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Volumn 26, Issue 17, 2007, Pages 3936-3944

Structural insights into the transcriptional and translational roles of Ebp1

Author keywords

Crystal structure; Ebp1 ITAF45 PA2G4; IRES; RNA binding; Translation initiation

Indexed keywords

BINDING PROTEIN; ERBB3 BINDING PROTEIN 1; METHIONYL AMINOPEPTIDASE; POLYPYRIMIDINE TRACT BINDING PROTEIN; PROTEIN; RNA; UNCLASSIFIED DRUG;

EID: 34548387149     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601817     Document Type: Article
Times cited : (82)

References (55)
  • 1
    • 33646759590 scopus 로고    scopus 로고
    • Nuclear Akt associates with PKC-phosphorylated Ebp1, preventing DNA fragmentation by inhibition of caspase-activated DNase
    • Ahn JY, Liu X, Liu Z, Pereira L, Cheng D, Peng J, Wade PA, Hamburger AW, Ye K (2006) Nuclear Akt associates with PKC-phosphorylated Ebp1, preventing DNA fragmentation by inhibition of caspase-activated DNase. EMBO J 25: 2083-2095
    • (2006) EMBO J , vol.25 , pp. 2083-2095
    • Ahn, J.Y.1    Liu, X.2    Liu, Z.3    Pereira, L.4    Cheng, D.5    Peng, J.6    Wade, P.A.7    Hamburger, A.W.8    Ye, K.9
  • 2
    • 0028198617 scopus 로고
    • Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold
    • Bazan JF, Weaver LH, Roderick SL, Huber R, Matthews BW (1994) Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold. Proc Natl Acad Sci USA 91: 2473-2477
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2473-2477
    • Bazan, J.F.1    Weaver, L.H.2    Roderick, S.L.3    Huber, R.4    Matthews, B.W.5
  • 3
    • 33646777450 scopus 로고    scopus 로고
    • Identification of Ebp1 as a component of cytoplasmic bcl-2 mRNP (messenger ribonucleoprotein particle) complexes
    • Bose SK, Sengupta TK, Bandyopadhyay S, Spicer EK (2006) Identification of Ebp1 as a component of cytoplasmic bcl-2 mRNP (messenger ribonucleoprotein particle) complexes. Biochem J 396: 99-107
    • (2006) Biochem J , vol.396 , pp. 99-107
    • Bose, S.K.1    Sengupta, T.K.2    Bandyopadhyay, S.3    Spicer, E.K.4
  • 5
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computer Project No. 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763
    • Collaborative Computer Project No. 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763
  • 6
    • 0342927495 scopus 로고    scopus 로고
    • Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold
    • Conte MR, Grüne T, Ghuman J, Kelly G, Ladas A, Matthews S, 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    Grüne, T.2    Ghuman, J.3    Kelly, G.4    Ladas, A.5    Matthews, S.6    Curry, S.7
  • 7
    • 0028177935 scopus 로고
    • Trans complementation by RNA of defective foot-and-mouth disease virus internal ribosome entry site elements
    • Drew J, Belsham GJ (1994) Trans complementation by RNA of defective foot-and-mouth disease virus internal ribosome entry site elements. J Virol 68: 697-703
    • (1994) J Virol , vol.68 , pp. 697-703
    • Drew, J.1    Belsham, G.J.2
  • 8
    • 33646853354 scopus 로고    scopus 로고
    • Mapping a nucleolar targeting sequence of an RNA binding nucleolar protein, Nop25
    • Fujiwara T, Suzuki S, Kanno M, Sugiyama H, Takahashi H, Tanaka J (2006) Mapping a nucleolar targeting sequence of an RNA binding nucleolar protein, Nop25. Exp Cell Res 312: 1703-1712
    • (2006) Exp Cell Res , vol.312 , pp. 1703-1712
    • Fujiwara, T.1    Suzuki, S.2    Kanno, M.3    Sugiyama, H.4    Takahashi, H.5    Tanaka, J.6
  • 10
    • 0035396727 scopus 로고    scopus 로고
    • Internal ribosome entry sites in eukaryotic mRNA molecules
    • Hellen CU, Sarnow P (2001) Internal ribosome entry sites in eukaryotic mRNA molecules. Genes Dev 15: 1593-1612
    • (2001) Genes Dev , vol.15 , pp. 1593-1612
    • Hellen, C.U.1    Sarnow, P.2
  • 12
    • 0033557935 scopus 로고    scopus 로고
    • unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA
    • Hunt SL, Hsuan JJ, Totty N, Jackson RJ (1999) unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA. Genes Dev 13: 437-448
    • (1999) Genes Dev , vol.13 , pp. 437-448
    • Hunt, S.L.1    Hsuan, J.J.2    Totty, N.3    Jackson, R.J.4
  • 14
    • 28844476749 scopus 로고    scopus 로고
    • Alternative mechanisms of initiating translation of mammalian mRNAs
    • Jackson RJ (2005) Alternative mechanisms of initiating translation of mammalian mRNAs. Biochem Soc Trans 33: 1231-1241
    • (2005) Biochem Soc Trans , vol.33 , pp. 1231-1241
    • Jackson, R.J.1
  • 15
    • 0023758546 scopus 로고
    • A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
    • Jang SK, Krausslich HG, Nicklin MJ, Duke GM, Palmenberg AC, Wimmer E (1988) A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J Virol 62: 2636-2643
    • (1988) J Virol , vol.62 , pp. 2636-2643
    • Jang, S.K.1    Krausslich, H.G.2    Nicklin, M.J.3    Duke, G.M.4    Palmenberg, A.C.5    Wimmer, E.6
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47 (Part 2): 110-119
    • (1991) Acta Crystallogr A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D 60: 2256-2268
    • (2004) Acta Crystallogr D , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 19
    • 0035946549 scopus 로고    scopus 로고
    • Regulation of the ErbB3 binding protein Ebp1 by protein kinase C
    • Lessor TJ, Hamburger AW (2001) Regulation of the ErbB3 binding protein Ebp1 by protein kinase C. Mol Cell Endocrinol 175: 185-191
    • (2001) Mol Cell Endocrinol , vol.175 , pp. 185-191
    • Lessor, T.J.1    Hamburger, A.W.2
  • 20
    • 0034054236 scopus 로고    scopus 로고
    • Ectopic expression of the ErbB-3 binding protein ebp1 inhibits growth and induces differentiation of human breast cancer cell lines
    • Lessor TJ, Yoo JY, Xia X, Woodford N, Hamburger AW (2000) Ectopic expression of the ErbB-3 binding protein ebp1 inhibits growth and induces differentiation of human breast cancer cell lines. J Cell Physiol 183: 321-329
    • (2000) J Cell Physiol , vol.183 , pp. 321-329
    • Lessor, T.J.1    Yoo, J.Y.2    Xia, X.3    Woodford, N.4    Hamburger, A.W.5
  • 21
    • 0032515029 scopus 로고    scopus 로고
    • Structure of human methionine aminopeptidase-2 complexed with fumagillin
    • Liu S, Widom J, Kemp CW, Crews CM, Clardy J (1998) Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science 282: 1324-1327
    • (1998) Science , vol.282 , pp. 1324-1327
    • Liu, S.1    Widom, J.2    Kemp, C.W.3    Crews, C.M.4    Clardy, J.5
  • 22
    • 33746660688 scopus 로고    scopus 로고
    • Ebp1 isoforms distinctively regulate cell survival and differentiation
    • Liu Z, Ahn JY, Liu X, Ye K (2006) Ebp1 isoforms distinctively regulate cell survival and differentiation. Proc Natl Acad Sci USA 103: 10917-10922
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10917-10922
    • Liu, Z.1    Ahn, J.Y.2    Liu, X.3    Ye, K.4
  • 23
    • 0036882401 scopus 로고    scopus 로고
    • Metalloaminopeptidases: Common functional themes in disparate structural surroundings
    • Lowther WT, Matthews BW (2002) Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chem Rev 102: 4581-4608
    • (2002) Chem Rev , vol.102 , pp. 4581-4608
    • Lowther, W.T.1    Matthews, B.W.2
  • 24
    • 0037349339 scopus 로고    scopus 로고
    • The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr
    • Mitchell SA, Spriggs KA, Coldwell MJ, Jackson RJ, Willis AE (2003) The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr. Mol Cell 11: 757-771
    • (2003) Mol Cell , vol.11 , pp. 757-771
    • Mitchell, S.A.1    Spriggs, K.A.2    Coldwell, M.J.3    Jackson, R.J.4    Willis, A.E.5
  • 25
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris RJ, Perrakis A, Lamzin VS (2003) ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol 374: 229-244
    • (2003) Methods Enzymol , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 26
    • 14644393728 scopus 로고    scopus 로고
    • Crystal structure of Mil (Mth680): Internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases
    • Ng CL, Waterman D, Koonin EV, Antson AA, Ortiz-Lombardia M (2005) Crystal structure of Mil (Mth680): internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases. EMBO Rep 6: 140-146
    • (2005) EMBO Rep , vol.6 , pp. 140-146
    • CL, N.1    Waterman, D.2    Koonin, E.V.3    Antson, A.A.4    Ortiz-Lombardia, M.5
  • 28
    • 33645846607 scopus 로고    scopus 로고
    • Human methionine aminopeptidase type 2 in complex with L- and D-methionine
    • Nonato MC, Widom J, Clardy J (2006) Human methionine aminopeptidase type 2 in complex with L- and D-methionine. Bioorg Med Chem Lett 16: 2580-2583
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 2580-2583
    • Nonato, M.C.1    Widom, J.2    Clardy, J.3
  • 30
    • 0023720048 scopus 로고
    • Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
    • Pelletier J, Sonenberg N (1988) Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA. Nature 334: 320-325
    • (1988) Nature , vol.334 , pp. 320-325
    • Pelletier, J.1    Sonenberg, N.2
  • 31
    • 0041372953 scopus 로고    scopus 로고
    • Multiple RRMs contribute to RNA binding specificity and affinity for polypyrimidine tract binding protein
    • Pérez I, McAfee JG, Patton JG (1997) Multiple RRMs contribute to RNA binding specificity and affinity for polypyrimidine tract binding protein. Biochemistry 36: 11881-11890
    • (1997) Biochemistry , vol.36 , pp. 11881-11890
    • Pérez, I.1    McAfee, J.G.2    Patton, J.G.3
  • 34
    • 13244295627 scopus 로고    scopus 로고
    • The LxxLL motif: A multi-functional binding sequence in transcriptional regulation
    • Plevin MJ, Mills MM, Ikura M (2005) The LxxLL motif: a multi-functional binding sequence in transcriptional regulation. Trends Biochem Sci 30: 66-69
    • (2005) Trends Biochem Sci , vol.30 , pp. 66-69
    • Plevin, M.J.1    Mills, M.M.2    Ikura, M.3
  • 35
    • 0034612372 scopus 로고    scopus 로고
    • A brain-enriched polypyrimidine tract-binding protein antagonizes the ability of Nova to regulate neuron-specific alternative splicing
    • Polydorides AD, Okano HJ, Yang YY, Stefani G, Darnell RB (2000) A brain-enriched polypyrimidine tract-binding protein antagonizes the ability of Nova to regulate neuron-specific alternative splicing. Proc Natl Acad Sci USA 97: 6350-6355
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6350-6355
    • Polydorides, A.D.1    Okano, H.J.2    Yang, Y.Y.3    Stefani, G.4    Darnell, R.B.5
  • 36
    • 0029165986 scopus 로고
    • Molecular cloning of a murine cDNA encoding a novel protein, p38-2G4, which varies with the cell cycle
    • Radomski N, Jost E (1995) Molecular cloning of a murine cDNA encoding a novel protein, p38-2G4, which varies with the cell cycle. Exp Cell Res 220: 434-445
    • (1995) Exp Cell Res , vol.220 , pp. 434-445
    • Radomski, N.1    Jost, E.2
  • 38
    • 0031956963 scopus 로고    scopus 로고
    • Recognition of picornavirus internal ribosome entry sites within cells; influence of cellular and viral proteins
    • Roberts LO, Seamons RA, Belsham GJ (1998) Recognition of picornavirus internal ribosome entry sites within cells; influence of cellular and viral proteins. RNA 4: 520-529
    • (1998) RNA , vol.4 , pp. 520-529
    • Roberts, L.O.1    Seamons, R.A.2    Belsham, G.J.3
  • 39
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31: 3381-3385
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 41
    • 3042620165 scopus 로고    scopus 로고
    • EBP1 is a nucleolar growth-regulating protein that is part of pre-ribosomal ribonucleoprotein complexes
    • Squatrito M, Mancino M, Donzelli M, Areces LB, Draetta GF (2004) EBP1 is a nucleolar growth-regulating protein that is part of pre-ribosomal ribonucleoprotein complexes. Oncogene 23: 4454-4465
    • (2004) Oncogene , vol.23 , pp. 4454-4465
    • Squatrito, M.1    Mancino, M.2    Donzelli, M.3    Areces, L.B.4    Draetta, G.F.5
  • 42
    • 33646164893 scopus 로고    scopus 로고
    • Ebp1 is a dsRNA-binding protein associated with ribosomes that modulates eIF2alpha phosphorylation
    • Squatrito M, Mancino M, Sala L, Draetta GF (2006) Ebp1 is a dsRNA-binding protein associated with ribosomes that modulates eIF2alpha phosphorylation. Biochem Biophys Res Commun 344: 859-868
    • (2006) Biochem Biophys Res Commun , vol.344 , pp. 859-868
    • Squatrito, M.1    Mancino, M.2    Sala, L.3    Draetta, G.F.4
  • 43
    • 0035040192 scopus 로고    scopus 로고
    • A novel protein-RNA binding assay: Functional interactions of the foot-and-mouth disease virus internal ribosome entry site with cellular proteins
    • Stassinopoulos IA, Belsham GJ (2001) A novel protein-RNA binding assay: functional interactions of the foot-and-mouth disease virus internal ribosome entry site with cellular proteins. RNA 7: 114-122
    • (2001) RNA , vol.7 , pp. 114-122
    • Stassinopoulos, I.A.1    Belsham, G.J.2
  • 44
    • 2342633872 scopus 로고    scopus 로고
    • Cellular internal ribosome entry segments: Structures, trans-acting factors and regulation of gene expression
    • Stoneley M, Willis AE (2004) Cellular internal ribosome entry segments: structures, trans-acting factors and regulation of gene expression. Oncogene 23: 3200-3207
    • (2004) Oncogene , vol.23 , pp. 3200-3207
    • Stoneley, M.1    Willis, A.E.2
  • 47
    • 0036183980 scopus 로고    scopus 로고
    • The sigma(70)-like motif: A eukaryotic RNA binding domain unique to a superfamily of proteins required for ribosome biogenesis
    • Wehner KA, Baserga SJ (2002) The sigma(70)-like motif: a eukaryotic RNA binding domain unique to a superfamily of proteins required for ribosome biogenesis. Mol Cell 9: 329-339
    • (2002) Mol Cell , vol.9 , pp. 329-339
    • Wehner, K.A.1    Baserga, S.J.2
  • 48
    • 0035059136 scopus 로고    scopus 로고
    • Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb transcriptional regulation
    • Xia X, Cheng A, Lessor T, Zhang Y, Hamburger AW (2001) Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb transcriptional regulation. J Cell Physiol 187: 209-217
    • (2001) J Cell Physiol , vol.187 , pp. 209-217
    • Xia, X.1    Cheng, A.2    Lessor, T.3    Zhang, Y.4    Hamburger, A.W.5
  • 49
    • 0028065287 scopus 로고
    • A fission yeast gene encoding a protein that preferentially associates with curved DNA
    • Yamada H, Mori H, Momoi H, Nakagawa Y, Ueguchi C, Mizuno T (1994) A fission yeast gene encoding a protein that preferentially associates with curved DNA. Yeast 10: 883-894
    • (1994) Yeast , vol.10 , pp. 883-894
    • Yamada, H.1    Mori, H.2    Momoi, H.3    Nakagawa, Y.4    Ueguchi, C.5    Mizuno, T.6
  • 51
    • 27744544281 scopus 로고    scopus 로고
    • The ErbB3 binding protein Ebp1 interacts with Sin3A to repress E2F1 and AR-mediated transcription
    • Zhang Y, Akinmade D, Hamburger AW (2005a) The ErbB3 binding protein Ebp1 interacts with Sin3A to repress E2F1 and AR-mediated transcription. Nucleic Acids Res 33: 6024-6033
    • (2005) Nucleic Acids Res , vol.33 , pp. 6024-6033
    • Zhang, Y.1    Akinmade, D.2    Hamburger, A.W.3
  • 52
    • 0037103989 scopus 로고    scopus 로고
    • Repression of androgen receptor mediated transcription by the ErbB-3 binding protein, Ebp1
    • Zhang Y, Fondell JD, Wang Q, Xia X, Cheng A, Lu ML, Hamburger AW (2002) Repression of androgen receptor mediated transcription by the ErbB-3 binding protein, Ebp1. Oncogene 21: 5609-5618
    • (2002) Oncogene , vol.21 , pp. 5609-5618
    • Zhang, Y.1    Fondell, J.D.2    Wang, Q.3    Xia, X.4    Cheng, A.5    Lu, M.L.6    Hamburger, A.W.7
  • 53
    • 2942703949 scopus 로고    scopus 로고
    • Heregulin regulates the ability of the ErbB3-binding protein Ebp1 to bind E2F promoter elements and repress E2F-mediated transcription
    • Zhang Y, Hamburger AW (2004) Heregulin regulates the ability of the ErbB3-binding protein Ebp1 to bind E2F promoter elements and repress E2F-mediated transcription. J Biol Chem 279: 26126-26133
    • (2004) J Biol Chem , vol.279 , pp. 26126-26133
    • Zhang, Y.1    Hamburger, A.W.2
  • 55
    • 0038813929 scopus 로고    scopus 로고
    • Repression of E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases
    • Zhang Y, Woodford N, Xia X, Hamburger AW (2003) Repression of E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases. Nucleic Acids Res 31: 2168-2177
    • (2003) Nucleic Acids Res , vol.31 , pp. 2168-2177
    • Zhang, Y.1    Woodford, N.2    Xia, X.3    Hamburger, A.W.4


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