메뉴 건너뛰기




Volumn 30, Issue 5, 2016, Pages 553-566

SR proteins are NXF1 adaptors that link alternative RNA processing to mRNA export

Author keywords

Alternative 3 end processing; iCLIP; mRNA export; NXF1; SR protein; SRSF3; SRSF7

Indexed keywords

ADAPTOR PROTEIN; MESSENGER RNA; NUCLEAR EXPORT FACTOR 1; SERINE ARGININE RICH PROTEIN; SRSF3 PROTEIN; SRSF7 PROTEIN; TRANSCRIPTOME; UNCLASSIFIED DRUG; 3' UNTRANSLATED REGION; NUCLEAR PROTEIN; NUCLEOCYTOPLASMIC TRANSPORT PROTEIN; NXF1 PROTEIN, MOUSE; PROTEIN BINDING; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN; SERINE ARGININE RICH SPLICING FACTOR; SFRS2 PROTEIN, MOUSE;

EID: 84959473078     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.276477.115     Document Type: Article
Times cited : (219)

References (64)
  • 1
    • 84865527768 scopus 로고    scopus 로고
    • Detecting differential usage ofexons from RNA-seq data
    • Anders S, Reyes A, HuberW. 2012. Detecting differential usage ofexons from RNA-seq data. Genome Res 22: 2008-2017.
    • (2012) Genome Res , vol.22 , pp. 2008-2017
    • Anders, S.1    Reyes, A.2    Huber, W.3
  • 2
    • 84904469265 scopus 로고    scopus 로고
    • Regulation of gene expression programmes byserine-arginine rich splicing factors
    • Änkö ML. 2014. Regulation of gene expression programmes byserine-arginine rich splicing factors. Semin Cell Dev Biol32: 11-21.
    • (2014) Semin Cell Dev Biol , vol.32 , pp. 11-21
    • Änkö, M.L.1
  • 3
  • 5
    • 61449254471 scopus 로고    scopus 로고
    • Specific combinations of SR proteins associatewith single pre-messenger RNAs in vivo and contribute differentfunctions
    • Björk P, Jin S, Zhao J, Singh OP, Persson JO, Hellman U, Wieslander L. 2009. Specific combinations of SR proteins associatewith single pre-messenger RNAs in vivo and contribute differentfunctions. J Cell Biol 184: 555-568.
    • (2009) J Cell Biol , vol.184 , pp. 555-568
    • Björk, P.1    Jin, S.2    Zhao, J.3    Singh, O.P.4    Persson, J.O.5    Hellman, U.6    Wieslander, L.7
  • 6
    • 84920540237 scopus 로고    scopus 로고
    • SR proteins controla complex network of RNA-processing events
    • Bradley T, Cook ME, Blanchette M. 2015. SR proteins controla complex network of RNA-processing events. RNA 21:75-92.
    • (2015) RNA , vol.21 , pp. 75-92
    • Bradley, T.1    Cook, M.E.2    Blanchette, M.3
  • 7
    • 0035827686 scopus 로고    scopus 로고
    • Overexpressionof TAP/p15 heterodimers bypasses nuclear retentionand stimulates nuclear mRNA export
    • Braun IC, Herold A, Rode M, Conti E, Izaurralde E. 2001. Overexpressionof TAP/p15 heterodimers bypasses nuclear retentionand stimulates nuclear mRNA export. J Biol Chem 276:20536-20543.
    • (2001) J Biol Chem , vol.276 , pp. 20536-20543
    • Braun, I.C.1    Herold, A.2    Rode, M.3    Conti, E.4    Izaurralde, E.5
  • 8
    • 0031929940 scopus 로고    scopus 로고
    • A specific subset ofSR proteins shuttles continuously between the nucleus andthe cytoplasm
    • Caceres JF, Screaton GR, Krainer AR. 1998. A specific subset ofSR proteins shuttles continuously between the nucleus andthe cytoplasm. Genes Dev 12: 55-66.
    • (1998) Genes Dev , vol.12 , pp. 55-66
    • Caceres, J.F.1    Screaton, G.R.2    Krainer, A.R.3
  • 11
    • 33845626622 scopus 로고    scopus 로고
    • HumanmRNA export machinery recruited to the 5' end of mRNA
    • Cheng H, Dufu K, Lee CS, Hsu JL, Dias A, Reed R. 2006. HumanmRNA export machinery recruited to the 5' end of mRNA.Cell 127: 1389-1400.
    • (2006) Cell , vol.127 , pp. 1389-1400
    • Cheng, H.1    Dufu, K.2    Lee, C.S.3    Hsu, J.L.4    Dias, A.5    Reed, R.6
  • 12
    • 82255194389 scopus 로고    scopus 로고
    • The SRSF1 linker induces semi-conservative ESE bindingby cooperating with the RRMs
    • Cho S, Hoang A, Chakrabarti S, Huynh N, Huang DB, Ghosh G.2011. The SRSF1 linker induces semi-conservative ESE bindingby cooperating with the RRMs. Nucleic Acids Res 39:9413-9421.
    • (2011) Nucleic Acids Res , vol.39 , pp. 9413-9421
    • Cho, S.1    Hoang, A.2    Chakrabarti, S.3    Huynh, N.4    Huang, D.B.5    Ghosh, G.6
  • 14
    • 84871401549 scopus 로고    scopus 로고
    • Position-dependent splicing activationand repression by SR and hnRNP proteins rely on commonmechanisms
    • Erkelenz S, Mueller WF, Evans MS, Busch A, Schöneweis K, Hertel KJ, Schaal H. 2013. Position-dependent splicing activationand repression by SR and hnRNP proteins rely on commonmechanisms. RNA 19: 96-102.
    • (2013) RNA , vol.19 , pp. 96-102
    • Erkelenz, S.1    Mueller, W.F.2    Evans, M.S.3    Busch, A.4    Schöneweis, K.5    Hertel, K.J.6    Schaal, H.7
  • 15
    • 79751504755 scopus 로고    scopus 로고
    • Phosphorylation mechanism andstructure of serine-arginine protein kinases
    • Ghosh G, Adams JA. 2011. Phosphorylation mechanism andstructure of serine-arginine protein kinases. FEBS J 278:587-597.
    • (2011) FEBS J , vol.278 , pp. 587-597
    • Ghosh, G.1    Adams, J.A.2
  • 17
    • 33751094078 scopus 로고    scopus 로고
    • The solution structure of REF2-I reveals interdomaininteractions and regions involved in binding mRNA exportfactors and RNA
    • Golovanov AP, Hautbergue GM, Tintaru AM, Lian LY, Wilson SA. 2006. The solution structure of REF2-I reveals interdomaininteractions and regions involved in binding mRNA exportfactors and RNA. RNA 12: 1933-1948.
    • (2006) RNA , vol.12 , pp. 1933-1948
    • Golovanov, A.P.1    Hautbergue, G.M.2    Tintaru, A.M.3    Lian, L.Y.4    Wilson, S.A.5
  • 18
    • 79956225149 scopus 로고    scopus 로고
    • Identification of mRNAsthat are spliced but not exported to the cytoplasm in the absenceof THOC5 in mouse embryo fibroblasts
    • Guria A, Tran DD, Ramachandran S, Koch A, El Bounkari O, Dutta P, Hauser H, Tamura T. 2011. Identification of mRNAsthat are spliced but not exported to the cytoplasm in the absenceof THOC5 in mouse embryo fibroblasts. RNA 17:1048-1056.
    • (2011) RNA , vol.17 , pp. 1048-1056
    • Guria, A.1    Tran, D.D.2    Ramachandran, S.3    Koch, A.4    El Bounkari, O.5    Dutta, P.6    Hauser, H.7    Tamura, T.8
  • 19
    • 79251584960 scopus 로고    scopus 로고
    • SR proteins induce alternative exon skipping throughtheir activities on the flanking constitutive exons
    • Han J, Ding JH, Byeon CW, Kim JH, Hertel KJ, Jeong S, Fu XD.2011. SR proteins induce alternative exon skipping throughtheir activities on the flanking constitutive exons. Mol CellBiol 31: 793-802.
    • (2011) Mol CellBiol , 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
  • 23
    • 84916640509 scopus 로고    scopus 로고
    • The RNAissance family: SR proteinsas multifaceted regulators of gene expression
    • Howard JM, Sanford JR. 2015. The RNAissance family: SR proteinsas multifaceted regulators of gene expression. WileyInterdiscip Rev RNA 6: 93-110.
    • (2015) WileyInterdiscip Rev RNA , vol.6 , pp. 93-110
    • Howard, J.M.1    Sanford, J.R.2
  • 24
    • 0035025061 scopus 로고    scopus 로고
    • Splicing factors SRp20 and 9G8 promotethe nucleocytoplasmic export of mRNA
    • Huang Y, Steitz JA. 2001. Splicing factors SRp20 and 9G8 promotethe nucleocytoplasmic export of mRNA. Mol Cell 7:899-905.
    • (2001) Mol Cell , vol.7 , pp. 899-905
    • Huang, Y.1    Steitz, J.A.2
  • 25
    • 14644445227 scopus 로고    scopus 로고
    • SRprises along a messenger's journey
    • Huang Y, Steitz JA. 2005. SRprises along a messenger's journey.Mol Cell 17: 613-615.
    • (2005) Mol Cell , vol.17 , pp. 613-615
    • Huang, Y.1    Steitz, J.A.2
  • 26
    • 0344211508 scopus 로고    scopus 로고
    • SR splicing factorsserve as adapter proteins for TAP-dependent mRNA export
    • Huang Y, Gattoni R, Stévenin J, Steitz JA. 2003. SR splicing factorsserve as adapter proteins for TAP-dependent mRNA export.Mol Cell 11: 837-843.
    • (2003) Mol Cell , vol.11 , pp. 837-843
    • Huang, Y.1    Gattoni, R.2    Stévenin, J.3    Steitz, J.A.4
  • 27
    • 3042836378 scopus 로고    scopus 로고
    • A molecular link between SRprotein dephosphorylation andmRNAexport
    • Huang Y, Yario TA, Steitz JA. 2004. A molecular link between SRprotein dephosphorylation andmRNAexport. Proc Natl AcadSci 101: 9666-9670.
    • (2004) Proc Natl AcadSci , vol.101 , pp. 9666-9670
    • Huang, Y.1    Yario, T.A.2    Steitz, J.A.3
  • 28
    • 62049085851 scopus 로고    scopus 로고
    • Adaptor Aly and coadaptorThoc5 function in the Tap-p15-mediated nuclear exportof HSP70 mRNA
    • Katahira J, Inoue H, Hurt E, Yoneda Y. 2009. Adaptor Aly and coadaptorThoc5 function in the Tap-p15-mediated nuclear exportof HSP70 mRNA. EMBO J 28: 556-567.
    • (2009) EMBO J , vol.28 , pp. 556-567
    • Katahira, J.1    Inoue, H.2    Hurt, E.3    Yoneda, Y.4
  • 29
    • 78649714014 scopus 로고    scopus 로고
    • Analysis and designof RNA sequencing experiments for identifying isoformregulation
    • Katz Y, Wang ET, Airoldi EM, Burge CB. 2010. Analysis and designof RNA sequencing experiments for identifying isoformregulation. Nat Methods 7: 1009-1015.
    • (2010) Nat Methods , vol.7 , pp. 1009-1015
    • Katz, Y.1    Wang, E.T.2    Airoldi, E.M.3    Burge, C.B.4
  • 30
    • 0037076221 scopus 로고    scopus 로고
    • HEL/UAP56 binds cotranscriptionallyto the Balbiani ring pre-mRNA in an intron-independentmanner and accompanies the BR mRNP to thenuclear pore
    • Kiesler E, Miralles F, Visa N. 2002. HEL/UAP56 binds cotranscriptionallyto the Balbiani ring pre-mRNA in an intron-independentmanner and accompanies the BR mRNP to thenuclear pore. Curr Biol 12: 859-862.
    • (2002) Curr Biol , vol.12 , pp. 859-862
    • Kiesler, E.1    Miralles, F.2    Visa, N.3
  • 32
    • 3843075319 scopus 로고    scopus 로고
    • Hypophosphorylated ASF/SF2 bindsTAP and is present in messenger ribonucleoproteins
    • Lai MC, Tarn WY. 2004. Hypophosphorylated ASF/SF2 bindsTAP and is present in messenger ribonucleoproteins. J BiolChem 279: 31745-31749.
    • (2004) J BiolChem , vol.279 , pp. 31745-31749
    • Lai, M.C.1    Tarn, W.Y.2
  • 33
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosomedeposits multiple proteins 20-24 nucleotides upstreamof mRNA exon-exon junctions
    • Le Hir H, Izaurralde E, Maquat LE, Moore MJ. 2000. The spliceosomedeposits multiple proteins 20-24 nucleotides upstreamof mRNA exon-exon junctions. EMBO J 19: 6860-6869.
    • (2000) EMBO J , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 34
    • 0036500149 scopus 로고    scopus 로고
    • Stability of a PKCI-1-related mRNA is controlled bythe splicing factor ASF/SF2: A novel function for SR proteins
    • Lemaire R, Prasad J, Kashima T, Gustafson J, Manley JL, Lafyatis R. 2002. Stability of a PKCI-1-related mRNA is controlled bythe splicing factor ASF/SF2: a novel function for SR proteins.Genes Dev 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
  • 35
    • 33748635988 scopus 로고    scopus 로고
    • An intron with a constitutive transport element is retainedin a Tap messenger RNA
    • Li Y, Bor YC, Misawa Y, Xue Y, Rekosh D, Hammarskjöld ML.2006. An intron with a constitutive transport element is retainedin a Tap messenger RNA. Nature 443: 234-237.
    • (2006) Nature , vol.443 , pp. 234-237
    • Li, Y.1    Bor, Y.C.2    Misawa, Y.3    Xue, Y.4    Rekosh, D.5    Hammarskjöld, M.L.6
  • 36
    • 27644592554 scopus 로고    scopus 로고
    • Dephosphorylation-dependentsorting of SR splicing factors during mRNP maturation
    • Lin S, Xiao R, Sun P, Xu X, Fu XD. 2005. Dephosphorylation-dependentsorting of SR splicing factors during mRNP maturation.Mol Cell 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
  • 37
    • 0031840978 scopus 로고    scopus 로고
    • Regulationof alternative polyadenylation by U1 snRNPs and SRp20
    • Lou H, Neugebauer KM, Gagel RF, Berget SM. 1998. Regulationof alternative polyadenylation by U1 snRNPs and SRp20.Mol Cell Biol 18: 4977-4985.
    • (1998) Mol Cell Biol , vol.18 , pp. 4977-4985
    • Lou, H.1    Neugebauer, K.M.2    Gagel, R.F.3    Berget, S.M.4
  • 38
    • 84899845940 scopus 로고    scopus 로고
    • Thetranslational landscape of the splicing factor SRSF1 and itsrole in mitosis
    • Maslon MM, Heras SR, Bellora N, Eyras E, Caceres JF. 2014. Thetranslational landscape of the splicing factor SRSF1 and itsrole in mitosis. Elife: e02028.
    • (2014) Elife
    • Maslon, M.M.1    Heras, S.R.2    Bellora, N.3    Eyras, E.4    Caceres, J.F.5
  • 39
    • 22344438756 scopus 로고    scopus 로고
    • Recruitmentof the human TREX complex to mRNA duringsplicing
    • Masuda S, Das R, Cheng H, Hurt E, Dorman N, Reed R. 2005. Recruitmentof the human TREX complex to mRNA duringsplicing. Genes Dev 19: 1512-1517.
    • (2005) Genes Dev , vol.19 , pp. 1512-1517
    • Masuda, S.1    Das, R.2    Cheng, H.3    Hurt, E.4    Dorman, N.5    Reed, R.6
  • 40
    • 5644226291 scopus 로고    scopus 로고
    • SR proteinspreferentially associate with mRNAs in the nucleus and facilitatetheir export to the cytoplasm
    • Masuyama K, Taniguchi I, Kataoka N, Ohno M. 2004. SR proteinspreferentially associate with mRNAs in the nucleus and facilitatetheir export to the cytoplasm. Genes Cells 9: 959-965.
    • (2004) Genes Cells , vol.9 , pp. 959-965
    • Masuyama, K.1    Taniguchi, I.2    Kataoka, N.3    Ohno, M.4
  • 41
    • 42949109848 scopus 로고    scopus 로고
    • The splicing factorSF2/ASF regulates translation initiation by enhancing phosphorylationof 4E-BP1
    • Michlewski G, Sanford JR, Caceres JF. 2008. The splicing factorSF2/ASF regulates translation initiation by enhancing phosphorylationof 4E-BP1. Mol Cell 30: 179-189.
    • (2008) Mol Cell , vol.30 , pp. 179-189
    • Michlewski, G.1    Sanford, J.R.2    Caceres, J.F.3
  • 42
    • 84875229872 scopus 로고    scopus 로고
    • How cells get themessage: Dynamic assembly and function of mRNA-proteincomplexes
    • Müller-McNicoll M, Neugebauer KM. 2013. How cells get themessage: dynamic assembly and function of mRNA-proteincomplexes. Nat Rev Genet 14: 275-287.
    • (2013) Nat Rev Genet , vol.14 , pp. 275-287
    • Müller-McNicoll, M.1    Neugebauer, K.M.2
  • 43
    • 34447527805 scopus 로고    scopus 로고
    • The interactionbetween cap-binding complex and RNA export factor isrequired for intronless mRNA export
    • Nojima T, Hirose T, Kimura H, Hagiwara M. 2007. The interactionbetween cap-binding complex and RNA export factor isrequired for intronless mRNA export. J Biol Chem 282:15645-15651.
    • (2007) J Biol Chem , vol.282 , pp. 15645-15651
    • Nojima, T.1    Hirose, T.2    Kimura, H.3    Hagiwara, M.4
  • 46
    • 27244441805 scopus 로고    scopus 로고
    • Reversible phosphorylationdifferentially affects nuclear and cytoplasmicfunctions of splicing factor 2/alternative splicing factor
    • Sanford JR, Ellis JD, Cazalla D, Caceres JF. 2005. Reversible phosphorylationdifferentially affects nuclear and cytoplasmicfunctions of splicing factor 2/alternative splicing factor. ProcNatl Acad Sci 102: 15042-15047.
    • (2005) ProcNatl Acad Sci , vol.102 , pp. 15042-15047
    • Sanford, J.R.1    Ellis, J.D.2    Cazalla, D.3    Caceres, J.F.4
  • 49
    • 38649087970 scopus 로고    scopus 로고
    • Efficiency of the pioneerround of translation affects the cellular site of nonsense-mediatedmRNA decay
    • Sato H, Hosoda N, Maquat LE. 2008. Efficiency of the pioneerround of translation affects the cellular site of nonsense-mediatedmRNA decay. Mol Cell 29: 255-262.
    • (2008) Mol Cell , vol.29 , pp. 255-262
    • Sato, H.1    Hosoda, N.2    Maquat, L.E.3
  • 50
    • 1242316952 scopus 로고    scopus 로고
    • Arginine-serine-rich domainsbound at splicing enhancers contact the branchpoint to promoteprespliceosome assembly
    • Shen H, Kan JL, Green MR. 2004. Arginine-serine-rich domainsbound at splicing enhancers contact the branchpoint to promoteprespliceosome assembly. Mol Cell 13: 367-376.
    • (2004) Mol Cell , vol.13 , pp. 367-376
    • Shen, H.1    Kan, J.L.2    Green, M.R.3
  • 53
    • 84869090905 scopus 로고    scopus 로고
    • The cellular EJC interactome reveals higherordermRNPstructure and an EJC-SR protein nexus
    • Singh G, Kucukural A, Cenik C, Leszyk JD, Shaffer SA, Weng Z, Moore MJ. 2012. The cellular EJC interactome reveals higherordermRNPstructure and an EJC-SR protein nexus. Cell 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
  • 54
    • 34547119966 scopus 로고    scopus 로고
    • The shuttling SR protein 9G8 plays a role in translationof unspliced mRNA containing a constitutive transport element
    • Swartz JE, Bor YC, Misawa Y, Rekosh D, Hammarskjöld ML.2007. The shuttling SR protein 9G8 plays a role in translationof unspliced mRNA containing a constitutive transport element.J Biol Chem 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    Hammarskjöld, M.L.5
  • 55
    • 37849054264 scopus 로고    scopus 로고
    • ATP-dependent recruitment of exportfactor Aly/REF onto intronless mRNAs by RNA helicaseUAP56
    • Taniguchi I, Ohno M. 2008. ATP-dependent recruitment of exportfactor Aly/REF onto intronless mRNAs by RNA helicaseUAP56. Mol Cell Biol 28: 601-608.
    • (2008) Mol Cell Biol , vol.28 , pp. 601-608
    • Taniguchi, I.1    Ohno, M.2
  • 56
    • 80052504962 scopus 로고    scopus 로고
    • Structure-function studies of nucleocytoplasmic transport ofretroviral genomic RNA by mRNA export factor TAP
    • Teplova M, Wohlbold L, Khin NW, Izaurralde E, Patel DJ. 2011.Structure-function studies of nucleocytoplasmic transport ofretroviral genomic RNA by mRNA export factor TAP. NatStruct Mol Biol 18: 990-998.
    • (2011) NatStruct Mol Biol , vol.18 , pp. 990-998
    • Teplova, M.1    Wohlbold, L.2    Khin, N.W.3    Izaurralde, E.4    Patel, D.J.5
  • 64
    • 59649107040 scopus 로고    scopus 로고
    • An RNA code for the FOX2 splicing regulator revealed bymapping RNA-protein interactions in stem cells
    • Yeo GW, Coufal NG, Liang TY, Peng GE, Fu XD, Gage FH. 2009.An RNA code for the FOX2 splicing regulator revealed bymapping RNA-protein interactions in stem cells. Nat StructMol Biol 16: 130-137.
    • (2009) Nat StructMol Biol , vol.16 , pp. 130-137
    • Yeo, G.W.1    Coufal, N.G.2    Liang, T.Y.3    Peng, G.E.4    Fu, X.D.5    Gage, F.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.