메뉴 건너뛰기




Volumn 6, Issue 1, 2015, Pages 93-110

The RNAissance family: SR proteins as multifaceted regulators of gene expression

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; SERINE ARGININE RICH PROTEIN; NUCLEAR PROTEIN; RNA BINDING PROTEIN; RNA PRECURSOR; SERINE ARGININE RICH SPLICING FACTOR;

EID: 84916640509     PISSN: 17577004     EISSN: 17577012     Source Type: Journal    
DOI: 10.1002/wrna.1260     Document Type: Review
Times cited : (178)

References (189)
  • 3
    • 77953030317 scopus 로고    scopus 로고
    • A rational nomenclature for serine/arginine-rich protein splicing factors (SR proteins)
    • Manley JL, Krainer AR. A rational nomenclature for serine/arginine-rich protein splicing factors (SR proteins). Genes Dev 2010, 24:1073-1074.
    • (2010) Genes Dev , vol.24 , pp. 1073-1074
    • Manley, J.L.1    Krainer, A.R.2
  • 4
    • 23744455164 scopus 로고    scopus 로고
    • Inactivation of the SR protein splicing factor ASF/SF2 results in genomic instability
    • Li X, Manley JL. Inactivation of the SR protein splicing factor ASF/SF2 results in genomic instability. Cell 2005, 122:365-378.
    • (2005) Cell , vol.122 , pp. 365-378
    • Li, X.1    Manley, J.L.2
  • 6
    • 84887009665 scopus 로고    scopus 로고
    • RRM1 domain of the splicing oncoprotein SRSF1 is required for MEK1-MAPK-ERK activation and cellular transformation
    • Shimoni-Sebag A, Lebenthal-Loinger I, Zender L, Karni R. RRM1 domain of the splicing oncoprotein SRSF1 is required for MEK1-MAPK-ERK activation and cellular transformation. Carcinogenesis 2013, 11:2498-2504.
    • (2013) Carcinogenesis , vol.11 , pp. 2498-2504
    • Shimoni-Sebag, A.1    Lebenthal-Loinger, I.2    Zender, L.3    Karni, R.4
  • 7
    • 84876075472 scopus 로고    scopus 로고
    • Splicing-factor oncoprotein SRSF1 stabilizes p53 via RPL5 and induces cellular senescence
    • Fregoso OI, Das S, Akerman M, Krainer AR. Splicing-factor oncoprotein SRSF1 stabilizes p53 via RPL5 and induces cellular senescence. Mol Cell 2013, 1:56-66.
    • (2013) Mol Cell , vol.1 , pp. 56-66
    • Fregoso, O.I.1    Das, S.2    Akerman, M.3    Krainer, A.R.4
  • 8
    • 84861131874 scopus 로고    scopus 로고
    • Oncogenic splicing factor SRSF1 is a critical transcriptional target of MYC
    • Das S, Anczukow O, Akerman M, Krainer AR. Oncogenic splicing factor SRSF1 is a critical transcriptional target of MYC. Cell Rep 2012, 2:110-117.
    • (2012) Cell Rep , vol.2 , pp. 110-117
    • Das, S.1    Anczukow, O.2    Akerman, M.3    Krainer, A.R.4
  • 10
    • 59749088601 scopus 로고    scopus 로고
    • Temporal requirement of the alternative-splicing factor Sfrs1 for the survival of retinal neurons
    • Kanadia RN, Clark VE, Punzo C, Trimarchi JM, Cepko CL. Temporal requirement of the alternative-splicing factor Sfrs1 for the survival of retinal neurons. Development 2008, 23:3923-3933.
    • (2008) Development , vol.23 , pp. 3923-3933
    • Kanadia, R.N.1    Clark, V.E.2    Punzo, C.3    Trimarchi, J.M.4    Cepko, C.L.5
  • 11
    • 34147213102 scopus 로고    scopus 로고
    • The SR family proteins B52 and dASF/SF2 modulate development of the Drosophila visual system by regulating specific RNA targets
    • Gabut M, Dejardin J, Tazi J, Soret J. The SR family proteins B52 and dASF/SF2 modulate development of the Drosophila visual system by regulating specific RNA targets. Mol Cell Biol 2007, 28:3087-3097.
    • (2007) Mol Cell Biol , vol.28 , pp. 3087-3097
    • Gabut, M.1    Dejardin, J.2    Tazi, J.3    Soret, J.4
  • 12
    • 27744441269 scopus 로고    scopus 로고
    • Loss of splicing factor ASF/SF2 induces G2 cell cycle arrest and apoptosis, but inhibits internucleosomal DNA fragmentation
    • Li X, Wang J, Manley JL. Loss of splicing factor ASF/SF2 induces G2 cell cycle arrest and apoptosis, but inhibits internucleosomal DNA fragmentation. Genes Dev 2005, 22:2705-2714.
    • (2005) Genes Dev , vol.22 , pp. 2705-2714
    • Li, X.1    Wang, J.2    Manley, J.L.3
  • 13
    • 19944427655 scopus 로고    scopus 로고
    • ASF/SF2-regulated CaMKIIδ alternative splicing temporally reprograms excitation-contraction coupling in cardiac muscle
    • Xu X, Yang D, Ding JH, Wang W, Chu PH, Dalton ND, Wang HY, Bermingham JR Jr, Ye Z, Liu F, et al. ASF/SF2-regulated CaMKIIδ alternative splicing temporally reprograms excitation-contraction coupling in cardiac muscle. Cell 2005, 1:59-72.
    • (2005) Cell , vol.1 , pp. 59-72
    • Xu, X.1    Yang, D.2    Ding, J.H.3    Wang, W.4    Chu, P.H.5    Dalton, N.D.6    Wang, H.Y.7    Bermingham Jr, J.R.8    Ye, Z.9    Liu, F.10
  • 14
    • 0034599949 scopus 로고    scopus 로고
    • Functional characterization of SR and SR-related genes in Caenorhabditis elegans
    • Longman D, Johnstone IL, Caceres JF. Functional characterization of SR and SR-related genes in Caenorhabditis elegans. EMBO J 2000, 7:1625-1637.
    • (2000) EMBO J , vol.7 , pp. 1625-1637
    • Longman, D.1    Johnstone, I.L.2    Caceres, J.F.3
  • 15
    • 77952614701 scopus 로고    scopus 로고
    • Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASF
    • Sinha R, Allemand E, Zhang Z, Karni R, Myers MP, Krainer AR. Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASF. Mol Cell Biol 2010, 30:2762-2774.
    • (2010) Mol Cell Biol , vol.30 , pp. 2762-2774
    • Sinha, R.1    Allemand, E.2    Zhang, Z.3    Karni, R.4    Myers, M.P.5    Krainer, A.R.6
  • 16
    • 84876254595 scopus 로고    scopus 로고
    • A new function of the splicing factor SRSF2 in the control of E2F1-mediated cell cycle progression in neuroendocrine lung tumors
    • Edmond V, Merdzhanova G, Gout S, Brambilla E, Gazzeri S, Eymin B. A new function of the splicing factor SRSF2 in the control of E2F1-mediated cell cycle progression in neuroendocrine lung tumors. Cell Cycle 2013, 12:1267-1278.
    • (2013) Cell Cycle , vol.12 , pp. 1267-1278
    • Edmond, V.1    Merdzhanova, G.2    Gout, S.3    Brambilla, E.4    Gazzeri, S.5    Eymin, B.6
  • 18
    • 80052754151 scopus 로고    scopus 로고
    • Exon 11 skipping of E-cadherin RNA downregulates its expression in head and neck cancer cells
    • Sharma S, Liao W, Zhou X, Wong DT, Lichtenstein A. Exon 11 skipping of E-cadherin RNA downregulates its expression in head and neck cancer cells. Mol Cancer Ther 2011, 9:1751-1759.
    • (2011) Mol Cancer Ther , vol.9 , pp. 1751-1759
    • Sharma, S.1    Liao, W.2    Zhou, X.3    Wong, D.T.4    Lichtenstein, A.5
  • 19
    • 79959215165 scopus 로고    scopus 로고
    • SRSF2 is required for sodium butyrate-mediated p21(WAF1) induction and premature senescence in human lung carcinoma cell lines
    • Edmond V, Brambilla C, Brambilla E, Gazzeri S, Eymin B. SRSF2 is required for sodium butyrate-mediated p21(WAF1) induction and premature senescence in human lung carcinoma cell lines. Cell Cycle 2011, 12:1968-1977.
    • (2011) Cell Cycle , vol.12 , pp. 1968-1977
    • Edmond, V.1    Brambilla, C.2    Brambilla, E.3    Gazzeri, S.4    Eymin, B.5
  • 20
    • 34547190674 scopus 로고    scopus 로고
    • Splicing regulator SC35 is essential for genomic stability and cell proliferation during mammalian organogenesis
    • Xiao R, Sun Y, Ding JH, Lin S, Rose DW, Rosenfeld MG, Fu XD, Li X. Splicing regulator SC35 is essential for genomic stability and cell proliferation during mammalian organogenesis. Mol Cell Biol 2007, 15:5393-5402.
    • (2007) Mol Cell Biol , vol.15 , pp. 5393-5402
    • Xiao, R.1    Sun, Y.2    Ding, J.H.3    Lin, S.4    Rose, D.W.5    Rosenfeld, M.G.6    Fu, X.D.7    Li, X.8
  • 21
    • 27544499653 scopus 로고    scopus 로고
    • SC35 promotes sustainable stress-induced alternative splicing of neuronal acetylcholinesterase mRNA
    • Meshorer E, Bryk B, Toiber D, Cohen J, Podoly E, Dori A, Soreq H. SC35 promotes sustainable stress-induced alternative splicing of neuronal acetylcholinesterase mRNA. Mol Psychiatry 2005, 11:985-997.
    • (2005) Mol Psychiatry , vol.11 , pp. 985-997
    • Meshorer, E.1    Bryk, B.2    Toiber, D.3    Cohen, J.4    Podoly, E.5    Dori, A.6    Soreq, H.7
  • 22
    • 16244373960 scopus 로고    scopus 로고
    • The SR protein SC35 is responsible for aberrant splicing of the E1α pyruvate dehydrogenase mRNA in a case of mental retardation with lactic acidosis
    • Gabut M, Mine M, Marsac C, Brivet M, Tazi J, Soret J. The SR protein SC35 is responsible for aberrant splicing of the E1α pyruvate dehydrogenase mRNA in a case of mental retardation with lactic acidosis. Mol Cell Biol 2005, 8:3286-3294.
    • (2005) Mol Cell Biol , vol.8 , pp. 3286-3294
    • Gabut, M.1    Mine, M.2    Marsac, C.3    Brivet, M.4    Tazi, J.5    Soret, J.6
  • 23
    • 22544464444 scopus 로고    scopus 로고
    • ASF/SF2 and SC35 regulate the glutamate receptor subunit 2 alternative flip/flop splicing
    • Crovato TE, Egebjerg J. ASF/SF2 and SC35 regulate the glutamate receptor subunit 2 alternative flip/flop splicing. FEBS Lett 2005, 19:4138-4144.
    • (2005) FEBS Lett , vol.19 , pp. 4138-4144
    • Crovato, T.E.1    Egebjerg, J.2
  • 24
    • 84893840697 scopus 로고    scopus 로고
    • Splicing factor SRSF3 represses the translation of programmed cell death 4 mRNA by associating with the 5′-UTR region
    • Kim J, Park RY, Chen JK, Kim J, Jeong S, Ohn T. Splicing factor SRSF3 represses the translation of programmed cell death 4 mRNA by associating with the 5′-UTR region. Cell Death Differ 2014, 3:481-490.
    • (2014) Cell Death Differ , vol.3 , pp. 481-490
    • Kim, J.1    Park, R.Y.2    Chen, J.K.3    Kim, J.4    Jeong, S.5    Ohn, T.6
  • 26
    • 84878550364 scopus 로고    scopus 로고
    • Splicing factor SRSF3 is crucial for hepatocyte differentiation and metabolic function
    • Sen S, Jumaa H, Webster NJ. Splicing factor SRSF3 is crucial for hepatocyte differentiation and metabolic function. Nat Commun 2013, 4:1336.
    • (2013) Nat Commun , vol.4 , pp. 1336
    • Sen, S.1    Jumaa, H.2    Webster, N.J.3
  • 28
    • 78650553169 scopus 로고    scopus 로고
    • SRp20 is a proto-oncogene critical for cell proliferation and tumor induction and maintenance
    • Jia R, Li C, McCoy JP, Deng CX, Zheng ZM. SRp20 is a proto-oncogene critical for cell proliferation and tumor induction and maintenance. Int J Biol Sci 2010, 6:806-826.
    • (2010) Int J Biol Sci , vol.6 , pp. 806-826
    • Jia, R.1    Li, C.2    McCoy, J.P.3    Deng, C.X.4    Zheng, Z.M.5
  • 29
    • 70350782482 scopus 로고    scopus 로고
    • Antagonistic SR proteins regulate alternative splicing of tumor-related Rac1b downstream of the PI3-kinase and Wnt pathways
    • Goncalves V, Matos P, Jordan P. Antagonistic SR proteins regulate alternative splicing of tumor-related Rac1b downstream of the PI3-kinase and Wnt pathways. Hum Mol Genet 2009, 18:3696-3707.
    • (2009) Hum Mol Genet , vol.18 , pp. 3696-3707
    • Goncalves, V.1    Matos, P.2    Jordan, P.3
  • 31
    • 0033607012 scopus 로고    scopus 로고
    • Blastocyst formation is blocked in mouse embryos lacking the splicing factor SRp20
    • Jumaa H, Wei G, Nielsen PJ. Blastocyst formation is blocked in mouse embryos lacking the splicing factor SRp20. Curr Biol 1999, 16:899-902.
    • (1999) Curr Biol , vol.16 , pp. 899-902
    • Jumaa, H.1    Wei, G.2    Nielsen, P.J.3
  • 32
    • 35448969301 scopus 로고    scopus 로고
    • Sex-dependent up-regulation of two splicing factors, Psf and Srp20, during hippocampal memory formation
    • Antunes-Martins A, Mizuno K, Irvine EE, Lepicard EM, Giese KP. Sex-dependent up-regulation of two splicing factors, Psf and Srp20, during hippocampal memory formation. Learn Mem 2007, 10:693-702.
    • (2007) Learn Mem , vol.10 , pp. 693-702
    • Antunes-Martins, A.1    Mizuno, K.2    Irvine, E.E.3    Lepicard, E.M.4    Giese, K.P.5
  • 34
    • 77955416143 scopus 로고    scopus 로고
    • Global analysis reveals SRp20- and SRp75-specific mRNPs in cycling and neural cells
    • Anko ML, Morales L, Henry I, Beyer A, Neugebauer KM. Global analysis reveals SRp20- and SRp75-specific mRNPs in cycling and neural cells. Nat Struct Mol Biol 2010, 8:962-970.
    • (2010) Nat Struct Mol Biol , vol.8 , pp. 962-970
    • Anko, M.L.1    Morales, L.2    Henry, I.3    Beyer, A.4    Neugebauer, K.M.5
  • 35
    • 84890567244 scopus 로고    scopus 로고
    • Par-4/THAP1 complex and Notch3 competitively regulated pre-mRNA splicing of CCAR1 and affected inversely the survival of T-cell acute lymphoblastic leukemia cells
    • Lu C, Li JY, Ge Z, Zhang L, Zhou GP. Par-4/THAP1 complex and Notch3 competitively regulated pre-mRNA splicing of CCAR1 and affected inversely the survival of T-cell acute lymphoblastic leukemia cells. Oncogene 2013, 50:5602-5613.
    • (2013) Oncogene , vol.50 , pp. 5602-5613
    • Lu, C.1    Li, J.Y.2    Ge, Z.3    Zhang, L.4    Zhou, G.P.5
  • 36
    • 84908553599 scopus 로고    scopus 로고
    • RNA-sequencing of the brain transcriptome implicates dysregulation of neuroplasticity, circadian rhythms and GTPase binding in bipolar disorder
    • Akula N, Barb J, Jiang X, Wendland JR, Choi KH, Sen SK, Hou L, Chen DT, Laje G, Johnson K, et al. RNA-sequencing of the brain transcriptome implicates dysregulation of neuroplasticity, circadian rhythms and GTPase binding in bipolar disorder. Mol Psychiatry 2014. doi: 10.1038/mp.2013.170.
    • (2014) Mol Psychiatry
    • Akula, N.1    Barb, J.2    Jiang, X.3    Wendland, J.R.4    Choi, K.H.5    Sen, S.K.6    Hou, L.7    Chen, D.T.8    Laje, G.9    Johnson, K.10
  • 37
    • 0037066788 scopus 로고    scopus 로고
    • Two proteins essential for apolipoprotein B mRNA editing are expressed from a single gene through alternative splicing
    • Dance GS, Sowden MP, Cartegni L, Cooper E, Krainer AR, Smith HC. Two proteins essential for apolipoprotein B mRNA editing are expressed from a single gene through alternative splicing. J Biol Chem 2002, 15:12703-12709.
    • (2002) J Biol Chem , vol.15 , pp. 12703-12709
    • Dance, G.S.1    Sowden, M.P.2    Cartegni, L.3    Cooper, E.4    Krainer, A.R.5    Smith, H.C.6
  • 38
    • 20244372405 scopus 로고    scopus 로고
    • Molecular and genetic studies imply Akt-mediated signaling promotes protein kinase CβII alternative splicing via phosphorylation of serine/arginine-rich splicing factor SRp40
    • Patel NA, Kaneko S, Apostolatos HS, Bae SS, Watson JE, Davidowitz K, Chappell DS, Birnbaum MJ, Cheng JQ, Cooper DR. Molecular and genetic studies imply Akt-mediated signaling promotes protein kinase CβII alternative splicing via phosphorylation of serine/arginine-rich splicing factor SRp40. J Biol Chem 2005, 14:14302-14309.
    • (2005) J Biol Chem , vol.14 , pp. 14302-14309
    • Patel, N.A.1    Kaneko, S.2    Apostolatos, H.S.3    Bae, S.S.4    Watson, J.E.5    Davidowitz, K.6    Chappell, D.S.7    Birnbaum, M.J.8    Cheng, J.Q.9    Cooper, D.R.10
  • 39
    • 10844260793 scopus 로고    scopus 로고
    • Enhancer-dependent splicing of FGFR1 α-exon is repressed by RNA interference-mediated down-regulation of SRp55
    • Jin W, Cote GJ. Enhancer-dependent splicing of FGFR1 α-exon is repressed by RNA interference-mediated down-regulation of SRp55. Cancer Res 2004, 24:8901-8905.
    • (2004) Cancer Res , vol.24 , pp. 8901-8905
    • Jin, W.1    Cote, G.J.2
  • 40
    • 78049422337 scopus 로고    scopus 로고
    • The SR protein B52/SRp55 is required for DNA topoisomerase I recruitment to chromatin, mRNA release and transcription shutdown
    • Juge F, Fernando C, Fic W, Tazi J. The SR protein B52/SRp55 is required for DNA topoisomerase I recruitment to chromatin, mRNA release and transcription shutdown. PLoS Genet 2010, 9:e1001124.
    • (2010) PLoS Genet , vol.9 , pp. e1001124
    • Juge, F.1    Fernando, C.2    Fic, W.3    Tazi, J.4
  • 42
    • 0028046121 scopus 로고
    • The SR protein B52/SRp55 is essential for Drosophila development
    • Ring HZ, Lis JT. The SR protein B52/SRp55 is essential for Drosophila development. Mol Cell Biol 1994, 11:7499-7506.
    • (1994) Mol Cell Biol , vol.11 , pp. 7499-7506
    • Ring, H.Z.1    Lis, J.T.2
  • 43
    • 1842690772 scopus 로고    scopus 로고
    • TIA proteins are necessary but not sufficient for the tissue-specific splicing of the myosin phosphatase targeting subunit 1
    • Shukla S, Dirksen WP, Joyce KM, Le Guiner-Blanvillain C, Breathnach R, Fisher SA. TIA proteins are necessary but not sufficient for the tissue-specific splicing of the myosin phosphatase targeting subunit 1. J Biol Chem 2004, 14:13668-13676.
    • (2004) J Biol Chem , vol.14 , pp. 13668-13676
    • Shukla, S.1    Dirksen, W.P.2    Joyce, K.M.3    Le Guiner-Blanvillain, C.4    Breathnach, R.5    Fisher, S.A.6
  • 44
    • 0037467677 scopus 로고    scopus 로고
    • Human transformer 2β and SRp55 interact with a calcitonin-specific splice enhancer
    • Tran Q, Coleman TP, Roesser JR. Human transformer 2β and SRp55 interact with a calcitonin-specific splice enhancer. Biochim Biophys Acta 2003, 2:141-152.
    • (2003) Biochim Biophys Acta , vol.2 , pp. 141-152
    • Tran, Q.1    Coleman, T.P.2    Roesser, J.R.3
  • 45
    • 0037417781 scopus 로고    scopus 로고
    • SRp55 is a regulator of calcitonin/CGRP alternative RNA splicing
    • Tran Q, Roesser JR. SRp55 is a regulator of calcitonin/CGRP alternative RNA splicing. Biochemistry 2003, 4:951-957.
    • (2003) Biochemistry , vol.4 , pp. 951-957
    • Tran, Q.1    Roesser, J.R.2
  • 46
    • 0029144216 scopus 로고
    • A subset of SR proteins activates splicing of the cardiac troponin T alternative exon by direct interactions with an exonic enhancer
    • Ramchatesingh J, Zahler AM, Neugebauer KM, Roth MB, Cooper TA. A subset of SR proteins activates splicing of the cardiac troponin T alternative exon by direct interactions with an exonic enhancer. Mol Cell Biol 1995, 9:4898-4907.
    • (1995) Mol Cell Biol , vol.9 , pp. 4898-4907
    • Ramchatesingh, J.1    Zahler, A.M.2    Neugebauer, K.M.3    Roth, M.B.4    Cooper, T.A.5
  • 48
    • 70350004235 scopus 로고    scopus 로고
    • HIV-1 mRNA 3′ end processing is distinctively regulated by eIF3f, CDK11, and splice factor 9G8
    • Valente ST, Gilmartin GM, Venkatarama K, Arriagada G, Goff SP. HIV-1 mRNA 3′ end processing is distinctively regulated by eIF3f, CDK11, and splice factor 9G8. Mol Cell 2009, 2:279-289.
    • (2009) Mol Cell , vol.2 , pp. 279-289
    • Valente, S.T.1    Gilmartin, G.M.2    Venkatarama, K.3    Arriagada, G.4    Goff, S.P.5
  • 49
    • 84860003859 scopus 로고    scopus 로고
    • Spliceosome protein (SRp) regulation of glucocorticoid receptor isoforms and glucocorticoid response in human trabecular meshwork cells
    • Jain A, Wordinger RJ, Yorio T, Clark AF. Spliceosome protein (SRp) regulation of glucocorticoid receptor isoforms and glucocorticoid response in human trabecular meshwork cells. Invest Ophthalmol Vis Sci 2012, 2:857-866.
    • (2012) Invest Ophthalmol Vis Sci , vol.2 , pp. 857-866
    • Jain, A.1    Wordinger, R.J.2    Yorio, T.3    Clark, A.F.4
  • 50
    • 34547630980 scopus 로고    scopus 로고
    • Eye development under the control of SRp55/B52-mediated alternative splicing of eyeless
    • Fic W, Juge F, Soret J, Tazi J. Eye development under the control of SRp55/B52-mediated alternative splicing of eyeless. PLoS One 2007, 2:e253.
    • (2007) PLoS One , vol.2 , pp. e253
    • Fic, W.1    Juge, F.2    Soret, J.3    Tazi, J.4
  • 51
    • 84879948802 scopus 로고    scopus 로고
    • Zinc-induced modulation of SRSF6 activity alters Bim splicing to promote generation of the most potent apoptotic isoform BimS
    • Hara H, Takeda T, Yamamoto N, Furuya K, Hirose K, Kamiya T, Adachi T. Zinc-induced modulation of SRSF6 activity alters Bim splicing to promote generation of the most potent apoptotic isoform BimS. FEBS J 2013, 14:3313-3327.
    • (2013) FEBS J , vol.14 , pp. 3313-3327
    • Hara, H.1    Takeda, T.2    Yamamoto, N.3    Furuya, K.4    Hirose, K.5    Kamiya, T.6    Adachi, T.7
  • 52
    • 84893805687 scopus 로고    scopus 로고
    • Splicing factor SRSF6 promotes hyperplasia of sensitized skin
    • Jensen MA, Wilkinson JE, Krainer AR. Splicing factor SRSF6 promotes hyperplasia of sensitized skin. Nat Struct Mol Biol 2014, 2:189-197.
    • (2014) Nat Struct Mol Biol , vol.2 , pp. 189-197
    • Jensen, M.A.1    Wilkinson, J.E.2    Krainer, A.R.3
  • 54
    • 0038035100 scopus 로고    scopus 로고
    • Serine-arginine-rich protein p30 directs alternative splicing of glucocorticoid receptor pre-mRNA to glucocorticoid receptor β in neutrophils
    • Xu Q, Leung DY, Kisich KO. Serine-arginine-rich protein p30 directs alternative splicing of glucocorticoid receptor pre-mRNA to glucocorticoid receptor β in neutrophils. J Biol Chem 2003, 29:27112-27118.
    • (2003) J Biol Chem , vol.29 , pp. 27112-27118
    • Xu, Q.1    Leung, D.Y.2    Kisich, K.O.3
  • 55
    • 84877332535 scopus 로고    scopus 로고
    • SRSF1 and SRSF9 RNA binding proteins promote Wnt signalling-mediated tumorigenesis by enhancing β-catenin biosynthesis
    • Fu Y, Huang B, Shi Z, Han J, Wang Y, Huangfu J, Wu W. SRSF1 and SRSF9 RNA binding proteins promote Wnt signalling-mediated tumorigenesis by enhancing β-catenin biosynthesis. EMBO Mol Med 2013, 5:737-750.
    • (2013) EMBO Mol Med , vol.5 , pp. 737-750
    • Fu, Y.1    Huang, B.2    Shi, Z.3    Han, J.4    Wang, Y.5    Huangfu, J.6    Wu, W.7
  • 56
    • 52049094582 scopus 로고    scopus 로고
    • Antagonistic effects of the SRp30c protein and cryptic 5′ splice sites on the alternative splicing of the apoptotic regulator Bcl-x
    • Cloutier P, Toutant J, Shkreta L, Goekjian S, Revil T, Chabot B. Antagonistic effects of the SRp30c protein and cryptic 5′ splice sites on the alternative splicing of the apoptotic regulator Bcl-x. J Biol Chem 2008, 31:21315-21324.
    • (2008) J Biol Chem , vol.31 , pp. 21315-21324
    • Cloutier, P.1    Toutant, J.2    Shkreta, L.3    Goekjian, S.4    Revil, T.5    Chabot, B.6
  • 57
    • 33748660487 scopus 로고    scopus 로고
    • SRp54 (SFRS11), a regulator for tau exon 10 alternative splicing identified by an expression cloning strategy
    • Wu JY, Kar A, Kuo D, Yu B, Havlioglu N. SRp54 (SFRS11), a regulator for tau exon 10 alternative splicing identified by an expression cloning strategy. Mol Cell Biol 2006, 26:6739-6747.
    • (2006) Mol Cell Biol , vol.26 , pp. 6739-6747
    • Wu, J.Y.1    Kar, A.2    Kuo, D.3    Yu, B.4    Havlioglu, N.5
  • 59
    • 34948892099 scopus 로고    scopus 로고
    • A complex signaling pathway regulates SRp38 phosphorylation and pre-mRNA splicing in response to heat shock
    • Shi Y, Manley JL. A complex signaling pathway regulates SRp38 phosphorylation and pre-mRNA splicing in response to heat shock. Mol Cell 2007, 28:79-90.
    • (2007) Mol Cell , vol.28 , pp. 79-90
    • Shi, Y.1    Manley, J.L.2
  • 60
    • 78751545915 scopus 로고    scopus 로고
    • Heat shock-induced SRSF10 dephosphorylation displays thermotolerance mediated by Hsp27
    • Shi Y, Nishida K, Campigli Di Giammartino D, Manley JL. Heat shock-induced SRSF10 dephosphorylation displays thermotolerance mediated by Hsp27. Mol Cell Biol 2011, 3:458-465.
    • (2011) Mol Cell Biol , vol.3 , pp. 458-465
    • Shi, Y.1    Nishida, K.2    Campigli Di Giammartino, D.3    Manley, J.L.4
  • 61
    • 77952734299 scopus 로고    scopus 로고
    • Role of SFRS13A in low-density lipoprotein receptor splicing
    • Ling IF, Estus S. Role of SFRS13A in low-density lipoprotein receptor splicing. Hum Mutat 2010, 6:702-709.
    • (2010) Hum Mutat , vol.6 , pp. 702-709
    • Ling, I.F.1    Estus, S.2
  • 62
    • 0032713422 scopus 로고    scopus 로고
    • Cloning and characterization of two neural-salient serine/arginine-rich (NSSR) proteins involved in the regulation of alternative splicing in neurones
    • Komatsu M, Kominami E, Arahata K, Tsukahara T. Cloning and characterization of two neural-salient serine/arginine-rich (NSSR) proteins involved in the regulation of alternative splicing in neurones. Genes Cells 1999, 10:593-606.
    • (1999) Genes Cells , vol.10 , pp. 593-606
    • Komatsu, M.1    Kominami, E.2    Arahata, K.3    Tsukahara, T.4
  • 65
    • 1642540255 scopus 로고    scopus 로고
    • Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo
    • Sakashita E, Tatsumi S, Werner D, Endo H, Mayeda A. Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo. Mol Cell Biol 2004, 3:1174-1187.
    • (2004) Mol Cell Biol , vol.3 , pp. 1174-1187
    • Sakashita, E.1    Tatsumi, S.2    Werner, D.3    Endo, H.4    Mayeda, A.5
  • 66
    • 0035966063 scopus 로고    scopus 로고
    • Serine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicing
    • Cowper AE, Caceres JF, Mayeda A, Screaton GR. Serine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicing. J Biol Chem 2001, 52:48908-48914.
    • (2001) J Biol Chem , vol.52 , pp. 48908-48914
    • Cowper, A.E.1    Caceres, J.F.2    Mayeda, A.3    Screaton, G.R.4
  • 67
    • 0025367075 scopus 로고
    • The essential pre-mRNA splicing factor SF2 influences 5′ splice site selection by activating proximal sites
    • Krainer AR, Conway GC, Kozak D. The essential pre-mRNA splicing factor SF2 influences 5′ splice site selection by activating proximal sites. Cell 1990, 62:35-42.
    • (1990) Cell , vol.62 , pp. 35-42
    • Krainer, A.R.1    Conway, G.C.2    Kozak, D.3
  • 68
    • 0025324948 scopus 로고
    • A protein factor, ASF, controls cell-specific alternative splicing of SV40 early pre-mRNA in vitro
    • Ge H, Manley JL. A protein factor, ASF, controls cell-specific alternative splicing of SV40 early pre-mRNA in vitro. Cell 1990, 62:25-34.
    • (1990) Cell , vol.62 , pp. 25-34
    • Ge, H.1    Manley, J.L.2
  • 69
    • 0025931225 scopus 로고
    • A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription
    • Roth MB, Zahler AM, Stolk JA. A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription. J Cell Biol 1991, 115:587-596.
    • (1991) J Cell Biol , vol.115 , pp. 587-596
    • Roth, M.B.1    Zahler, A.M.2    Stolk, J.A.3
  • 70
    • 0026516573 scopus 로고
    • Two members of a conserved family of nuclear phosphoproteins are involved in pre-mRNA splicing
    • Mayeda A, Zahler AM, Krainer AR, Roth MB. Two members of a conserved family of nuclear phosphoproteins are involved in pre-mRNA splicing. Proc Natl Acad Sci U S A 1992, 89:1301-1304.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 1301-1304
    • Mayeda, A.1    Zahler, A.M.2    Krainer, A.R.3    Roth, M.B.4
  • 71
    • 0026599345 scopus 로고
    • The 35-kDa mammalian splicing factor SC35 mediates specific interactions between U1 and U2 small nuclear ribonucleoprotein particles at the 3′ splice site
    • Fu XD, Maniatis T. The 35-kDa mammalian splicing factor SC35 mediates specific interactions between U1 and U2 small nuclear ribonucleoprotein particles at the 3′ splice site. Proc Natl Acad Sci U S A 1992, 89:1725-1729.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 1725-1729
    • Fu, X.D.1    Maniatis, T.2
  • 72
    • 0026716104 scopus 로고
    • SR proteins: a conserved family of pre-mRNA splicing factors
    • Zahler AM, Lane WS, Stolk JA, Roth MB. SR proteins: a conserved family of pre-mRNA splicing factors. Genes Dev 1992, 6:837-847.
    • (1992) Genes Dev , vol.6 , pp. 837-847
    • Zahler, A.M.1    Lane, W.S.2    Stolk, J.A.3    Roth, M.B.4
  • 73
    • 0025689134 scopus 로고
    • A monoclonal antibody that recognizes a phosphorylated epitope stains lampbrush chromosome loops and small granules in the amphibian germinal vesicle
    • Roth MB, Murphy C, Gall JG. A monoclonal antibody that recognizes a phosphorylated epitope stains lampbrush chromosome loops and small granules in the amphibian germinal vesicle. J Cell Biol 1990, 111:2217-2223.
    • (1990) J Cell Biol , vol.111 , pp. 2217-2223
    • Roth, M.B.1    Murphy, C.2    Gall, J.G.3
  • 74
    • 0023600271 scopus 로고
    • Monoclonal antibodies that recognize transcription unit proteins on newt lampbrush chromosomes
    • Roth MB, Gall JG. Monoclonal antibodies that recognize transcription unit proteins on newt lampbrush chromosomes. J Cell Biol 1987, 105:1047-1054.
    • (1987) J Cell Biol , vol.105 , pp. 1047-1054
    • Roth, M.B.1    Gall, J.G.2
  • 75
    • 0028286596 scopus 로고
    • A serine kinase regulates intracellular localization of splicing factors in the cell cycle
    • Gui JF, Lane WS, Fu XD. A serine kinase regulates intracellular localization of splicing factors in the cell cycle. Nature 1994, 369:678-682.
    • (1994) Nature , vol.369 , pp. 678-682
    • Gui, J.F.1    Lane, W.S.2    Fu, X.D.3
  • 76
    • 0030028882 scopus 로고    scopus 로고
    • The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution
    • Colwill K, Pawson T, Andrews B, Prasad J, Manley JL, Bell JC, Duncan PI. The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution. EMBO J 1996, 15:265-275.
    • (1996) EMBO J , vol.15 , pp. 265-275
    • Colwill, K.1    Pawson, T.2    Andrews, B.3    Prasad, J.4    Manley, J.L.5    Bell, J.C.6    Duncan, P.I.7
  • 78
    • 67649306195 scopus 로고    scopus 로고
    • Regiospecific phosphorylation control of the SR protein ASF/SF2 by SRPK1
    • Ma CT, Hagopian JC, Ghosh G, Fu XD, Adams JA. Regiospecific phosphorylation control of the SR protein ASF/SF2 by SRPK1. J Mol Biol 2009, 390:618-634.
    • (2009) J Mol Biol , vol.390 , pp. 618-634
    • Ma, C.T.1    Hagopian, J.C.2    Ghosh, G.3    Fu, X.D.4    Adams, J.A.5
  • 79
    • 0029744344 scopus 로고    scopus 로고
    • SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors
    • Colwill K, Feng LL, Yeakley JM, Gish GD, Caceres JF, Pawson T, Fu XD. SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors. J Biol Chem 1996, 271:24569-24575.
    • (1996) J Biol Chem , vol.271 , pp. 24569-24575
    • Colwill, K.1    Feng, L.L.2    Yeakley, J.M.3    Gish, G.D.4    Caceres, J.F.5    Pawson, T.6    Fu, X.D.7
  • 80
    • 73149115306 scopus 로고    scopus 로고
    • Allosteric interactions direct binding and phosphorylation of ASF/SF2 by SRPK1
    • Huynh N, Ma CT, Giang N, Hagopian J, Ngo J, Adams J, Ghosh G. Allosteric interactions direct binding and phosphorylation of ASF/SF2 by SRPK1. Biochemistry 2009, 48:11432-11440.
    • (2009) Biochemistry , vol.48 , pp. 11432-11440
    • Huynh, N.1    Ma, C.T.2    Giang, N.3    Hagopian, J.4    Ngo, J.5    Adams, J.6    Ghosh, G.7
  • 81
    • 0028043718 scopus 로고
    • Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism
    • Mermoud JE, Cohen PT, Lamond AI. Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism. EMBO J 1994, 13:5679-5688.
    • (1994) EMBO J , vol.13 , pp. 5679-5688
    • Mermoud, J.E.1    Cohen, P.T.2    Lamond, A.I.3
  • 83
    • 77957754590 scopus 로고    scopus 로고
    • Mechanism of dephosphorylation of the SR protein ASF/SF2 by protein phosphatase 1
    • Ma CT, Ghosh G, Fu XD, Adams JA. Mechanism of dephosphorylation of the SR protein ASF/SF2 by protein phosphatase 1. J Mol Biol 2010, 403:386-404.
    • (2010) J Mol Biol , vol.403 , pp. 386-404
    • Ma, C.T.1    Ghosh, G.2    Fu, X.D.3    Adams, J.A.4
  • 84
    • 79957784833 scopus 로고    scopus 로고
    • Interaction between the RNA binding domains of Ser-Arg splicing factor 1 and U1-70K snRNP protein determines early spliceosome assembly
    • Cho S, Hoang A, Sinha R, Zhong XY, Fu XD, Krainer AR, Ghosh G. Interaction between the RNA binding domains of Ser-Arg splicing factor 1 and U1-70K snRNP protein determines early spliceosome assembly. Proc Natl Acad Sci U S A 2011, 108:8233-8238.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 8233-8238
    • Cho, S.1    Hoang, A.2    Sinha, R.3    Zhong, X.Y.4    Fu, X.D.5    Krainer, A.R.6    Ghosh, G.7
  • 85
    • 0032547829 scopus 로고    scopus 로고
    • Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo
    • Misteli T, Caceres JF, Clement JQ, Krainer AR, Wilkinson MF, Spector DL. Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo. J Cell Biol 1998, 143:297-307.
    • (1998) J Cell Biol , vol.143 , pp. 297-307
    • Misteli, T.1    Caceres, J.F.2    Clement, J.Q.3    Krainer, A.R.4    Wilkinson, M.F.5    Spector, D.L.6
  • 86
    • 0031037690 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by an SR protein requires RS domain phosphorylation: creation of an SRp40-specific splicing enhancer
    • Tacke R, Chen Y, Manley JL. Sequence-specific RNA binding by an SR protein requires RS domain phosphorylation: creation of an SRp40-specific splicing enhancer. Proc Natl Acad Sci U S A 1997, 94:1148-1153.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 1148-1153
    • Tacke, R.1    Chen, Y.2    Manley, J.L.3
  • 87
    • 0031042396 scopus 로고    scopus 로고
    • Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing
    • Xiao SH, Manley JL. Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing. Genes Dev 1997, 11:334-344.
    • (1997) Genes Dev , vol.11 , pp. 334-344
    • Xiao, S.H.1    Manley, J.L.2
  • 89
    • 0031929940 scopus 로고    scopus 로고
    • A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm
    • Caceres JF, Screaton GR, Krainer AR. A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm. Genes Dev 1998, 12:55-66.
    • (1998) Genes Dev , vol.12 , pp. 55-66
    • Caceres, J.F.1    Screaton, G.R.2    Krainer, A.R.3
  • 90
    • 25844491145 scopus 로고    scopus 로고
    • Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2
    • Ngo JC, Chakrabarti S, Ding JH, Velazquez-Dones A, Nolen B, Aubol BE, Adams JA, Fu XD, Ghosh G. Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2. Mol Cell 2005, 20:77-89.
    • (2005) Mol Cell , vol.20 , pp. 77-89
    • Ngo, J.C.1    Chakrabarti, S.2    Ding, J.H.3    Velazquez-Dones, A.4    Nolen, B.5    Aubol, B.E.6    Adams, J.A.7    Fu, X.D.8    Ghosh, G.9
  • 91
    • 27244441805 scopus 로고    scopus 로고
    • Reversible phosphorylation differentially affects nuclear and cytoplasmic functions of splicing factor 2/alternative splicing factor
    • Sanford JR, Ellis JD, Cazalla D, Caceres JF. Reversible phosphorylation differentially affects nuclear and cytoplasmic functions of splicing factor 2/alternative splicing factor. Proc Natl Acad Sci U S A 2005, 102:15042-15047.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15042-15047
    • Sanford, J.R.1    Ellis, J.D.2    Cazalla, D.3    Caceres, J.F.4
  • 92
    • 0033553882 scopus 로고    scopus 로고
    • Transportin-SR, a nuclear import receptor for SR proteins
    • Kataoka N, Bachorik JL, Dreyfuss G. Transportin-SR, a nuclear import receptor for SR proteins. J Cell Biol 1999, 145:1145-1152.
    • (1999) J Cell Biol , vol.145 , pp. 1145-1152
    • Kataoka, N.1    Bachorik, J.L.2    Dreyfuss, G.3
  • 93
    • 0034677884 scopus 로고    scopus 로고
    • A human importin-β family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins
    • Lai MC, Lin RI, Huang SY, Tsai CW, Tarn WY. A human importin-β family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins. J Biol Chem 2000, 275:7950-7957.
    • (2000) J Biol Chem , vol.275 , pp. 7950-7957
    • Lai, M.C.1    Lin, R.I.2    Huang, S.Y.3    Tsai, C.W.4    Tarn, W.Y.5
  • 94
    • 0033564196 scopus 로고    scopus 로고
    • Developmental regulation of SR protein phosphorylation and activity
    • Sanford JR, Bruzik JP. Developmental regulation of SR protein phosphorylation and activity. Genes Dev 1999, 13:1513-1518.
    • (1999) Genes Dev , vol.13 , pp. 1513-1518
    • Sanford, J.R.1    Bruzik, J.P.2
  • 95
    • 0035964316 scopus 로고    scopus 로고
    • Regulation of SR protein localization during development
    • Sanford JR, Bruzik JP. Regulation of SR protein localization during development. Proc Natl Acad Sci U S A 2001, 98:10184-10189.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 10184-10189
    • Sanford, J.R.1    Bruzik, J.P.2
  • 97
    • 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, Qiu J, Liu W, Zhou Y, Plocinik RM, Li H, Hu Q, Ghosh G, Adams JA, Rosenfeld MG, et al. The Akt-SRPK-SR axis constitutes a major pathway in transducing EGF signaling to regulate alternative splicing in the nucleus. Mol Cell 2012, 47:422-433.
    • (2012) Mol Cell , vol.47 , pp. 422-433
    • Zhou, Z.1    Qiu, J.2    Liu, W.3    Zhou, Y.4    Plocinik, R.M.5    Li, H.6    Hu, Q.7    Ghosh, G.8    Adams, J.A.9    Rosenfeld, M.G.10
  • 101
    • 0027143943 scopus 로고
    • A splicing enhancer in the human fibronectin alternate ED1 exon interacts with SR proteins and stimulates U2 snRNP binding
    • Lavigueur A, La Branche H, Kornblihtt AR, Chabot B. A splicing enhancer in the human fibronectin alternate ED1 exon interacts with SR proteins and stimulates U2 snRNP binding. Genes Dev 1993, 7:2405-2417.
    • (1993) Genes Dev , vol.7 , pp. 2405-2417
    • Lavigueur, A.1    La Branche, H.2    Kornblihtt, A.R.3    Chabot, B.4
  • 102
    • 0027715743 scopus 로고
    • General splicing factor SF2/ASF promotes alternative splicing by binding to an exonic splicing enhancer
    • Sun Q, Mayeda A, Hampson RK, Krainer AR, Rottman FM. General splicing factor SF2/ASF promotes alternative splicing by binding to an exonic splicing enhancer. Genes Dev 1993, 7:2598-2608.
    • (1993) Genes Dev , vol.7 , pp. 2598-2608
    • Sun, Q.1    Mayeda, A.2    Hampson, R.K.3    Krainer, A.R.4    Rottman, F.M.5
  • 103
    • 0027185151 scopus 로고
    • A splicing enhancer complex controls alternative splicing of doublesex pre-mRNA
    • Tian M, Maniatis T. A splicing enhancer complex controls alternative splicing of doublesex pre-mRNA. Cell 1993, 74:105-114.
    • (1993) Cell , vol.74 , pp. 105-114
    • Tian, M.1    Maniatis, T.2
  • 104
    • 0029894931 scopus 로고    scopus 로고
    • Identification of proteins that interact with exon sequences, splice sites, and the branchpoint sequence during each stage of spliceosome assembly
    • Chiara MD, Gozani O, Bennett M, Champion-Arnaud P, Palandjian L, Reed R. Identification of proteins that interact with exon sequences, splice sites, and the branchpoint sequence during each stage of spliceosome assembly. Mol Cell Biol 1996, 16:3317-3326.
    • (1996) Mol Cell Biol , vol.16 , pp. 3317-3326
    • Chiara, M.D.1    Gozani, O.2    Bennett, M.3    Champion-Arnaud, P.4    Palandjian, L.5    Reed, R.6
  • 105
    • 0028006713 scopus 로고
    • SR proteins promote the first specific recognition of Pre-mRNA and are present together with the U1 small nuclear ribonucleoprotein particle in a general splicing enhancer complex
    • Staknis D, Reed R. SR proteins promote the first specific recognition of Pre-mRNA and are present together with the U1 small nuclear ribonucleoprotein particle in a general splicing enhancer complex. Mol Cell Biol 1994, 14:7670-7682.
    • (1994) Mol Cell Biol , vol.14 , pp. 7670-7682
    • Staknis, D.1    Reed, R.2
  • 107
    • 0027137934 scopus 로고
    • Specific interactions between proteins implicated in splice site selection and regulated alternative splicing
    • Wu JY, Maniatis T. Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell 1993, 75:1061-1070.
    • (1993) Cell , vol.75 , pp. 1061-1070
    • Wu, J.Y.1    Maniatis, T.2
  • 108
    • 0032476604 scopus 로고    scopus 로고
    • Phosphorylation-dephosphorylation differentially affects activities of splicing factor ASF/SF2
    • Xiao SH, Manley JL. Phosphorylation-dephosphorylation differentially affects activities of splicing factor ASF/SF2. EMBO J 1998, 17:6359-6367.
    • (1998) EMBO J , vol.17 , pp. 6359-6367
    • Xiao, S.H.1    Manley, J.L.2
  • 109
    • 0034671932 scopus 로고    scopus 로고
    • Pre-mRNA splicing in the absence of an SR protein RS domain
    • Zhu J, Krainer AR. Pre-mRNA splicing in the absence of an SR protein RS domain. Genes Dev 2000, 14:3166-3178.
    • (2000) Genes Dev , vol.14 , pp. 3166-3178
    • Zhu, J.1    Krainer, A.R.2
  • 110
    • 0029258817 scopus 로고
    • Intrinsic U2AF binding is modulated by exon enhancer signals in parallel with changes in splicing activity
    • Wang Z, Hoffmann HM, Grabowski PJ. Intrinsic U2AF binding is modulated by exon enhancer signals in parallel with changes in splicing activity. RNA 1995, 1:21-35.
    • (1995) RNA , vol.1 , pp. 21-35
    • Wang, Z.1    Hoffmann, H.M.2    Grabowski, P.J.3
  • 111
    • 0034755256 scopus 로고    scopus 로고
    • Dual function for U2AF(35) in AG-dependent pre-mRNA splicing
    • Guth S, Tange TO, Kellenberger E, Valcarcel J. Dual function for U2AF(35) in AG-dependent pre-mRNA splicing. Mol Cell Biol 2001, 21:7673-7681.
    • (2001) Mol Cell Biol , vol.21 , pp. 7673-7681
    • Guth, S.1    Tange, T.O.2    Kellenberger, E.3    Valcarcel, J.4
  • 112
    • 0034743627 scopus 로고    scopus 로고
    • The role of U2AF35 and U2AF65 in enhancer-dependent splicing
    • Graveley BR, Hertel KJ, Maniatis T. The role of U2AF35 and U2AF65 in enhancer-dependent splicing. RNA 2001, 7:806-818.
    • (2001) RNA , vol.7 , pp. 806-818
    • Graveley, B.R.1    Hertel, K.J.2    Maniatis, T.3
  • 113
    • 1242316952 scopus 로고    scopus 로고
    • Arginine-serine-rich domains bound at splicing enhancers contact the branchpoint to promote prespliceosome assembly
    • Shen H, Kan JL, Green MR. Arginine-serine-rich domains bound at splicing enhancers contact the branchpoint to promote prespliceosome assembly. Mol Cell 2004, 13:367-376.
    • (2004) Mol Cell , vol.13 , pp. 367-376
    • Shen, H.1    Kan, J.L.2    Green, M.R.3
  • 114
    • 0029377886 scopus 로고
    • SR proteins escort the U4/U6.U5 tri-snRNP to the spliceosome
    • Roscigno RF, Garcia-Blanco MA. SR proteins escort the U4/U6.U5 tri-snRNP to the spliceosome. RNA 1995, 1:692-706.
    • (1995) RNA , vol.1 , pp. 692-706
    • Roscigno, R.F.1    Garcia-Blanco, M.A.2
  • 115
    • 77950870601 scopus 로고    scopus 로고
    • Exon definition complexes contain the tri-snRNP and can be directly converted into B-like precatalytic splicing complexes
    • Schneider M, Will CL, Anokhina M, Tazi J, Urlaub H, Luhrmann R. Exon definition complexes contain the tri-snRNP and can be directly converted into B-like precatalytic splicing complexes. Mol Cell 2010, 38:223-235.
    • (2010) Mol Cell , vol.38 , pp. 223-235
    • Schneider, M.1    Will, C.L.2    Anokhina, M.3    Tazi, J.4    Urlaub, H.5    Luhrmann, R.6
  • 116
    • 8644268780 scopus 로고    scopus 로고
    • A pathway of sequential arginine-serine-rich domain-splicing signal interactions during mammalian spliceosome assembly
    • Shen H, Green MR. A pathway of sequential arginine-serine-rich domain-splicing signal interactions during mammalian spliceosome assembly. Mol Cell 2004, 16:363-373.
    • (2004) Mol Cell , vol.16 , pp. 363-373
    • Shen, H.1    Green, M.R.2
  • 117
    • 0031468240 scopus 로고    scopus 로고
    • Both phosphorylation and dephosphorylation of ASF/SF2 are required for pre-mRNA splicing in vitro
    • Cao W, Jamison SF, Garcia-Blanco MA. Both phosphorylation and dephosphorylation of ASF/SF2 are required for pre-mRNA splicing in vitro. RNA 1997, 3:1456-1467.
    • (1997) RNA , vol.3 , pp. 1456-1467
    • Cao, W.1    Jamison, S.F.2    Garcia-Blanco, M.A.3
  • 119
    • 0028895417 scopus 로고
    • Exon recognition in vertebrate splicing
    • Berget SM. Exon recognition in vertebrate splicing. J Biol Chem 1995, 270:2411-2414.
    • (1995) J Biol Chem , vol.270 , pp. 2411-2414
    • Berget, S.M.1
  • 120
    • 84871449381 scopus 로고    scopus 로고
    • Exon and intron definition in pre-mRNA splicing
    • De Conti L, Baralle M, Buratti E. Exon and intron definition in pre-mRNA splicing. WIREs RNA 2013, 4:49-60.
    • (2013) WIREs RNA , vol.4 , pp. 49-60
    • De Conti, L.1    Baralle, M.2    Buratti, E.3
  • 122
    • 84871401549 scopus 로고    scopus 로고
    • Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms
    • Erkelenz S, Mueller WF, Evans MS, Busch A, Schoneweis K, Hertel KJ, Schaal H. Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms. RNA 2013, 19:96-102.
    • (2013) RNA , vol.19 , pp. 96-102
    • Erkelenz, S.1    Mueller, W.F.2    Evans, M.S.3    Busch, A.4    Schoneweis, K.5    Hertel, K.J.6    Schaal, H.7
  • 123
    • 33745207758 scopus 로고    scopus 로고
    • Comparative analysis identifies exonic splicing regulatory sequences-the complex definition of enhancers and silencers
    • Goren A, Ram O, Amit M, Keren H, Lev-Maor G, Vig I, Pupko T, Ast G. Comparative analysis identifies exonic splicing regulatory sequences-the complex definition of enhancers and silencers. Mol Cell 2006, 22:769-781.
    • (2006) Mol Cell , vol.22 , pp. 769-781
    • Goren, A.1    Ram, O.2    Amit, M.3    Keren, H.4    Lev-Maor, G.5    Vig, I.6    Pupko, T.7    Ast, G.8
  • 124
    • 54849438715 scopus 로고    scopus 로고
    • Identification of nuclear and cytoplasmic mRNA targets for the shuttling protein SF2/ASF
    • Sanford JR, Coutinho P, Hackett JA, Wang X, Ranahan W, Caceres JF. Identification of nuclear and cytoplasmic mRNA targets for the shuttling protein SF2/ASF. PLoS One 2008, 3:e3369.
    • (2008) PLoS One , vol.3 , pp. e3369
    • Sanford, J.R.1    Coutinho, P.2    Hackett, J.A.3    Wang, X.4    Ranahan, W.5    Caceres, J.F.6
  • 125
    • 79251584960 scopus 로고    scopus 로고
    • SR proteins induce alternative exon skipping through their activities on the flanking constitutive exons
    • Han J, Ding JH, Byeon CW, Kim JH, Hertel KJ, Jeong S, Fu XD. SR proteins induce alternative exon skipping through their activities on the flanking constitutive exons. Mol Cell Biol 2011, 31:793-802.
    • (2011) Mol Cell Biol , vol.31 , pp. 793-802
    • Han, J.1    Ding, J.H.2    Byeon, C.W.3    Kim, J.H.4    Hertel, K.J.5    Jeong, S.6    Fu, X.D.7
  • 129
    • 0029973772 scopus 로고    scopus 로고
    • Demonstration of a dynamic, transcription-dependent organization of pre-mRNA splicing factors in polytene nuclei
    • Bauren G, Jiang WQ, Bernholm K, Gu F, Wieslander L. Demonstration of a dynamic, transcription-dependent organization of pre-mRNA splicing factors in polytene nuclei. J Cell Biol 1996, 133:929-941.
    • (1996) J Cell Biol , vol.133 , pp. 929-941
    • Bauren, G.1    Jiang, W.Q.2    Bernholm, K.3    Gu, F.4    Wieslander, L.5
  • 130
    • 61449254471 scopus 로고    scopus 로고
    • Specific combinations of SR proteins associate with single pre-messenger RNAs in vivo and contribute different functions
    • Bjork P, Jin S, Zhao J, Singh OP, Persson JO, Hellman U, Wieslander L. Specific combinations of SR proteins associate with single pre-messenger RNAs in vivo and contribute different functions. J Cell Biol 2009, 184:555-568.
    • (2009) J Cell Biol , vol.184 , pp. 555-568
    • Bjork, P.1    Jin, S.2    Zhao, J.3    Singh, O.P.4    Persson, J.O.5    Hellman, U.6    Wieslander, L.7
  • 131
    • 0028077730 scopus 로고
    • Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors
    • Caceres JF, Stamm S, Helfman DM, Krainer AR. Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors. Science 1994, 265:1706-1709.
    • (1994) Science , vol.265 , pp. 1706-1709
    • Caceres, J.F.1    Stamm, S.2    Helfman, D.M.3    Krainer, A.R.4
  • 132
    • 0033762534 scopus 로고    scopus 로고
    • Selection of alternative 5′ splice sites: role of U1 snRNP and models for the antagonistic effects of SF2/ASF and hnRNP A1
    • Eperon IC, Makarova OV, Mayeda A, Munroe SH, Caceres JF, Hayward DG, Krainer AR. Selection of alternative 5′ splice sites: role of U1 snRNP and models for the antagonistic effects of SF2/ASF and hnRNP A1. Mol Cell Biol 2000, 20:8303-8318.
    • (2000) Mol Cell Biol , vol.20 , pp. 8303-8318
    • Eperon, I.C.1    Makarova, O.V.2    Mayeda, A.3    Munroe, S.H.4    Caceres, J.F.5    Hayward, D.G.6    Krainer, A.R.7
  • 133
    • 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 AR. Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins. Mol Cell 2001, 8:1351-1361.
    • (2001) Mol Cell , vol.8 , pp. 1351-1361
    • Zhu, J.1    Mayeda, A.2    Krainer, A.R.3
  • 134
    • 0344074646 scopus 로고    scopus 로고
    • Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors
    • Hanamura A, Caceres JF, Mayeda A, Franza BR Jr, Krainer AR. Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors. RNA 1998, 4:430-444.
    • (1998) RNA , vol.4 , pp. 430-444
    • Hanamura, A.1    Caceres, J.F.2    Mayeda, A.3    Franza Jr, B.R.4    Krainer, A.R.5
  • 135
    • 9244221107 scopus 로고    scopus 로고
    • Relative amounts of antagonistic splicing factors, hnRNP A1 and ASF/SF2, change during neoplastic lung growth: implications for pre-mRNA processing
    • Zerbe LK, Pino I, Pio R, Cosper PF, Dwyer-Nield LD, Meyer AM, Port JD, Montuenga LM, Malkinson AM. Relative amounts of antagonistic splicing factors, hnRNP A1 and ASF/SF2, change during neoplastic lung growth: implications for pre-mRNA processing. Mol Carcinog 2004, 41:187-196.
    • (2004) Mol Carcinog , vol.41 , pp. 187-196
    • Zerbe, L.K.1    Pino, I.2    Pio, R.3    Cosper, P.F.4    Dwyer-Nield, L.D.5    Meyer, A.M.6    Port, J.D.7    Montuenga, L.M.8    Malkinson, A.M.9
  • 136
    • 0036261810 scopus 로고    scopus 로고
    • SRp30c is a repressor of 3′ splice site utilization
    • Simard MJ, Chabot B. SRp30c is a repressor of 3′ splice site utilization. Mol Cell Biol 2002, 22:4001-4010.
    • (2002) Mol Cell Biol , vol.22 , pp. 4001-4010
    • Simard, M.J.1    Chabot, B.2
  • 137
    • 0036848091 scopus 로고    scopus 로고
    • The SR protein SRp38 represses splicing in M phase cells
    • Shin C, Manley JL. The SR protein SRp38 represses splicing in M phase cells. Cell 2002, 111:407-417.
    • (2002) Cell , vol.111 , pp. 407-417
    • Shin, C.1    Manley, J.L.2
  • 138
    • 53549089314 scopus 로고    scopus 로고
    • Phosphorylation switches the general splicing repressor SRp38 to a sequence-specific activator
    • Feng Y, Chen M, Manley JL. Phosphorylation switches the general splicing repressor SRp38 to a sequence-specific activator. Nat Struct Mol Biol 2008, 15:1040-1048.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1040-1048
    • Feng, Y.1    Chen, M.2    Manley, J.L.3
  • 139
    • 58249093940 scopus 로고    scopus 로고
    • The SR protein family of splicing factors: master regulators of gene expression
    • Long JC, Caceres JF. The SR protein family of splicing factors: master regulators of gene expression. Biochem J 2009, 417:15-27.
    • (2009) Biochem J , vol.417 , pp. 15-27
    • Long, J.C.1    Caceres, J.F.2
  • 140
    • 0029064220 scopus 로고
    • The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities
    • Tacke R, Manley JL. The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities. EMBO J 1995, 14:3540-3551.
    • (1995) EMBO J , vol.14 , pp. 3540-3551
    • Tacke, R.1    Manley, J.L.2
  • 141
    • 0032128255 scopus 로고    scopus 로고
    • Identification of functional exonic splicing enhancer motifs recognized by individual SR proteins
    • Liu HX, Zhang M, Krainer AR. Identification of functional exonic splicing enhancer motifs recognized by individual SR proteins. Genes Dev 1998, 12:1998-2012.
    • (1998) Genes Dev , vol.12 , pp. 1998-2012
    • Liu, H.X.1    Zhang, M.2    Krainer, A.R.3
  • 142
    • 0027424442 scopus 로고
    • Specific commitment of different pre-mRNAs to splicing by single SR proteins
    • Fu XD. Specific commitment of different pre-mRNAs to splicing by single SR proteins. Nature 1993, 365:82-85.
    • (1993) Nature , vol.365 , pp. 82-85
    • Fu, X.D.1
  • 143
    • 27644592554 scopus 로고    scopus 로고
    • Dephosphorylation-dependent sorting of SR splicing factors during mRNP maturation
    • Lin S, Xiao R, Sun P, Xu X, Fu XD. Dephosphorylation-dependent sorting of SR splicing factors during mRNP maturation. Mol Cell 2005, 20:413-425.
    • (2005) Mol Cell , vol.20 , pp. 413-425
    • Lin, S.1    Xiao, R.2    Sun, P.3    Xu, X.4    Fu, X.D.5
  • 149
    • 77950357450 scopus 로고    scopus 로고
    • A splicing-independent function of SF2/ASF in microRNA processing
    • Wu H, Sun S, Tu K, Gao Y, Xie B, Krainer AR, Zhu J. A splicing-independent function of SF2/ASF in microRNA processing. Mol Cell 2010, 38:67-77.
    • (2010) Mol Cell , vol.38 , pp. 67-77
    • Wu, H.1    Sun, S.2    Tu, K.3    Gao, Y.4    Xie, B.5    Krainer, A.R.6    Zhu, J.7
  • 151
    • 33947305594 scopus 로고    scopus 로고
    • Ultraconserved elements are associated with homeostatic control of splicing regulators by alternative splicing and nonsense-mediated decay
    • Ni JZ, Grate L, Donohue JP, Preston C, Nobida N, O'Brien G, Shiue L, Clark TA, Blume JE, Ares M Jr. Ultraconserved elements are associated with homeostatic control of splicing regulators by alternative splicing and nonsense-mediated decay. Genes Dev 2007, 21:708-718.
    • (2007) Genes Dev , vol.21 , pp. 708-718
    • Ni, J.Z.1    Grate, L.2    Donohue, J.P.3    Preston, C.4    Nobida, N.5    O'Brien, G.6    Shiue, L.7    Clark, T.A.8    Blume, J.E.9    Ares Jr, M.10
  • 153
    • 84874972604 scopus 로고    scopus 로고
    • Coupling pre-mRNA processing to transcription on the RNA factory assembly line
    • Lee KM, Tarn WY. Coupling pre-mRNA processing to transcription on the RNA factory assembly line. RNA Biol 2013, 10:380-390.
    • (2013) RNA Biol , vol.10 , pp. 380-390
    • Lee, K.M.1    Tarn, W.Y.2
  • 154
    • 1842376906 scopus 로고    scopus 로고
    • The dynamics of a pre-mRNA splicing factor in living cells
    • Misteli T, Caceres JF, Spector DL. The dynamics of a pre-mRNA splicing factor in living cells. Nature 1997, 387:523-527.
    • (1997) Nature , vol.387 , pp. 523-527
    • Misteli, T.1    Caceres, J.F.2    Spector, D.L.3
  • 155
    • 0029959435 scopus 로고    scopus 로고
    • The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins
    • Yuryev A, Patturajan M, Litingtung Y, Joshi RV, Gentile C, Gebara M, Corden JL. The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins. Proc Natl Acad Sci U S A 1996, 93:6975-6980.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6975-6980
    • Yuryev, A.1    Patturajan, M.2    Litingtung, Y.3    Joshi, R.V.4    Gentile, C.5    Gebara, M.6    Corden, J.L.7
  • 156
    • 0031022189 scopus 로고    scopus 로고
    • Splicing factors associate with hyperphosphorylated RNA polymerase II in the absence of pre-mRNA
    • Kim E, Du L, Bregman DB, Warren SL. Splicing factors associate with hyperphosphorylated RNA polymerase II in the absence of pre-mRNA. J Cell Biol 1997, 136:19-28.
    • (1997) J Cell Biol , vol.136 , pp. 19-28
    • Kim, E.1    Du, L.2    Bregman, D.B.3    Warren, S.L.4
  • 157
    • 0031032049 scopus 로고    scopus 로고
    • A functional interaction between the carboxy-terminal domain of RNA polymerase II and pre-mRNA splicing
    • Du L, Warren SL. A functional interaction between the carboxy-terminal domain of RNA polymerase II and pre-mRNA splicing. J Cell Biol 1997, 136:5-18.
    • (1997) J Cell Biol , vol.136 , pp. 5-18
    • Du, L.1    Warren, S.L.2
  • 158
    • 0033153543 scopus 로고    scopus 로고
    • RNA polymerase II targets pre-mRNA splicing factors to transcription sites in vivo
    • Misteli T, Spector DL. RNA polymerase II targets pre-mRNA splicing factors to transcription sites in vivo. Mol Cell 1999, 3:697-705.
    • (1999) Mol Cell , vol.3 , pp. 697-705
    • Misteli, T.1    Spector, D.L.2
  • 159
    • 33750596100 scopus 로고    scopus 로고
    • RNA polymerase II C-terminal domain mediates regulation of alternative splicing by SRp20
    • de la Mata M, Kornblihtt AR. RNA polymerase II C-terminal domain mediates regulation of alternative splicing by SRp20. Nat Struct Mol Biol 2006, 13:973-980.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 973-980
    • de la Mata, M.1    Kornblihtt, A.R.2
  • 162
    • 84877721757 scopus 로고    scopus 로고
    • SR proteins collaborate with 7SK and promoter-associated nascent RNA to release paused polymerase
    • Ji X, Zhou Y, Pandit S, Huang J, Li H, Lin CY, Xiao R, Burge CB, Fu XD. SR proteins collaborate with 7SK and promoter-associated nascent RNA to release paused polymerase. Cell 2013, 153:855-868.
    • (2013) Cell , vol.153 , pp. 855-868
    • Ji, X.1    Zhou, Y.2    Pandit, S.3    Huang, J.4    Li, H.5    Lin, C.Y.6    Xiao, R.7    Burge, C.B.8    Fu, X.D.9
  • 163
    • 80052485020 scopus 로고    scopus 로고
    • Shuttling SR proteins: more than splicing factors
    • Twyffels L, Gueydan C, Kruys V. Shuttling SR proteins: more than splicing factors. FEBS J 2011, 278:3246-3255.
    • (2011) FEBS J , vol.278 , pp. 3246-3255
    • Twyffels, L.1    Gueydan, C.2    Kruys, V.3
  • 164
    • 0035025061 scopus 로고    scopus 로고
    • Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA
    • Huang Y, Steitz JA. Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA. Mol Cell 2001, 7:899-905.
    • (2001) Mol Cell , vol.7 , pp. 899-905
    • Huang, Y.1    Steitz, J.A.2
  • 165
    • 0344211508 scopus 로고    scopus 로고
    • SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
    • Huang Y, Gattoni R, Stevenin J, Steitz JA. SR splicing factors serve as adapter proteins for TAP-dependent mRNA export. Mol Cell 2003, 11:837-843.
    • (2003) Mol Cell , vol.11 , pp. 837-843
    • Huang, Y.1    Gattoni, R.2    Stevenin, J.3    Steitz, J.A.4
  • 166
    • 3843075319 scopus 로고    scopus 로고
    • Hypophosphorylated ASF/SF2 binds TAP and is present in messenger ribonucleoproteins
    • Lai MC, Tarn WY. Hypophosphorylated ASF/SF2 binds TAP and is present in messenger ribonucleoproteins. J Biol Chem 2004, 279:31745-31749.
    • (2004) J Biol Chem , vol.279 , pp. 31745-31749
    • Lai, M.C.1    Tarn, W.Y.2
  • 167
    • 77952313512 scopus 로고    scopus 로고
    • SR proteins SRp20 and 9G8 contribute to efficient export of herpes simplex virus 1 mRNAs
    • Escudero-Paunetto L, Li L, Hernandez FP, Sandri-Goldin RM. SR proteins SRp20 and 9G8 contribute to efficient export of herpes simplex virus 1 mRNAs. Virology 2010, 401:155-164.
    • (2010) Virology , vol.401 , pp. 155-164
    • Escudero-Paunetto, L.1    Li, L.2    Hernandez, F.P.3    Sandri-Goldin, R.M.4
  • 168
    • 34547119966 scopus 로고    scopus 로고
    • The shuttling SR protein 9G8 plays a role in translation of unspliced mRNA containing a constitutive transport element
    • Swartz JE, Bor YC, Misawa Y, Rekosh D, Hammarskjold ML. The shuttling SR protein 9G8 plays a role in translation of unspliced mRNA containing a constitutive transport element. J Biol Chem 2007, 282:19844-19853.
    • (2007) J Biol Chem , vol.282 , pp. 19844-19853
    • Swartz, J.E.1    Bor, Y.C.2    Misawa, Y.3    Rekosh, D.4    Hammarskjold, M.L.5
  • 169
    • 1842632326 scopus 로고    scopus 로고
    • A novel role for shuttling SR proteins in mRNA translation
    • Sanford JR, Gray NK, Beckmann K, Caceres JF. A novel role for shuttling SR proteins in mRNA translation. Genes Dev 2004, 18:755-768.
    • (2004) Genes Dev , vol.18 , pp. 755-768
    • Sanford, J.R.1    Gray, N.K.2    Beckmann, K.3    Caceres, J.F.4
  • 170
    • 42949109848 scopus 로고    scopus 로고
    • The splicing factor SF2/ASF regulates translation initiation by enhancing phosphorylation of 4E-BP1
    • Michlewski G, Sanford JR, Caceres JF. The splicing factor SF2/ASF regulates translation initiation by enhancing phosphorylation of 4E-BP1. Mol Cell 2008, 30:179-189.
    • (2008) Mol Cell , vol.30 , pp. 179-189
    • Michlewski, G.1    Sanford, J.R.2    Caceres, J.F.3
  • 171
    • 84899845940 scopus 로고    scopus 로고
    • The translational landscape of the splicing factor SRSF1 and its role in mitosis
    • Maslon MM, Heras SR, Bellora N, Eyras E, Caceres JF. The translational landscape of the splicing factor SRSF1 and its role in mitosis. eLife 2014, 3:020208.
    • (2014) eLife , vol.3 , pp. 020208
    • Maslon, M.M.1    Heras, S.R.2    Bellora, N.3    Eyras, E.4    Caceres, J.F.5
  • 172
    • 33846505055 scopus 로고    scopus 로고
    • A nucleo-cytoplasmic SR protein functions in viral IRES-mediated translation initiation
    • Bedard KM, Daijogo S, Semler BL. A nucleo-cytoplasmic SR protein functions in viral IRES-mediated translation initiation. EMBO J 2007, 26:459-467.
    • (2007) EMBO J , vol.26 , pp. 459-467
    • Bedard, K.M.1    Daijogo, S.2    Semler, B.L.3
  • 173
    • 77953297915 scopus 로고    scopus 로고
    • SRp40 and SRp55 promote the translation of unspliced human immunodeficiency virus type 1 RNA
    • Swanson CM, Sherer NM, Malim MH. SRp40 and SRp55 promote the translation of unspliced human immunodeficiency virus type 1 RNA. J Virol 2010, 84:6748-6759.
    • (2010) J Virol , vol.84 , pp. 6748-6759
    • Swanson, C.M.1    Sherer, N.M.2    Malim, M.H.3
  • 174
    • 17744393658 scopus 로고    scopus 로고
    • Inhibition of neurogenesis by SRp38, a neuroD-regulated RNA-binding protein
    • Liu KJ, Harland RM. Inhibition of neurogenesis by SRp38, a neuroD-regulated RNA-binding protein. Development 2005, 132:1511-1523.
    • (2005) Development , vol.132 , pp. 1511-1523
    • Liu, K.J.1    Harland, R.M.2
  • 175
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss G, Kim VN, Kataoka N. Messenger-RNA-binding proteins and the messages they carry. Nat Rev Mol Cell Biol 2002, 3:195-205.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 177
    • 0036500149 scopus 로고    scopus 로고
    • Stability of a PKCI-1-related mRNA is controlled by the splicing factor ASF/SF2: a novel function for SR proteins
    • Lemaire R, Prasad J, Kashima T, Gustafson J, Manley JL, Lafyatis R. Stability of a PKCI-1-related mRNA is controlled by the splicing factor ASF/SF2: a novel function for SR proteins. Genes Dev 2002, 16:594-607.
    • (2002) Genes Dev , vol.16 , pp. 594-607
    • Lemaire, R.1    Prasad, J.2    Kashima, T.3    Gustafson, J.4    Manley, J.L.5    Lafyatis, R.6
  • 178
    • 34247330971 scopus 로고    scopus 로고
    • Unproductive splicing of SR genes associated with highly conserved and ultraconserved DNA elements
    • Lareau LF, Inada M, Green RE, Wengrod JC, Brenner SE. Unproductive splicing of SR genes associated with highly conserved and ultraconserved DNA elements. Nature 2007, 446:926-929.
    • (2007) Nature , vol.446 , pp. 926-929
    • Lareau, L.F.1    Inada, M.2    Green, R.E.3    Wengrod, J.C.4    Brenner, S.E.5
  • 179
    • 8844219677 scopus 로고    scopus 로고
    • Involvement of SR proteins in mRNA surveillance
    • Zhang Z, Krainer AR. Involvement of SR proteins in mRNA surveillance. Mol Cell 2004, 16:597-607.
    • (2004) Mol Cell , vol.16 , pp. 597-607
    • Zhang, Z.1    Krainer, A.R.2
  • 180
    • 38649087970 scopus 로고    scopus 로고
    • Efficiency of the pioneer round of translation affects the cellular site of nonsense-mediated mRNA decay
    • Sato H, Hosoda N, Maquat LE. Efficiency of the pioneer round of translation affects the cellular site of nonsense-mediated mRNA decay. Mol Cell 2008, 29:255-262.
    • (2008) Mol Cell , vol.29 , pp. 255-262
    • Sato, H.1    Hosoda, N.2    Maquat, L.E.3
  • 181
    • 0035801373 scopus 로고    scopus 로고
    • The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay
    • Le Hir H, Gatfield D, Izaurralde E, Moore MJ. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay. EMBO J 2001, 20:4987-4997.
    • (2001) EMBO J , vol.20 , pp. 4987-4997
    • Le Hir, H.1    Gatfield, D.2    Izaurralde, E.3    Moore, M.J.4
  • 182
    • 0942268832 scopus 로고    scopus 로고
    • Splicing enhances translation in mammalian cells: an additional function of the exon junction complex
    • Nott A, Le Hir H, Moore MJ. Splicing enhances translation in mammalian cells: an additional function of the exon junction complex. Genes Dev 2004, 18:210-222.
    • (2004) Genes Dev , vol.18 , pp. 210-222
    • Nott, A.1    Le Hir, H.2    Moore, M.J.3
  • 183
    • 84869090905 scopus 로고    scopus 로고
    • The cellular EJC interactome reveals higher-order mRNP structure and an EJC-SR protein nexus
    • Singh G, Kucukural A, Cenik C, Leszyk JD, Shaffer SA, Weng Z, Moore MJ. The cellular EJC interactome reveals higher-order mRNP structure and an EJC-SR protein nexus. Cell 2012, 151:750-764.
    • (2012) Cell , vol.151 , pp. 750-764
    • Singh, G.1    Kucukural, A.2    Cenik, C.3    Leszyk, J.D.4    Shaffer, S.A.5    Weng, Z.6    Moore, M.J.7
  • 185
    • 0028157139 scopus 로고
    • The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein particles
    • Huang M, Rech JE, Northington SJ, Flicker PF, Mayeda A, Krainer AR, LeStourgeon WM. The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein particles. Mol Cell Biol 1994, 14:518-533.
    • (1994) Mol Cell Biol , vol.14 , pp. 518-533
    • Huang, M.1    Rech, J.E.2    Northington, S.J.3    Flicker, P.F.4    Mayeda, A.5    Krainer, A.R.6    LeStourgeon, W.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.