메뉴 건너뛰기




Volumn 42, Issue 13, 2014, Pages 8605-8620

The organization of RNA contacts by PTB for regulation of FAS splicing

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; FAS ANTIGEN; MESSENGER RNA PRECURSOR; POLYPYRIMIDINE TRACT BINDING PROTEIN; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN; RRM4 PROTEIN; UNCLASSIFIED DRUG;

EID: 84905562333     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku519     Document Type: Article
Times cited : (14)

References (48)
  • 2
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk, C. and Gold, L. (1990) Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science, 249, 505-510.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 5
    • 84881493949 scopus 로고    scopus 로고
    • Prediction of clustered RNA-binding protein motif sites in the mammalian genome
    • Zhang, C., Lee, K.Y., Swanson, M.S. and Darnell, R.B. (2013) Prediction of clustered RNA-binding protein motif sites in the mammalian genome. Nucleic Acids Res., 41, 6793-6807.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 6793-6807
    • Zhang, C.1    Lee, K.Y.2    Swanson, M.S.3    Darnell, R.B.4
  • 6
    • 84862679962 scopus 로고    scopus 로고
    • Neuronal regulation of pre-mRNA splicing by polypyrimidine tract binding proteins, PTBP1 and PTBP2
    • Keppetipola, N., Sharma, S., Li, Q. and Black, D.L. (2012) Neuronal regulation of pre-mRNA splicing by polypyrimidine tract binding proteins, PTBP1 and PTBP2. Crit. Rev. Biochem. Mol. Biol., 47, 360-378.
    • (2012) Crit. Rev. Biochem. Mol. Biol. , vol.47 , pp. 360-378
    • Keppetipola, N.1    Sharma, S.2    Li, Q.3    Black, D.L.4
  • 7
    • 49349112872 scopus 로고    scopus 로고
    • Polypyrimidine-tract-binding protein: A multifunctional RNA-binding protein
    • Sawicka, K., Bushell, M., Spriggs, K.A. and Willis, A.E. (2008) Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein. Biochem. Soc. Trans., 36, 641-647.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 641-647
    • Sawicka, K.1    Bushell, M.2    Spriggs, K.A.3    Willis, A.E.4
  • 8
    • 0030878682 scopus 로고    scopus 로고
    • Mutation of PTB binding sites causes misregulation of alternative 3′ splice site selection in vivo
    • Perez, I., Lin, C.H., McAfee, J.G. and Patton, J.G. (1997) Mutation of PTB binding sites causes misregulation of alternative 3′ splice site selection in vivo. RNA, 3, 764-778.
    • (1997) RNA , vol.3 , pp. 764-778
    • Perez, I.1    Lin, C.H.2    McAfee, J.G.3    Patton, J.G.4
  • 9
    • 84893743482 scopus 로고    scopus 로고
    • De novo prediction of PTBP1 binding and splicing targets reveals unexpected features of its RNA recognition and function
    • Han, A., Stoilov, P., Linares, A.J., Zhou, Y., Fu, X.D. and Black, D.L. (2014) De novo prediction of PTBP1 binding and splicing targets reveals unexpected features of its RNA recognition and function. PLoS Comput. Biol., 10, e1003442.
    • (2014) PLoS Comput. Biol. , vol.10
    • Han, A.1    Stoilov, P.2    Linares, A.J.3    Zhou, Y.4    Fu, X.D.5    Black, D.L.6
  • 10
    • 0029055472 scopus 로고
    • Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins
    • Singh, R., Valcarcel, J. and Green, M.R. (1995) Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins. Science, 268, 1173-1176.
    • (1995) Science , vol.268 , pp. 1173-1176
    • Singh, R.1    Valcarcel, J.2    Green, M.R.3
  • 15
    • 66449130983 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein stabilizes the encephalomyocarditis virus IRES structure via binding multiple sites in a unique orientation
    • Kafasla, P., Morgner, N., Poyry, T.A., Curry, S., Robinson, C.V. and Jackson, R.J. (2009) Polypyrimidine tract binding protein stabilizes the encephalomyocarditis virus IRES structure via binding multiple sites in a unique orientation. Mol. Cell, 34, 556-568.
    • (2009) Mol. Cell , vol.34 , pp. 556-568
    • Kafasla, P.1    Morgner, N.2    Poyry, T.A.3    Curry, S.4    Robinson, C.V.5    Jackson, R.J.6
  • 16
    • 78149282522 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein stimulates the poliovirus IRES by modulating eIF4G binding
    • Kafasla, P., Morgner, N., Robinson, C.V. and Jackson, R.J. (2010) Polypyrimidine tract-binding protein stimulates the poliovirus IRES by modulating eIF4G binding. EMBO J., 29, 3710-3722.
    • (2010) EMBO J. , vol.29 , pp. 3710-3722
    • Kafasla, P.1    Morgner, N.2    Robinson, C.V.3    Jackson, R.J.4
  • 17
    • 80455173909 scopus 로고    scopus 로고
    • The mechanism of translation initiation on Aichivirus RNA mediated by a novel type of picornavirus IRES
    • Yu, Y., Sweeney, T.R., Kafasla, P., Jackson, R.J., Pestova, T.V. and Hellen, C.U. (2011) The mechanism of translation initiation on Aichivirus RNA mediated by a novel type of picornavirus IRES. EMBO J., 30, 4423-4436.
    • (2011) EMBO J. , vol.30 , pp. 4423-4436
    • Yu, Y.1    Sweeney, T.R.2    Kafasla, P.3    Jackson, R.J.4    Pestova, T.V.5    Hellen, C.U.6
  • 18
    • 79956202149 scopus 로고    scopus 로고
    • Activation of picornaviral IRESs by PTB shows differential dependence on each PTB RNA-binding domain
    • Kafasla, P., Lin, H., Curry, S. and Jackson, R.J. (2011) Activation of picornaviral IRESs by PTB shows differential dependence on each PTB RNA-binding domain. RNA, 17, 1120-1131.
    • (2011) RNA , vol.17 , pp. 1120-1131
    • Kafasla, P.1    Lin, H.2    Curry, S.3    Jackson, R.J.4
  • 19
    • 0028883219 scopus 로고
    • Directed hydroxyl radical probing of 16S rRNA using Fe(II) tethered to ribosomal protein S4
    • Heilek, G.M., Marusak, R., Meares, C.F. and Noller, H.F. (1995) Directed hydroxyl radical probing of 16S rRNA using Fe(II) tethered to ribosomal protein S4. Proc. Natl. Acad. Sci. U.S.A., 92, 1113-1116.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1113-1116
    • Heilek, G.M.1    Marusak, R.2    Meares, C.F.3    Noller, H.F.4
  • 20
    • 33846665912 scopus 로고    scopus 로고
    • The 5′ end of U2 snRNA is in close proximity to U1 and functional sites of the pre-mRNA in early spliceosomal complexes
    • Donmez, G., Hartmuth, K., Kastner, B., Will, C.L. and Luhrmann, R. (2007) The 5′ end of U2 snRNA is in close proximity to U1 and functional sites of the pre-mRNA in early spliceosomal complexes. Mol. Cell, 25, 399-411.
    • (2007) Mol. Cell , vol.25 , pp. 399-411
    • Donmez, G.1    Hartmuth, K.2    Kastner, B.3    Will, C.L.4    Luhrmann, R.5
  • 21
    • 0036315512 scopus 로고    scopus 로고
    • Early organization of pre-mRNA during spliceosome assembly
    • Kent, O.A. and MacMillan, A.M. (2002) Early organization of pre-mRNA during spliceosome assembly. Nat Struct Biol, 9, 576-581.
    • (2002) Nat Struct Biol , vol.9 , pp. 576-581
    • Kent, O.A.1    Macmillan, A.M.2
  • 22
    • 33745755054 scopus 로고    scopus 로고
    • Proximity of conserved U6 and U2 snRNA elements to the 5′ splice site region in activated spliceosomes
    • Rhode, B.M., Hartmuth, K., Westhof, E. and Luhrmann, R. (2006) Proximity of conserved U6 and U2 snRNA elements to the 5′ splice site region in activated spliceosomes. EMBO J., 25, 2475-2486.
    • (2006) EMBO J. , vol.25 , pp. 2475-2486
    • Rhode, B.M.1    Hartmuth, K.2    Westhof, E.3    Luhrmann, R.4
  • 23
    • 0031985529 scopus 로고    scopus 로고
    • Role of an inhibitory pyrimidine element and polypyrimidine tract binding protein in repression of a regulated alpha-tropomyosin exon
    • Gooding, C., Roberts, G.C. and Smith, C.W. (1998) Role of an inhibitory pyrimidine element and polypyrimidine tract binding protein in repression of a regulated alpha-tropomyosin exon. RNA, 4, 85-100.
    • (1998) RNA , vol.4 , pp. 85-100
    • Gooding, C.1    Roberts, G.C.2    Smith, C.W.3
  • 24
    • 0034977633 scopus 로고    scopus 로고
    • Differential alternative splicing activity of isoforms of polypyrimidine tract binding protein (PTB)
    • Wollerton, M.C., Gooding, C., Robinson, F., Brown, E.C., Jackson, R.J. and Smith, C.W. (2001) Differential alternative splicing activity of isoforms of polypyrimidine tract binding protein (PTB). RNA, 7, 819-832.
    • (2001) RNA , vol.7 , pp. 819-832
    • Wollerton, M.C.1    Gooding, C.2    Robinson, F.3    Brown, E.C.4    Jackson, R.J.5    Smith, C.W.6
  • 28
    • 0028963667 scopus 로고
    • Three functional soluble forms of the human apoptosis-inducing Fas molecule are produced by alternative splicing
    • Cascino, I., Fiucci, G., Papoff, G. and Ruberti, G. (1995) Three functional soluble forms of the human apoptosis-inducing Fas molecule are produced by alternative splicing. J. Immunol., 154, 2706-2713.
    • (1995) J. Immunol. , vol.154 , pp. 2706-2713
    • Cascino, I.1    Fiucci, G.2    Papoff, G.3    Ruberti, G.4
  • 30
    • 78149466662 scopus 로고    scopus 로고
    • Cell-specific regulation of Fas exon 6 splicing mediated by Hu antigen R
    • Izquierdo, J.M. (2012) Cell-specific regulation of Fas exon 6 splicing mediated by Hu antigen R. Biochem. Biophys. Res. Commun., 402, 324-328.
    • (2012) Biochem. Biophys. Res. Commun. , vol.402 , pp. 324-328
    • Izquierdo, J.M.1
  • 31
    • 78650434686 scopus 로고    scopus 로고
    • Heterogeneous ribonucleoprotein C displays a repressor activity mediated by T-cell intracellular antigen-1-related/like protein to modulate Fas exon 6 splicing through a mechanism involving Hu antigen R
    • Izquierdo, J.M. (2010) Heterogeneous ribonucleoprotein C displays a repressor activity mediated by T-cell intracellular antigen-1-related/like protein to modulate Fas exon 6 splicing through a mechanism involving Hu antigen R. Nucleic Acids Res., 38, 8001-8014.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 8001-8014
    • Izquierdo, J.M.1
  • 32
    • 49649128843 scopus 로고    scopus 로고
    • Hu antigen R (HuR) functions as an alternative pre-mRNA splicing regulator of Fas apoptosis-promoting receptor on exon definition
    • Izquierdo, J.M. (2008) Hu antigen R (HuR) functions as an alternative pre-mRNA splicing regulator of Fas apoptosis-promoting receptor on exon definition. J. Biol. Chem., 283, 19077-19084.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19077-19084
    • Izquierdo, J.M.1
  • 33
    • 53149145051 scopus 로고    scopus 로고
    • RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition
    • Bonnal, S., Martinez, C., Forch, P., Bachi, A., Wilm, M. and Valcarcel, J. (2008) RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition. Mol. Cell, 32, 81-95.
    • (2008) Mol. Cell , vol.32 , pp. 81-95
    • Bonnal, S.1    Martinez, C.2    Forch, P.3    Bachi, A.4    Wilm, M.5    Valcarcel, J.6
  • 35
    • 0037121924 scopus 로고    scopus 로고
    • The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5′ splice sites
    • Forch, P., Puig, O., Martinez, C., Seraphin, B. and Valcarcel, J. (2002) The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5′ splice sites. EMBO J., 21, 6882-6892.
    • (2002) EMBO J. , vol.21 , pp. 6882-6892
    • Forch, P.1    Puig, O.2    Martinez, C.3    Seraphin, B.4    Valcarcel, J.5
  • 36
    • 13944278373 scopus 로고    scopus 로고
    • SAFA: Semi-automated footprinting analysis software for high-throughput quantification of nucleic acid footprinting experiments
    • Das, R., Laederach, A., Pearlman, S.M., Herschlag, D. and Altman, R.B. (2005) SAFA: semi-automated footprinting analysis software for high-throughput quantification of nucleic acid footprinting experiments. RNA, 11, 344-354.
    • (2005) RNA , vol.11 , pp. 344-354
    • Das, R.1    Laederach, A.2    Pearlman, S.M.3    Herschlag, D.4    Altman, R.B.5
  • 37
    • 51649119387 scopus 로고    scopus 로고
    • Semiautomated and rapid quantification of nucleic acid footprinting and structure mapping experiments
    • Laederach, A., Das, R., Vicens, Q., Pearlman, S.M., Brenowitz, M., Herschlag, D. and Altman, R.B. (2008) Semiautomated and rapid quantification of nucleic acid footprinting and structure mapping experiments. Nat. Protoc., 3, 1395-1401.
    • (2008) Nat. Protoc. , vol.3 , pp. 1395-1401
    • Laederach, A.1    Das, R.2    Vicens, Q.3    Pearlman, S.M.4    Brenowitz, M.5    Herschlag, D.6    Altman, R.B.7
  • 38
    • 84861714640 scopus 로고    scopus 로고
    • Designing cell-compatible hydrogels for biomedical applications
    • Seliktar, D. (2012) Designing cell-compatible hydrogels for biomedical applications. Science, 336, 1124-1128.
    • (2012) Science , vol.336 , pp. 1124-1128
    • Seliktar, D.1
  • 40
    • 30444459024 scopus 로고    scopus 로고
    • Structure of the two most C-terminal RNA recognition motifs of PTB using segmental isotope labeling
    • Vitali, F., Henning, A., Oberstrass, F.C., Hargous, Y., Auweter, S.D., Erat, M. and Allain, F.H. (2006) Structure of the two most C-terminal RNA recognition motifs of PTB using segmental isotope labeling. EMBO J., 25, 150-162.
    • (2006) EMBO J. , vol.25 , pp. 150-162
    • Vitali, F.1    Henning, A.2    Oberstrass, F.C.3    Hargous, Y.4    Auweter, S.D.5    Erat, M.6    Allain, F.H.7
  • 41
    • 77249156731 scopus 로고    scopus 로고
    • Interactions between PTB RRMs induce slow motions and increase RNA binding affinity
    • Maynard, C.M. and Hall, K.B. (2010) Interactions between PTB RRMs induce slow motions and increase RNA binding affinity. J. Mol. Biol., 397, 260-277.
    • (2010) J. Mol. Biol. , vol.397 , pp. 260-277
    • Maynard, C.M.1    Hall, K.B.2
  • 42
    • 0342927495 scopus 로고    scopus 로고
    • Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold
    • Conte, M.R., Grune, T., Ghuman, J., Kelly, G., Ladas, A., Matthews, S. and Curry, S. (2000) Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold. EMBO J., 19, 3132-3141.
    • (2000) EMBO J. , vol.19 , pp. 3132-3141
    • Conte, M.R.1    Grune, T.2    Ghuman, J.3    Kelly, G.4    Ladas, A.5    Matthews, S.6    Curry, S.7
  • 43
    • 84897939104 scopus 로고    scopus 로고
    • Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB)
    • Joshi, A., Esteve, V., Buckroyd, A., Blatter, M., Allain, F.H. and Curry, S. (2014) Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB). Peer J., 2, e305.
    • (2014) Peer J. , vol.2
    • Joshi, A.1    Esteve, V.2    Buckroyd, A.3    Blatter, M.4    Allain, F.H.5    Curry, S.6
  • 44
    • 0037674850 scopus 로고    scopus 로고
    • A novel polypyrimidine tract-binding protein paralog expressed in smooth muscle cells
    • Gooding, C., Kemp, P. and Smith, C.W. (2003) A novel polypyrimidine tract-binding protein paralog expressed in smooth muscle cells. J. Biol. Chem., 278, 15201-15207.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15201-15207
    • Gooding, C.1    Kemp, P.2    Smith, C.W.3
  • 45
    • 79951996054 scopus 로고    scopus 로고
    • U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression
    • Sharma, S., Maris, C., Allain, F.H. and Black, D.L. (2011) U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression. Mol. Cell, 41, 579-588.
    • (2011) Mol. Cell , vol.41 , pp. 579-588
    • Sharma, S.1    Maris, C.2    Allain, F.H.3    Black, D.L.4
  • 46
    • 84896524463 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein inhibits IgM pre-mRNA splicing by diverting U2 snRNA base-pairing away from the branch point
    • Zheng, X., Cho, S., Moon, H., Loh, T.J., Oh, H.K., Green, M.R. and Shen, H. (2014) Polypyrimidine tract binding protein inhibits IgM pre-mRNA splicing by diverting U2 snRNA base-pairing away from the branch point. RNA, 20, 440-446.
    • (2014) RNA , vol.20 , pp. 440-446
    • Zheng, X.1    Cho, S.2    Moon, H.3    Loh, T.J.4    Oh, H.K.5    Green, M.R.6    Shen, H.7
  • 47
    • 0036214013 scopus 로고    scopus 로고
    • Mutations in RRM4 uncouple the splicing repression and RNA-binding activities of polypyrimidine tract binding protein
    • Liu, H., Zhang, W., Reed, R.B., Liu, W. and Grabowski, P.J. (2002) Mutations in RRM4 uncouple the splicing repression and RNA-binding activities of polypyrimidine tract binding protein. RNA, 8, 137-149.
    • (2002) RNA , vol.8 , pp. 137-149
    • Liu, H.1    Zhang, W.2    Reed, R.B.3    Liu, W.4    Grabowski, P.J.5
  • 48
    • 79952105381 scopus 로고    scopus 로고
    • Understanding splicing regulation through RNA splicing maps
    • Witten, J.T. and Ule, J. (2011) Understanding splicing regulation through RNA splicing maps. Trends Genet., 27, 89-97.
    • (2011) Trends Genet. , vol.27 , pp. 89-97
    • Witten, J.T.1    Ule, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.