메뉴 건너뛰기




Volumn 28, Issue 13, 2014, Pages 1498-1514

A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins

Author keywords

Binuclear zinc binding domain; CPEB1; CPEB4; Cytoplasmic polyadenylation; Protein RNA interactions; Translational regulation

Indexed keywords

CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN 1; CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN 4; RNA; UNCLASSIFIED DRUG;

EID: 84903757966     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.241133.114     Document Type: Article
Times cited : (68)

References (62)
  • 2
    • 0034692906 scopus 로고    scopus 로고
    • Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target
    • Allain FH, Gilbert DE, Bouvet P, Feigon J. 2000. Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target. J Mol Biol 303: 227-241.
    • (2000) J Mol Biol , vol.303 , pp. 227-241
    • Allain, F.H.1    Gilbert, D.E.2    Bouvet, P.3    Feigon, J.4
  • 4
    • 84873059804 scopus 로고    scopus 로고
    • Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: How the relative orientation between RRMs influences the nucleic acid binding topology
    • Barraud P, Allain FH. 2013. Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology. J Biol NMR 55: 119-138.
    • (2013) J Biol NMR , vol.55 , pp. 119-138
    • Barraud, P.1    Allain, F.H.2
  • 6
    • 42549107372 scopus 로고    scopus 로고
    • A deadenylation negative feedback mechanism governs meiotic metaphase arrest
    • Belloc E, Mendez R. 2008. A deadenylation negative feedback mechanism governs meiotic metaphase arrest. Nature 452: 1017-1021.
    • (2008) Nature , vol.452 , pp. 1017-1021
    • Belloc, E.1    Mendez, R.2
  • 7
    • 49349093646 scopus 로고    scopus 로고
    • Sequential waves of polyadenylation and deadenylation define a translation circuit that drives meiotic progression
    • Belloc E, Pique M, Mendez R. 2008. Sequential waves of polyadenylation and deadenylation define a translation circuit that drives meiotic progression. Biochem Soc Trans 36: 665-670.
    • (2008) Biochem Soc Trans , vol.36 , pp. 665-670
    • Belloc, E.1    Pique, M.2    Mendez, R.3
  • 8
    • 32044432375 scopus 로고    scopus 로고
    • Reduced extinction of hippocampal-dependent memories in CPEB knockout mice
    • Berger-Sweeney J, Zearfoss NR, Richter JD. 2006. Reduced extinction of hippocampal-dependent memories in CPEB knockout mice. Learn Mem 13: 4-7.
    • (2006) Learn Mem , vol.13 , pp. 4-7
    • Berger-Sweeney, J.1    Zearfoss, N.R.2    Richter, J.D.3
  • 11
    • 0033609121 scopus 로고    scopus 로고
    • Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of sex-lethal
    • Crowder SM, Kanaar R, Rio DC, Alber T. 1999. Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of sex-lethal. Proc Natl Acad Sci 96: 4892-4897.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 4892-4897
    • Crowder, S.M.1    Kanaar, R.2    Rio, D.C.3    Alber, T.4
  • 13
    • 0033560759 scopus 로고    scopus 로고
    • Cytoplasmic polyadenylation elements mediate masking and unmasking of cyclin B1 mRNA
    • de Moor CH, Richter JD. 1999. Cytoplasmic polyadenylation elements mediate masking and unmasking of cyclin B1 mRNA. EMBO J 18: 2294-2303.
    • (1999) EMBO J , vol.18 , pp. 2294-2303
    • de Moor, C.H.1    Richter, J.D.2
  • 14
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • Deo RC, Bonanno JB, Sonenberg N, Burley SK. 1999. Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell 98: 835-845.
    • (1999) Cell , vol.98 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 15
    • 46449139041 scopus 로고    scopus 로고
    • Spindle-localized CPE-mediated translation controls meiotic chromosome segregation
    • Eliscovich C, Peset I, Vernos I, Mendez R. 2008. Spindle-localized CPE-mediated translation controls meiotic chromosome segregation. Nat Cell Biol 10: 858-865.
    • (2008) Nat Cell Biol , vol.10 , pp. 858-865
    • Eliscovich, C.1    Peset, I.2    Vernos, I.3    Mendez, R.4
  • 17
    • 84866520245 scopus 로고    scopus 로고
    • The CPEB-family of proteins, translational control in senescence and cancer
    • Fernandez-Miranda G, Mendez R. 2012. The CPEB-family of proteins, translational control in senescence and cancer. Ageing Res Rev 11: 460-472.
    • (2012) Ageing Res Rev , vol.11 , pp. 460-472
    • Fernandez-Miranda, G.1    Mendez, R.2
  • 18
    • 0024820904 scopus 로고
    • Poly(A) addition during maturation of frog oocytes: Distinct nuclear and cytoplasmic activities and regulation by the sequence UUUUUAU
    • Fox CA, Sheets MD, Wickens MP. 1989. Poly(A) addition during maturation of frog oocytes: distinct nuclear and cytoplasmic activities and regulation by the sequence UUUUUAU. Genes Dev 3: 2151-2162.
    • (1989) Genes Dev , vol.3 , pp. 2151-2162
    • Fox, C.A.1    Sheets, M.D.2    Wickens, M.P.3
  • 19
    • 0028029983 scopus 로고
    • CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation
    • Hake LE, Richter JD. 1994. CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation. Cell 79: 617-627.
    • (1994) Cell , vol.79 , pp. 617-627
    • Hake, L.E.1    Richter, J.D.2
  • 20
    • 0031883566 scopus 로고    scopus 로고
    • Specificity of RNA binding by CPEB: Requirement for RNA recognition motifs and a novel zinc finger
    • Hake LE, Mendez R, Richter JD. 1998. Specificity of RNA binding by CPEB: requirement for RNA recognition motifs and a novel zinc finger. Mol Cell Biol 18: 685-693.
    • (1998) Mol Cell Biol , vol.18 , pp. 685-693
    • Hake, L.E.1    Mendez, R.2    Richter, J.D.3
  • 22
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Guntert P, Wuthrich K. 2002a. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biomol 319: 209-227.
    • (2002) J Mol Biomol , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 23
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann T, Guntert P, Wuthrich K. 2002b. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 24: 171-189.
    • (2002) J Biomol NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 24
    • 33750220093 scopus 로고    scopus 로고
    • CPEB3 and CPEB4 in neurons: Analysis of RNA-binding specificity and translational control of AMPA receptor GluR2 mRNA
    • Huang YS, Kan MC, Lin CL, Richter JD. 2006. CPEB3 and CPEB4 in neurons: analysis of RNA-binding specificity and translational control of AMPA receptor GluR2 mRNA. EMBO J 25: 4865-4876.
    • (2006) EMBO J , vol.25 , pp. 4865-4876
    • Huang, Y.S.1    Kan, M.C.2    Lin, C.L.3    Richter, J.D.4
  • 25
    • 77954955355 scopus 로고    scopus 로고
    • Meiosis requires a translational positive loop where CPEB1 ensues its replacement by CPEB4
    • Igea A, Mendez R. 2010. Meiosis requires a translational positive loop where CPEB1 ensues its replacement by CPEB4. EMBO J 29: 2182-2193.
    • (2010) EMBO J , vol.29 , pp. 2182-2193
    • Igea, A.1    Mendez, R.2
  • 26
    • 82955205878 scopus 로고    scopus 로고
    • Crystallographic analysis of polypyrimidine tract-binding protein-Raver1 interactions involved in regulation of alternative splicing
    • Joshi A, Coelho MB, Kotik-Kogan O, Simpson PJ, Matthews SJ, Smith CW, Curry S. 2011. Crystallographic analysis of polypyrimidine tract-binding protein-Raver1 interactions involved in regulation of alternative splicing. Structure 19: 1816-1825.
    • (2011) Structure , vol.19 , pp. 1816-1825
    • Joshi, A.1    Coelho, M.B.2    Kotik-Kogan, O.3    Simpson, P.J.4    Matthews, S.J.5    Smith, C.W.6    Curry, S.7
  • 28
    • 0035823011 scopus 로고    scopus 로고
    • A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer
    • Kielkopf CL, Rodionova NA, Green MR, Burley SK. 2001. A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer. Cell 106: 595-605.
    • (2001) Cell , vol.106 , pp. 595-605
    • Kielkopf, C.L.1    Rodionova, N.A.2    Green, M.R.3    Burley, S.K.4
  • 29
    • 3042737403 scopus 로고    scopus 로고
    • U2AF homology motifs: Protein recognition in the RRM world
    • Kielkopf CL, Lucke S, Green MR. 2004. U2AF homology motifs: protein recognition in the RRM world. Genes Dev 18: 1513-1526.
    • (2004) Genes Dev , vol.18 , pp. 1513-1526
    • Kielkopf, C.L.1    Lucke, S.2    Green, M.R.3
  • 31
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 29-32
    • Koradi R, Billeter M, Wuthrich K. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14: 51-55, 29-32.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 33
    • 75149173478 scopus 로고    scopus 로고
    • The nuclear experience of CPEB: Implications for RNA processing and translational control
    • Lin CL, Evans V, Shen S, Xing Y, Richter JD. 2010. The nuclear experience of CPEB: implications for RNA processing and translational control. RNA 16: 338-348.
    • (2010) RNA , vol.16 , pp. 338-348
    • Lin, C.L.1    Evans, V.2    Shen, S.3    Xing, Y.4    Richter, J.D.5
  • 36
    • 0024687134 scopus 로고
    • Poly(A) elongation during Xenopus oocyte maturation is required for translational recruitment and is mediated by a short sequence element
    • McGrew LL, Dworkin-Rastl E, Dworkin MB, Richter JD. 1989. Poly(A) elongation during Xenopus oocyte maturation is required for translational recruitment and is mediated by a short sequence element. Genes Dev 3: 803-815.
    • (1989) Genes Dev , vol.3 , pp. 803-815
    • McGrew, L.L.1    Dworkin-Rastl, E.2    Dworkin, M.B.3    Richter, J.D.4
  • 37
    • 0033634850 scopus 로고    scopus 로고
    • Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an active cytoplasmic polyadenylation complex
    • Mendez R, Murthy KG, Ryan K, Manley JL, Richter JD. 2000. Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an active cytoplasmic polyadenylation complex. Mol Cell 6: 1253-1259.
    • (2000) Mol Cell , vol.6 , pp. 1253-1259
    • Mendez, R.1    Murthy, K.G.2    Ryan, K.3    Manley, J.L.4    Richter, J.D.5
  • 38
    • 0037007233 scopus 로고    scopus 로고
    • Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction
    • Mendez R, Barnard D, Richter JD. 2002. Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction. EMBO J 21: 1833-1844.
    • (2002) EMBO J , vol.21 , pp. 1833-1844
    • Mendez, R.1    Barnard, D.2    Richter, J.D.3
  • 39
    • 84877723134 scopus 로고    scopus 로고
    • The C-terminal region of cytoplasmic polyadenylation element binding protein is a ZZ domain with potential for protein-protein interactions
    • Merkel DJ, Wells SB, Hilburn BC, Elazzouzi F, Perez-Alvarado GC, Lee BM. 2013. The C-terminal region of cytoplasmic polyadenylation element binding protein is a ZZ domain with potential for protein-protein interactions. J Mol Biol 425: 2015-2026.
    • (2013) J Mol Biol , vol.425 , pp. 2015-2026
    • Merkel, D.J.1    Wells, S.B.2    Hilburn, B.C.3    Elazzouzi, F.4    Perez-Alvarado, G.C.5    Lee, B.M.6
  • 40
    • 77951978351 scopus 로고    scopus 로고
    • Mitotic cellcycle progression is regulated by CPEB1 and CPEB4-dependent translational control
    • Novoa I, Gallego J, Ferreira PG, Mendez R. 2010. Mitotic cellcycle progression is regulated by CPEB1 and CPEB4-dependent translational control. Nat Cell Biol 12: 447-456.
    • (2010) Nat Cell Biol , vol.12 , pp. 447-456
    • Novoa, I.1    Gallego, J.2    Ferreira, P.G.3    Mendez, R.4
  • 44
    • 33746296753 scopus 로고    scopus 로고
    • Grabbing the message: Structural basis of mRNA 39UTR recognition by Hrp1
    • Perez-Canadillas JM. 2006. Grabbing the message: structural basis of mRNA 39UTR recognition by Hrp1. EMBO J 25: 3167-3178.
    • (2006) EMBO J , vol.25 , pp. 3167-3178
    • Perez-Canadillas, J.M.1
  • 45
    • 1242340502 scopus 로고    scopus 로고
    • New applications of 2D filtered/edited NOESY for assignment and structure elucidation of RNA and RNA-protein complexes
    • Peterson RD, Theimer CA, Wu H, Feigon J. 2004. New applications of 2D filtered/edited NOESY for assignment and structure elucidation of RNA and RNA-protein complexes. J Biomol NMR 28: 59-67.
    • (2004) J Biomol NMR , vol.28 , pp. 59-67
    • Peterson, R.D.1    Theimer, C.A.2    Wu, H.3    Feigon, J.4
  • 46
    • 38849190013 scopus 로고    scopus 로고
    • A combinatorial code for CPE-mediated translational control
    • Pique M, Lopez JM, Foissac S, Guigo R, Mendez R. 2008. A combinatorial code for CPE-mediated translational control. Cell 132: 434-448.
    • (2008) Cell , vol.132 , pp. 434-448
    • Pique, M.1    Lopez, J.M.2    Foissac, S.3    Guigo, R.4    Mendez, R.5
  • 47
    • 34249908103 scopus 로고    scopus 로고
    • CPEB: A life in translation
    • Richter JD. 2007. CPEB: a life in translation. Trends Biochem Sci 32: 279-285.
    • (2007) Trends Biochem Sci , vol.32 , pp. 279-285
    • Richter, J.D.1
  • 49
    • 84869085954 scopus 로고    scopus 로고
    • Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G
    • Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. 2012. Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. Mol Cell 48: 375-386.
    • (2012) Mol Cell , vol.48 , pp. 375-386
    • Safaee, N.1    Kozlov, G.2    Noronha, A.M.3    Xie, J.4    Wilds, C.J.5    Gehring, K.6
  • 50
    • 0032506009 scopus 로고    scopus 로고
    • TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
    • Salzmann M, Pervushin K, Wider G, Senn H, Wuthrich K. 1998. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc Natl Acad Sci 95: 13585-13590.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wuthrich, K.5
  • 51
    • 36749104324 scopus 로고    scopus 로고
    • Mechanism of degradation of CPEB during Xenopus oocyte maturation
    • Setoyama D, Yamashita M, Sagata N. 2007. Mechanism of degradation of CPEB during Xenopus oocyte maturation. Proc Natl Acad Sci 104: 18001-18006.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 18001-18006
    • Setoyama, D.1    Yamashita, M.2    Sagata, N.3
  • 52
    • 36349027062 scopus 로고    scopus 로고
    • Improved segmental isotope labeling methods for the NMR study of multidomain or large proteins: Application to the RRMs of Npl3p and hnRNP L
    • Skrisovska L, Allain FH. 2008. Improved segmental isotope labeling methods for the NMR study of multidomain or large proteins: application to the RRMs of Npl3p and hnRNP L. J Mol Biol 375: 151-164.
    • (2008) J Mol Biol , vol.375 , pp. 151-164
    • Skrisovska, L.1    Allain, F.H.2
  • 54
    • 30444459024 scopus 로고    scopus 로고
    • Structure of the two most Cterminal RNA recognition motifs of PTB using segmental isotope labeling
    • Vitali F, Henning A, Oberstrass FC, Hargous Y, Auweter SD, Erat M, Allain FH. 2006. Structure of the two most Cterminal 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
  • 55
    • 77957107437 scopus 로고    scopus 로고
    • Comparative in silico analyses of cpeb1-4 with functional predictions
    • Wang XP, Cooper NG. 2010. Comparative in silico analyses of cpeb1-4 with functional predictions. Bioinform Biol insights 4: 61-83.
    • (2010) Bioinform Biol insights , vol.4 , pp. 61-83
    • Wang, X.P.1    Cooper, N.G.2
  • 56
    • 84875467178 scopus 로고    scopus 로고
    • The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes conformational changes during RNA binding
    • Wang H, Zeng F, Liu Q, Liu H, Liu Z, Niu L, Teng M, Li X. 2013. The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes conformational changes during RNA binding. Acta Crystallogr D Biol Crystallogr 69: 373-380.
    • (2013) Acta Crystallogr D Biol Crystallogr , vol.69 , pp. 373-380
    • Wang, H.1    Zeng, F.2    Liu, Q.3    Liu, H.4    Liu, Z.5    Niu, L.6    Teng, M.7    Li, X.8
  • 57
    • 84861911071 scopus 로고    scopus 로고
    • Translational control by changes in poly(A) tail length: Recycling mRNAs
    • Weill L, Belloc E, Bava FA, Mendez R. 2012. Translational control by changes in poly(A) tail length: recycling mRNAs. Nat Struct Mol Biol 19: 577-585.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 577-585
    • Weill, L.1    Belloc, E.2    Bava, F.A.3    Mendez, R.4
  • 59
    • 84881232947 scopus 로고    scopus 로고
    • Crystal structures and RNA-binding properties of the RNA recognition motifs of heterogeneous nuclear ribonucleoprotein L: Insights into its roles in alternative splicing regulation
    • Zhang W, Zeng F, Liu Y, Zhao Y, Lv H, Niu L, Teng M, Li X. 2013. Crystal structures and RNA-binding properties of the RNA recognition motifs of heterogeneous nuclear ribonucleoprotein L: insights into its roles in alternative splicing regulation. J Biol Chem 288: 22636-22649.
    • (2013) J Biol Chem , vol.288 , pp. 22636-22649
    • Zhang, W.1    Zeng, F.2    Liu, Y.3    Zhao, Y.4    Lv, H.5    Niu, L.6    Teng, M.7    Li, X.8
  • 60
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng N, Wang P, Jeffrey PD, Pavletich NP. 2000. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102: 533-539.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 61
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage l N-peptide/boxB RNA complex
    • Zwahlen C, Legault P, Vincent SJF, Greenblatt J, Konrat R, Kay LE. 1997. Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage l N-peptide/boxB RNA complex. J Am Chem Soc 119: 6711-6721.
    • (1997) J Am Chem Soc , vol.119 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6
  • 62
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR
    • Zweckstetter M, Bax A. 2000. Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR. J Am Chem Soc 122: 3791-3792.
    • (2000) J Am Chem Soc , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.