surface plasmon resonance. Methods 20, 310-318 (2000).
    • (2000) Methods , vol.20 , pp. 310-318
    • Lipschultz, C.A.1    Li, Y.2    Smith-Gill, S.3
  • 36
    • 60549095576 scopus 로고    scopus 로고
    • DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins
    • Yang, H. T., Peggie, M., Cohen, P., Rousseau, S. DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins. Biochem. Biophys. Res. Commun. 380, 705-709 (2009).
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 705-709
    • Yang, H.T.1    Peggie, M.2    Cohen, P.3    Rousseau, S.4
  • 37
    • 84860863700 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Bound RNAs identify features and components of cellular assemblies
    • Han, T. W. et al. Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. Cell 149, 768-779 (2012).
    • (2012) Cell , vol.149 , pp. 768-779
    • Han, T.W.1
  • 38
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels
    • Kato, M. et al. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell 149, 753-767 (2012).
    • (2012) Cell , vol.149 , pp. 753-767
    • Kato, M.1
  • 39
    • 0018198574 scopus 로고
    • Heterogeneous nuclear RNA-protein fibers in chromatin-depleted nuclei
    • Herman, R., Weymouth, L., Penman, S. Heterogeneous nuclear RNA-protein fibers in chromatin-depleted nuclei. J. Cell Biol. 78, 663-674 (1978).
    • (1978) J. Cell Biol. , vol.78 , pp. 663-674
    • Herman, R.1    Weymouth, L.2    Penman, S.3
  • 40
    • 1542619619 scopus 로고    scopus 로고
    • Spectroscopic evidence revealing polyproline II structure in hydrophobic, putatively elastomeric sequences encoded by specific exons of human tropoelastin
    • Bochicchio, B., Ait-Ali, A., Tamburro, A. M., Alix, A. J. Spectroscopic evidence revealing polyproline II structure in hydrophobic, putatively elastomeric sequences encoded by specific exons of human tropoelastin. Biopolymers 73, 484-493 (2004).
    • (2004) Biopolymers , vol.73 , pp. 484-493
    • Bochicchio, B.1    Ait-Ali, A.2    Tamburro, A.M.3    Alix, A.J.4
  • 41
    • 74749089043 scopus 로고    scopus 로고
    • Context-dependent regulatory mechanism of the splicing factor hnRNP L
    • Motta-Mena, L. B., Heyd, F., Lynch, K. W. Context-dependent regulatory mechanism of the splicing factor hnRNP L. Mol. Cell 37, 223-234 (2010).
    • (2010) Mol. Cell , vol.37 , pp. 223-234
    • Motta-Mena, L.B.1    Heyd, F.2    Lynch, K.W.3
  • 42
    • 70349843229 scopus 로고    scopus 로고
    • Splice site strength-dependent activity and genetic buffering by poly-G runs
    • Xiao, X. et al. Splice site strength-dependent activity and genetic buffering by poly-G runs. Nat. Struct. Mol. Biol. 16, 1094-1100 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1094-1100
    • Xiao, X.1
  • 43
    • 70350719211 scopus 로고    scopus 로고
    • Engineering splicing factors with designed specificities
    • Wang, Y., Cheong, C. G., Hall, T. M., Wang, Z. Engineering splicing factors with designed specificities. Nat. Methods 6, 825-830 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 825-830
    • Wang, Y.1    Cheong, C.G.2    Hall, T.M.3    Wang, Z.4
  • 44
    • 70350433635 scopus 로고    scopus 로고
    • Cooperative-binding and splicing-repressive properties of hnRNP A1
    • Okunola, H. L., Krainer, A. R. Cooperative-binding and splicing-repressive properties of hnRNP A1. Mol. Cell Biol. 29, 5620-5631 (2009).
    • (2009) Mol. Cell Biol. , vol.29 , pp. 5620-5631
    • Okunola, H.L.1    Krainer, A.R.2
  • 45
    • 0035691667 scopus 로고    scopus 로고
    • Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins
    • Zhu, J., Mayeda, A., Krainer, A. R. Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins. Mol. Cell 8, 1351-1361 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 1351-1361
    • Zhu, J.1    Mayeda, A.2    Krainer, A.R.3
  • 46
    • 78649345104 scopus 로고    scopus 로고
    • MapSplice: Accurate mapping of RNA-seq reads for splice junction discovery
    • Wang, K. et al. MapSplice: accurate mapping of RNA-seq reads for splice junction discovery. Nucleic Acids Res. 38, e178 (2010).
    • (2010) Nucleic Acids Res. , vol.38 , pp. e178
    • Wang, K.1
  • 47
    • 77952123055 scopus 로고    scopus 로고
    • Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation
    • Trapnell, C. et al. Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation. Nat. Biotechnol. 28, 511-515 (2010).
    • (2010) Nat. Biotechnol. , vol.28 , pp. 511-515
    • Trapnell, C.1
  • 48
    • 78649714014 scopus 로고    scopus 로고
    • Analysis and design of RNA sequencing experiments for identifying isoform regulation
    • Katz, Y., Wang, E. T., Airoldi, E. M., Burge, C. B. Analysis and design of RNA sequencing experiments for identifying isoform regulation. Nat. Methods 7, 1009-1015 (2010).
    • (2010) Nat. Methods , vol.7 , pp. 1009-1015
    • Katz, Y.1    Wang, E.T.2    Airoldi, E.M.3    Burge, C.B.4
  • 49
    • 79951488010 scopus 로고    scopus 로고
    • WAC a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription
    • Zhang, F., Yu, X. WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription. Mol. Cell 41, 384-397 (2011).
    • (2011) Mol. Cell , vol.41 , pp. 384-397
    • Zhang, F.1    Yu, X.2
  • 50
    • 84874087676 scopus 로고    scopus 로고
    • The splicing factor SRSF6 is amplified and is an oncoprotein in lung and colon cancers
    • Cohen-Eliav, M. et al. The splicing factor SRSF6 is amplified and is an oncoprotein in lung and colon cancers. J. Pathol. 229, 630-639 (2013).
    • (2013) J. Pathol. , vol.229 , pp. 630-639
    • Cohen-Eliav, M.1
  • 51
    • 0037206945 scopus 로고    scopus 로고
    • Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: A potential role for pEg3 in cell cycle regulation
    • Davezac, N., Baldin, V., Blot, J., Ducommun, B., Tassan, J. P. Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a potential role for pEg3 in cell cycle regulation. Oncogene 21, 7630-7641 (2002).
    • (2002) Oncogene , vol.21 , pp. 7630-7641
    • Davezac, N.1    Baldin, V.2    Blot, J.3    Ducommun, B.4    Tassan, J.P.5
  • 52
    • 0037047644 scopus 로고    scopus 로고
    • Predictive identification of exonic splicing enhancers in human genes
    • Fairbrother, W. G., Yeh, R. F., Sharp, P. A., Burge, C. B. Predictive identification of exonic splicing enhancers in human genes. Science 297, 1007-1013 (2002).
    • (2002) Science , vol.297 , pp. 1007-1013
    • Fairbrother, W.G.1    Yeh, R.F.2    Sharp, P.A.3    Burge, C.B.4
  • 53
    • 33749995013 scopus 로고    scopus 로고
    • Phosphorylation of the ARE-binding protein DAZAP1 by ERK2 induces its dissociation from DAZ
    • Morton, S. et al. Phosphorylation of the ARE-binding protein DAZAP1 by ERK2 induces its dissociation from DAZ. Biochem. J. 399, 265-273 (2006).
    • (2006) Biochem. J. , vol.399 , pp. 265-273
    • Morton, S.1
  • 54
    • 78650790948 scopus 로고    scopus 로고
    • Improved Phos-tag SDS-PAGE under neutral pH conditions for advanced protein phosphorylation profiling
    • Kinoshita, E., Kinoshita-Kikuta, E. Improved Phos-tag SDS-PAGE under neutral pH conditions for advanced protein phosphorylation profiling. Proteomics 11, 319-323 (2011).
    • (2011) Proteomics , vol.11 , pp. 319-323
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2
  • 55
    • 80055089204 scopus 로고    scopus 로고
    • Acetylation of Prrp K150 regulates the subcellular localization
    • Sasaki, K. et al. Acetylation of Prrp K150 regulates the subcellular localization. Gene 491, 13-19 (2012).
    • (2012) Gene , vol.491 , pp. 13-19
    • Sasaki, K.1
  • 56
    • 84869874612 scopus 로고    scopus 로고
    • Transcription-dependent nuclear localization of DAZAP1 requires an N-terminal signal
    • Lin, Y. T., Wen, W. C., Yen, P. H. Transcription-dependent nuclear localization of DAZAP1 requires an N-terminal signal. Biochem. Biophys. Res. Commun. 428, 422-426 (2012).
    • (2012) Biochem. Biophys. Res. Commun. , vol.428 , pp. 422-426
    • Lin, Y.T.1    Wen, W.C.2    Yen, P.H.3
  • 57
    • 0025888298 scopus 로고
    • Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases
    • Gonzalez, F. A., Raden, D. L., Davis, R. J. Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases. J. Biol. Chem. 266, 22159-22163 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 22159-22163
    • Gonzalez, F.A.1    Raden, D.L.2    Davis, R.J.3
  • 58
    • 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. 30, 510-523 (2011).
    • (2011) EMBO J. , vol.30 , pp. 510-523
    • Edmond, V.1
  • 59
    • 33745501015 scopus 로고    scopus 로고
    • General and specific functions of exonic splicing silencers in splicing control
    • Wang, Z., Xiao, X., Van Nostrand, E., Burge, C. B. General and specific functions of exonic splicing silencers in splicing control. Mol. Cell 23, 61-70 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 61-70
    • Wang, Z.1    Xiao, X.2    Van Nostrand, E.3    Burge, C.B.4
  • 60
    • 10944256767 scopus 로고    scopus 로고
    • Systematic identification and analysis of exonic splicing silencers
    • Wang, Z. et al. Systematic identification and analysis of exonic splicing silencers. Cell 119, 831-845 (2004).
    • (2004) Cell , vol.119 , pp. 831-845
    • Wang, Z.1
  • 61
    • 34347218991 scopus 로고    scopus 로고
    • In vitro scratch assay: A convenient and inexpensive method for analysis of cell migration in vitro
    • Liang, C. C., Park, A. Y., Guan, J. L. In vitro scratch assay: a convenient and inexpensive method for analysis of cell migration in vitro. Nat. Protoc. 2, 329-333 (2007).
    • (2007) Nat. Protoc. , vol.2 , pp. 329-333
    • Liang, C.C.1    Park, A.Y.2    Guan, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.