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Volumn 108, Issue 49, 2011, Pages 19635-19640

Dual role of methionyl-tRNA synthetase in the regulation of translation and tumor suppressor activity of aminoacyl-tRNA synthetase-interacting multifunctional protein-3

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYLTRANSFER RNA SYNTHETASE INTERACTING MULTIFUNCTIONAL PROTEIN 3; INITIATION FACTOR 2ALPHA; METHIONINE TRANSFER RNA LIGASE; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 83755207354     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1103922108     Document Type: Article
Times cited : (97)

References (31)
  • 1
    • 5044229348 scopus 로고    scopus 로고
    • Molecular mechanisms of translational control
    • DOI 10.1038/nrm1488
    • Gebauer F, HentzeMW(2004) Molecular mechanisms of translational control. Nat Rev Mol Cell Biol 5:827-835. (Pubitemid 39336276)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.10 , pp. 827-835
    • Gebauer, F.1    Hentze, M.W.2
  • 2
    • 75149181741 scopus 로고    scopus 로고
    • TRNA over-expression in breast cancer and functional consequences
    • Pavon-Eternod M, et al. (2009) tRNA over-expression in breast cancer and functional consequences. Nucleic Acids Res 37:7268-7280.
    • (2009) Nucleic Acids Res , vol.37 , pp. 7268-7280
    • Pavon-Eternod, M.1
  • 3
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG (2009) Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136:731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 4
    • 4444369924 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase complexes: Beyond translation
    • DOI 10.1242/jcs.01342
    • Lee SW, Cho BH, Park SG, Kim S (2004) Aminoacyl-tRNA synthetase complexes: Beyond translation. J Cell Sci 117:3725-3734. (Pubitemid 39207312)
    • (2004) Journal of Cell Science , vol.117 , Issue.17 , pp. 3725-3734
    • Lee, S.W.1    Cho, B.H.2    Park, S.G.3    Kim, S.4
  • 5
    • 25144489447 scopus 로고    scopus 로고
    • Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: New perspectives on housekeepers
    • DOI 10.1016/j.tibs.2005.08.004, PII S0968000405002392
    • Park SG, Ewalt KL, Kim S (2005) Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers. Trends Biochem Sci 30:569-574. (Pubitemid 41356495)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.10 , pp. 569-574
    • Sang, G.P.1    Ewalt, K.L.2    Kim, S.3
  • 6
    • 0034192459 scopus 로고    scopus 로고
    • Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis
    • DOI 10.1083/jcb.149.3.567
    • Ko YG, Kang YS, Kim EK, Park SG, Kim S (2000) Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis. J Cell Biol 149:567-574. (Pubitemid 30252391)
    • (2000) Journal of Cell Biology , vol.149 , Issue.3 , pp. 567-574
    • Ko, Y.-G.1    Kang, Y.-S.2    Kim, E.-K.3    Park, S.G.4    Kim, S.5
  • 7
    • 70849104780 scopus 로고    scopus 로고
    • Innate immune and chemically triggered oxidative stress modifies translational fidelity
    • Netzer N, et al. (2009) Innate immune and chemically triggered oxidative stress modifies translational fidelity. Nature 462:522-526.
    • (2009) Nature , vol.462 , pp. 522-526
    • Netzer, N.1
  • 8
    • 41349089950 scopus 로고    scopus 로고
    • Met Synthesis Can Drive Cell Proliferation and Oncogenic Transformation
    • DOI 10.1016/j.cell.2008.02.035, PII S0092867408002869
    • Marshall L, Kenneth NS, White RJ (2008) Elevated tRNA(iMet) synthesis can drive cell proliferation and oncogenic transformation. Cell 133:78-89. (Pubitemid 351447300)
    • (2008) Cell , vol.133 , Issue.1 , pp. 78-89
    • Marshall, L.1    Kenneth, N.S.2    White, R.J.3
  • 9
    • 77951139250 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs): A triad for cellular homeostasis
    • Park SG, Choi EC, Kim S (2010) Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs): A triad for cellular homeostasis. IUBMB Life 62:296-302.
    • (2010) IUBMB Life , vol.62 , pp. 296-302
    • Park, S.G.1    Choi, E.C.2    Kim, S.3
  • 10
    • 33846016966 scopus 로고    scopus 로고
    • Hierarchical network between the components of the multi-tRNA synthetase complex: Implications for complex formation
    • Han JM, et al. (2006) Hierarchical network between the components of the multi-tRNA synthetase complex: Implications for complex formation. J Biol Chem 281:38663-38667.
    • (2006) J Biol Chem , vol.281 , pp. 38663-38667
    • Han, J.M.1
  • 11
    • 19944431746 scopus 로고    scopus 로고
    • The haploinsufficient tumor suppressor p18 upregulates p53 via interactions with ATM/ATR
    • Park BJ, et al. (2005) The haploinsufficient tumor suppressor p18 upregulates p53 via interactions with ATM/ATR. Cell 120:209-221.
    • (2005) Cell , vol.120 , pp. 209-221
    • Park, B.J.1
  • 13
    • 46649105125 scopus 로고    scopus 로고
    • Determination of three-dimensional structure and residues of the novel tumor suppressor AIMP3/p18 required for the interaction with ATM
    • Kim KJ, et al. (2008) Determination of three-dimensional structure and residues of the novel tumor suppressor AIMP3/p18 required for the interaction with ATM. J Biol Chem 283:14032-14040.
    • (2008) J Biol Chem , vol.283 , pp. 14032-14040
    • Kim, K.J.1
  • 14
    • 33746872495 scopus 로고    scopus 로고
    • AIMP3 haploinsufficiency disrupts oncogene-induced p53 activation and genomic stability
    • Park BJ, et al. (2006) AIMP3 haploinsufficiency disrupts oncogene-induced p53 activation and genomic stability. Cancer Res 66:6913-6918.
    • (2006) Cancer Res , vol.66 , pp. 6913-6918
    • Park, B.J.1
  • 15
    • 0034671820 scopus 로고    scopus 로고
    • A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation
    • DOI 10.1093/emboj/19.24.6908
    • Kaminska M, Deniziak M, Kerjan P, Barciszewski J, Mirande M (2000) A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation. EMBO J 19:6908-6917. (Pubitemid 32011684)
    • (2000) EMBO Journal , vol.19 , Issue.24 , pp. 6908-6917
    • Kaminska, M.1    Deniziak, M.2    Kerjan, P.3    Barciszewski, J.4    Mirande, M.5
  • 16
    • 77956095201 scopus 로고    scopus 로고
    • New functions of aminoacyl-tRNA synthetases beyond translation
    • Guo M, Yang XL, Schimmel P (2010) New functions of aminoacyl-tRNA synthetases beyond translation. Nat Rev Mol Cell Biol 11:668-674.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 668-674
    • Guo, M.1    Yang, X.L.2    Schimmel, P.3
  • 18
    • 54049146934 scopus 로고    scopus 로고
    • Visualization of ternary complexes in living cells by using a BiFC-based FRET assay
    • Shyu YJ, Suarez CD, Hu C-D (2008) Visualization of ternary complexes in living cells by using a BiFC-based FRET assay. Nat Protoc 3:1693-1702.
    • (2008) Nat Protoc , vol.3 , pp. 1693-1702
    • Shyu, Y.J.1    Suarez, C.D.2    Hu, C.-D.3
  • 20
    • 0001598487 scopus 로고    scopus 로고
    • Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase
    • DOI 10.1046/j.1432-1327.1999.00780.x
    • Berlanga JJ, Santoyo J, De Haro C (1999) Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase. Eur J Biochem 265:754-762. (Pubitemid 29489008)
    • (1999) European Journal of Biochemistry , vol.265 , Issue.2 , pp. 754-762
    • Berlanga, J.J.1    Santoyo, J.2    De Haro, C.3
  • 21
    • 0033635215 scopus 로고    scopus 로고
    • Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain
    • Dong J, Qiu H, Garcia-Barrio M, Anderson J, Hinnebusch AG (2000) Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain. Mol Cell 6:269-279.
    • (2000) Mol Cell , vol.6 , pp. 269-279
    • Dong, J.1    Qiu, H.2    Garcia-Barrio, M.3    Anderson, J.4    Hinnebusch, A.G.5
  • 22
    • 0029006391 scopus 로고
    • The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids
    • Wek SA, Zhu S, Wek RC (1995) The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Mol Cell Biol 15:4497-4506.
    • (1995) Mol Cell Biol , vol.15 , pp. 4497-4506
    • Wek, S.A.1    Zhu, S.2    Wek, R.C.3
  • 23
    • 12844259491 scopus 로고    scopus 로고
    • GCN2 phosphorylation of eIF2alpha activates NF-kappaB in response to UV irradiation
    • Jiang HY, Wek RC (2005) GCN2 phosphorylation of eIF2alpha activates NF-kappaB in response to UV irradiation. Biochem J 385:371-380.
    • (2005) Biochem J , vol.385 , pp. 371-380
    • Jiang, H.Y.1    Wek, R.C.2
  • 24
    • 58149302677 scopus 로고    scopus 로고
    • Two non-redundant fragments in the N-terminal peptide of human cytosolic methionyl-tRNA synthetase were indispensable for the multisynthetase complex incorporation and enzyme activity
    • He R, Zu LD, Yao P, Chen X, Wang ED (2009) Two non-redundant fragments in the N-terminal peptide of human cytosolic methionyl-tRNA synthetase were indispensable for the multisynthetase complex incorporation and enzyme activity. Biochim Biophys Acta 1794:347-354.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 347-354
    • He, R.1    Zu, L.D.2    Yao, P.3    Chen, X.4    Wang, E.D.5
  • 26
    • 35648944297 scopus 로고    scopus 로고
    • A study of communication pathways in methionyl-tRNA synthetase by molecular dynamics simulations and structure network analysis
    • DOI 10.1073/pnas.0704459104
    • Ghosh A, Vishveshwara S (2007) A study of communication pathways in methionyl-tRNA synthetase by molecular dynamics simulations and structure network analysis. Proc Natl Acad Sci USA 104:15711-15716. (Pubitemid 350035365)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.40 , pp. 15711-15716
    • Ghosh, A.1    Vishveshwara, S.2
  • 27
    • 78349290448 scopus 로고    scopus 로고
    • Downregulation of lamin A by tumor suppressor AIMP3/p18 leads to a progeroid phenotype in mice
    • Oh YS, et al. (2010) Downregulation of lamin A by tumor suppressor AIMP3/p18 leads to a progeroid phenotype in mice. Aging Cell 9:810-822.
    • (2010) Aging Cell , vol.9 , pp. 810-822
    • Oh, Y.S.1
  • 28
    • 67651095905 scopus 로고    scopus 로고
    • Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity
    • Arif A, et al. (2009) Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity. Mol Cell 35:164-180.
    • (2009) Mol Cell , vol.35 , pp. 164-180
    • Arif, A.1
  • 29
    • 1342287127 scopus 로고    scopus 로고
    • The Function of Lysyl-tRNA Synthetase and Ap4A as Signaling Regulators of MITF Activity in FcepsilonRI-Activated Mast Cells
    • DOI 10.1016/S1074-7613(04)00020-2
    • Lee YN, Nechushtan H, Figov N, Razin E (2004) The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells. Immunity 20:145-151. (Pubitemid 38258391)
    • (2004) Immunity , vol.20 , Issue.2 , pp. 145-151
    • Lee, Y.-N.1    Nechushtan, H.2    Figov, N.3    Razin, E.4
  • 30
    • 49649116700 scopus 로고    scopus 로고
    • AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53
    • Han JM, et al. (2008) AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53. Proc Natl Acad Sci USA 105:11206-11211.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11206-11211
    • Han, J.M.1
  • 31
    • 37249004668 scopus 로고    scopus 로고
    • The Gcn2 kinase as a cell cycle regulator
    • Grallert B, Boye E (2007) The Gcn2 kinase as a cell cycle regulator. Cell Cycle 6:2768-2772. (Pubitemid 350277168)
    • (2007) Cell Cycle , vol.6 , Issue.22 , pp. 2768-2772
    • Grallert, B.1    Boye, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.