메뉴 건너뛰기




Volumn 26, Issue 34, 2007, Pages 4941-4950

Structure of the C-terminal MA-3 domain of the tumour suppressor protein Pdcd4 and characterization of its interaction with eIF4A

Author keywords

eIF4A; HEAT; MA 3; NMR; Pdcd4; Translation

Indexed keywords

HELIX LOOP HELIX PROTEIN; INITIATION FACTOR 4A; PROGRAMMED CELL DEATH PROTEIN 4; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 34547410355     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/sj.onc.1210305     Document Type: Article
Times cited : (47)

References (43)
  • 1
    • 7944225548 scopus 로고    scopus 로고
    • Induction of PDCD4 tumor suppressor gene expression by RAR agonists, antiestrogen and HER-2/neu antagonist in breast cancer cells. Evidence for a role in apoptosis
    • Afonja O, Juste D, Das S, Matsuhashi S, Samuels H. (2004). Induction of PDCD4 tumor suppressor gene expression by RAR agonists, antiestrogen and HER-2/neu antagonist in breast cancer cells. Evidence for a role in apoptosis. Oncogene 23: 8135-8145.
    • (2004) Oncogene , vol.23 , pp. 8135-8145
    • Afonja, O.1    Juste, D.2    Das, S.3    Matsuhashi, S.4    Samuels, H.5
  • 2
    • 0029392854 scopus 로고
    • HEAT repeats in the Huntingtons-disease protein
    • Andrade M, Bork P. (1995). HEAT repeats in the Huntingtons-disease protein. Nat Genet 11: 115-116.
    • (1995) Nat Genet , vol.11 , pp. 115-116
    • Andrade, M.1    Bork, P.2
  • 3
    • 33646341222 scopus 로고    scopus 로고
    • Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1
    • Bellsolell L, Cho-Park PF, Poulin F, Sonenberg N, Burley SK. (2006). Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. Structure 14: 913-923.
    • (2006) Structure , vol.14 , pp. 913-923
    • Bellsolell, L.1    Cho-Park, P.F.2    Poulin, F.3    Sonenberg, N.4    Burley, S.K.5
  • 4
    • 6344231276 scopus 로고    scopus 로고
    • Transformation suppressor protein Pdcd4 interferes with JNK-mediated phosphorylation of c-Jun and recruitment of the coactivator p300 by c-Jun
    • Bitomsky N, Bohm M, Klempnauer K. (2004). Transformation suppressor protein Pdcd4 interferes with JNK-mediated phosphorylation of c-Jun and recruitment of the coactivator p300 by c-Jun. Oncogene 23: 7484-7493.
    • (2004) Oncogene , vol.23 , pp. 7484-7493
    • Bitomsky, N.1    Bohm, M.2    Klempnauer, K.3
  • 5
    • 18144432729 scopus 로고    scopus 로고
    • The transformation suppressor protein Pdcd4 shuttles between nucleus and cytoplasm and binds RNA
    • Bohm M, Sawicka K, Siebrasse J, Brehmer-Fastnacht A, Peters R, Klempnauer K. (2003). The transformation suppressor protein Pdcd4 shuttles between nucleus and cytoplasm and binds RNA. Oncogene 22: 4905-4910.
    • (2003) Oncogene , vol.22 , pp. 4905-4910
    • Bohm, M.1    Sawicka, K.2    Siebrasse, J.3    Brehmer-Fastnacht, A.4    Peters, R.5    Klempnauer, K.6
  • 6
    • 0042524204 scopus 로고    scopus 로고
    • Loss of PDCD4 expression in human lung cancer correlates with tumour progression and prognosis
    • Chen Y, Knosel T, Kristiansen G, Pietas A, Garber M, Matsuhashi S et al. (2003). Loss of PDCD4 expression in human lung cancer correlates with tumour progression and prognosis. J Pathol 200: 640-646.
    • (2003) J Pathol , vol.200 , pp. 640-646
    • Chen, Y.1    Knosel, T.2    Kristiansen, G.3    Pietas, A.4    Garber, M.5    Matsuhashi, S.6
  • 7
    • 0033598712 scopus 로고    scopus 로고
    • Differentially expressed protein Pdcd4 inhibits tumor promoter-induced neoplastic transformation
    • Cmarik J, Min H, Hegamyer G, Zhan S, Kulesz-Martin M, Yoshinaga H et al. (1999). Differentially expressed protein Pdcd4 inhibits tumor promoter-induced neoplastic transformation. Proc Natl Acad Sci USA 96: 14037-14042.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14037-14042
    • Cmarik, J.1    Min, H.2    Hegamyer, G.3    Zhan, S.4    Kulesz-Martin, M.5    Yoshinaga, H.6
  • 8
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G, Delaglio F, Bax A. (1999). Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13: 289-302.
    • (1999) J Biomol NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 11
    • 0033150672 scopus 로고    scopus 로고
    • Topological characteristics of helical repeat proteins
    • Groves MR, Barford D. (1999). Topological characteristics of helical repeat proteins. Curr Opin Struct Biol 9: 383-389.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 383-389
    • Groves, M.R.1    Barford, D.2
  • 12
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P, Mumenthaler C, Wuthrich K. (1997). Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 273: 283-298.
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 13
    • 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. (2002). Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319: 209-227.
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 15
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. (1993). Protein structure comparison by alignment of distance matrices. J Mol Biol 233: 123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 16
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A
    • Imataka H, Sonenberg N. (1997). Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol Cell Biol 17: 6940-6947.
    • (1997) Mol Cell Biol , vol.17 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 17
    • 4444285717 scopus 로고    scopus 로고
    • Characterization of programmed cell death 4 in multiple human cancers reveals a novel enhancer of drug sensitivity
    • Jansen A, Camalier C, Stark C, Colburn N. (2004). Characterization of programmed cell death 4 in multiple human cancers reveals a novel enhancer of drug sensitivity. Mol Cancer Ther 3: 103-110.
    • (2004) Mol Cancer Ther , vol.3 , pp. 103-110
    • Jansen, A.1    Camalier, C.2    Stark, C.3    Colburn, N.4
  • 18
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14: 51-55.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 20
    • 0035105502 scopus 로고    scopus 로고
    • A conserved HEAT domain within elF4G directs assembly of the translation initiation machinery
    • Marcotrigiano J, Lomakin I, Sonenberg N, Pestova T, Hellen C, Burley S. (2001). A conserved HEAT domain within elF4G directs assembly of the translation initiation machinery. Mol Cell 7: 193-203.
    • (2001) Mol Cell , vol.7 , pp. 193-203
    • Marcotrigiano, J.1    Lomakin, I.2    Sonenberg, N.3    Pestova, T.4    Hellen, C.5    Burley, S.6
  • 21
    • 25644436944 scopus 로고    scopus 로고
    • Translation initiation: Structures, mechanisms and evolution
    • Marintchev A, Wagner G. (2004). Translation initiation: structures, mechanisms and evolution. Q Rev Biophys 37: 197-284.
    • (2004) Q Rev Biophys , vol.37 , pp. 197-284
    • Marintchev, A.1    Wagner, G.2
  • 22
    • 0034852936 scopus 로고    scopus 로고
    • Crystal structure of the human nuclear cap binding complex
    • Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. (2001). Crystal structure of the human nuclear cap binding complex. Mol Cell 8: 383-396.
    • (2001) Mol Cell , vol.8 , pp. 383-396
    • Mazza, C.1    Ohno, M.2    Segref, A.3    Mattaj, I.W.4    Cusack, S.5
  • 23
    • 0032555593 scopus 로고    scopus 로고
    • High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3
    • Muskett F, Frenkiel T, Feeney J, Freedman R, Carr M, Williamson R. (1998). High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3. J Biol Chem 273: 21736-21743.
    • (1998) J Biol Chem , vol.273 , pp. 21736-21743
    • Muskett, F.1    Frenkiel, T.2    Feeney, J.3    Freedman, R.4    Carr, M.5    Williamson, R.6
  • 24
    • 24944469031 scopus 로고    scopus 로고
    • Structural basis for the enhancement of eIF4A helicase activity by eIF4G
    • Oberer M, Marintchev A, Wagner G. (2005). Structural basis for the enhancement of eIF4A helicase activity by eIF4G. Genes Dev 19: 2212-2223.
    • (2005) Genes Dev , vol.19 , pp. 2212-2223
    • Oberer, M.1    Marintchev, A.2    Wagner, G.3
  • 26
    • 0027494565 scopus 로고
    • The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor-4A is required for RNA-binding and ATP hydrolysis
    • Pause A, Methot N, Sonenberg N. (1993). The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor-4A is required for RNA-binding and ATP hydrolysis. Mol Cell Biol 13: 6789-6798.
    • (1993) Mol Cell Biol , vol.13 , pp. 6789-6798
    • Pause, A.1    Methot, N.2    Sonenberg, N.3
  • 27
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase- The mammalian translation initiation-factor eIF-4A
    • Pause A, Sonenberg N. (1992). Mutational analysis of a DEAD box RNA helicase- The mammalian translation initiation-factor eIF-4A. EMBO J 11: 2643-2654.
    • (1992) EMBO J , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 28
    • 0034284394 scopus 로고    scopus 로고
    • Novel eIF4G domain homologues linking mRNA translation with nonsense-mediated mRNA decay
    • Ponting CP. (2000). Novel eIF4G domain homologues linking mRNA translation with nonsense-mediated mRNA decay. Trends Biochem Sci 25: 423-426.
    • (2000) Trends Biochem Sci , vol.25 , pp. 423-426
    • Ponting, C.P.1
  • 29
    • 23044505589 scopus 로고    scopus 로고
    • Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6
    • Renshaw P, Lightbody K, Veverka V, Muskett F, Kelly G, Frenkiel T et al. (2005). Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6. EMBO J 24: 2491-2498.
    • (2005) EMBO J , vol.24 , pp. 2491-2498
    • Renshaw, P.1    Lightbody, K.2    Veverka, V.3    Muskett, F.4    Kelly, G.5    Frenkiel, T.6
  • 30
    • 0037077299 scopus 로고    scopus 로고
    • Conclusive evidence that the major T-cell antigens of the Mycobacterium tuberculosis complex ESAT-6 and CFP-10 form a tight, 1:1 complex and characterization of the structural properties of ESAT-6, CFP-10, and the ESAT-6.CFP-10 complex. Implications for pathogenesis and virulence
    • Renshaw PS, Panagiotidou P, Whelan A, Gordon SV, Hewinson RG, Williamson RA et al. (2002). Conclusive evidence that the major T-cell antigens of the Mycobacterium tuberculosis complex ESAT-6 and CFP-10 form a tight, 1:1 complex and characterization of the structural properties of ESAT-6, CFP-10, and the ESAT-6.CFP-10 complex. Implications for pathogenesis and virulence. J Biol Chem 277: 21598-21603.
    • (2002) J Biol Chem , vol.277 , pp. 21598-21603
    • Renshaw, P.S.1    Panagiotidou, P.2    Whelan, A.3    Gordon, S.V.4    Hewinson, R.G.5    Williamson, R.A.6
  • 31
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eukaryotic translation initiation factor-4A and factor-4F
    • Rozen F, Edery I, Meerovitch K, Dever T, Merrick W, Sonenberg N. (1990). Bidirectional RNA helicase activity of eukaryotic translation initiation factor-4A and factor-4F. Mol Cell Biol 10: 1134-1144.
    • (1990) Mol Cell Biol , vol.10 , pp. 1134-1144
    • Rozen, F.1    Edery, I.2    Meerovitch, K.3    Dever, T.4    Merrick, W.5    Sonenberg, N.6
  • 32
    • 0029595270 scopus 로고
    • Isolation of a novel mouse gene MA-3 that is induced upon programmed cell death
    • Shibahara K, Asano M, Ishida Y, Aoki T, Koike T, Honjo T. (1995). Isolation of a novel mouse gene MA-3 that is induced upon programmed cell death. GENE 166: 297-301.
    • (1995) GENE , vol.166 , pp. 297-301
    • Shibahara, K.1    Asano, M.2    Ishida, Y.3    Aoki, T.4    Koike, T.5    Honjo, T.6
  • 33
    • 0035032444 scopus 로고    scopus 로고
    • The requirement for eukaryotic initiation factor 4A (eIF4A) in translation is in direct proportion to the degree of mRNA 5′ secondary structure
    • Svitkin Y, Pause A, Haghighat A, Pyronnet S, Witherell G, Belsham G et al. (2001). The requirement for eukaryotic initiation factor 4A (eIF4A) in translation is in direct proportion to the degree of mRNA 5′ secondary structure. RNA 7: 382-394.
    • (2001) RNA , vol.7 , pp. 382-394
    • Svitkin, Y.1    Pause, A.2    Haghighat, A.3    Pyronnet, S.4    Witherell, G.5    Belsham, G.6
  • 34
    • 0037252143 scopus 로고    scopus 로고
    • The Q motif: A newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis
    • Tanner N, Cordin O, Banroques J, Doere M, Linder P. (2003). The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis. Mol Cell 11: 127-138.
    • (2003) Mol Cell , vol.11 , pp. 127-138
    • Tanner, N.1    Cordin, O.2    Banroques, J.3    Doere, M.4    Linder, P.5
  • 35
    • 33744960022 scopus 로고    scopus 로고
    • Structural diversity in p160/CREB-binding protein coactivator complexes
    • Waters L, Yue B, Veverka V, Renshaw P, Bramham J, Matsuda S et al. (2006a). Structural diversity in p160/CREB-binding protein coactivator complexes. J Biol Chem 281: 14787-14795.
    • (2006) J Biol Chem , vol.281 , pp. 14787-14795
    • Waters, L.1    Yue, B.2    Veverka, V.3    Renshaw, P.4    Bramham, J.5    Matsuda, S.6
  • 36
    • 34250314906 scopus 로고    scopus 로고
    • NMR assignment and secondary structure determination of the C-terminal MA-3 domain of the tumour suppressor protein Pdcd4
    • Waters LC, Bohm M, Veverka V, Muskett FW, Frenkiel TA, Kelly GP et al. (2006b). NMR assignment and secondary structure determination of the C-terminal MA-3 domain of the tumour suppressor protein Pdcd4. J Biomol NMR 36: S5:18.
    • (2006) J Biomol NMR , vol.36 , Issue.S5 , pp. 18
    • Waters, L.C.1    Bohm, M.2    Veverka, V.3    Muskett, F.W.4    Frenkiel, T.A.5    Kelly, G.P.6
  • 37
    • 0030666085 scopus 로고    scopus 로고
    • Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation
    • Williamson R, Carr M, Frenkiel T, Feeney J, Freedman R. (1997). Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation. Biochemistry 36: 13882-13889.
    • (1997) Biochemistry , vol.36 , pp. 13882-13889
    • Williamson, R.1    Carr, M.2    Frenkiel, T.3    Feeney, J.4    Freedman, R.5
  • 38
    • 28044445673 scopus 로고    scopus 로고
    • The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G
    • Yamamoto Y, Singh CR, Marintchev A, Hall NS, Hannig EM, Wagner G et al. (2005). The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G. Proc Natl Acad Sci USA 102: 16164-16169.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16164-16169
    • Yamamoto, Y.1    Singh, C.R.2    Marintchev, A.3    Hall, N.S.4    Hannig, E.M.5    Wagner, G.6
  • 39
    • 1942453838 scopus 로고    scopus 로고
    • A novel function of the MA-3 domains in transformation and translation suppressor Pdcd4 is essential for its binding to eukaryotic translation initiation factor 4A
    • Yang H, Cho M, Zakowicz H, Hegamyer G, Sonenberg N, Colburn N. (2004). A novel function of the MA-3 domains in transformation and translation suppressor Pdcd4 is essential for its binding to eukaryotic translation initiation factor 4A. Mol Cell Biol 24: 3894-3906.
    • (2004) Mol Cell Biol , vol.24 , pp. 3894-3906
    • Yang, H.1    Cho, M.2    Zakowicz, H.3    Hegamyer, G.4    Sonenberg, N.5    Colburn, N.6
  • 40
    • 0037216626 scopus 로고    scopus 로고
    • The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation
    • Yang H, Jansen A, Komar A, Zheng X, Merrick W, Costes S et al. (2003a). The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation. Mol Cell Biol 23: 26-37.
    • (2003) Mol Cell Biol , vol.23 , pp. 26-37
    • Yang, H.1    Jansen, A.2    Komar, A.3    Zheng, X.4    Merrick, W.5    Costes, S.6
  • 41
    • 0035825611 scopus 로고    scopus 로고
    • A novel transformation suppressor, Pdcd4, inhibits AP-1 transactivation but not NF-kappa B or ODC transactivation
    • Yang H, Jansen A, Nair R, Shibahara K, Verma A, Cmarik J et al. (2001). A novel transformation suppressor, Pdcd4, inhibits AP-1 transactivation but not NF-kappa B or ODC transactivation. Oncogene 20: 669-676.
    • (2001) Oncogene , vol.20 , pp. 669-676
    • Yang, H.1    Jansen, A.2    Nair, R.3    Shibahara, K.4    Verma, A.5    Cmarik, J.6
  • 42
    • 0038209450 scopus 로고    scopus 로고
    • Pdcd4 suppresses tumor phenotype in JB6 cells by inhibiting AP-1 transactivation
    • Yang H, Knies J, Stark C, Colburn N. (2003b). Pdcd4 suppresses tumor phenotype in JB6 cells by inhibiting AP-1 transactivation. Oncogene 22: 3712-3720.
    • (2003) Oncogene , vol.22 , pp. 3712-3720
    • Yang, H.1    Knies, J.2    Stark, C.3    Colburn, N.4
  • 43
    • 13944274057 scopus 로고    scopus 로고
    • Mutational analysis of the DEAD-box RNA helicase eIF4AII characterizes its interaction with transformation suppressor Pdcd4 and eIF4GI
    • Zakowicz H, Yang H, Stark C, Wlodawer A, Laronde-Leblanc N, Colburn N. (2005). Mutational analysis of the DEAD-box RNA helicase eIF4AII characterizes its interaction with transformation suppressor Pdcd4 and eIF4GI. RNA 11: 261-274.
    • (2005) RNA , vol.11 , pp. 261-274
    • Zakowicz, H.1    Yang, H.2    Stark, C.3    Wlodawer, A.4    Laronde-Leblanc, N.5    Colburn, N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.