메뉴 건너뛰기




Volumn 24, Issue 10, 2005, Pages 1852-1862

Antiapoptotic function of RNA-binding protein HuR effected through prothymosin α

Author keywords

ELAV; Post transcriptional gene expression; ProT ; Stress response; Translational regulation

Indexed keywords

APOPTOSOME; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HUR PROTEIN; MESSENGER RNA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTHYMOSIN ALPHA; RNA BINDING PROTEIN;

EID: 20044366611     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600661     Document Type: Article
Times cited : (147)

References (69)
  • 2
    • 0033557936 scopus 로고    scopus 로고
    • ELAV tumor antigen, Hel-N1, increases translation of neurofilament M mRNA and induces formation of neurites in human teratocarcinoma cells
    • Antic D, Lu N, Keene JD (1999) ELAV tumor antigen, Hel-N1, increases translation of neurofilament M mRNA and induces formation of neurites in human teratocarcinoma cells. Genes Dev 13: 449-461
    • (1999) Genes Dev , vol.13 , pp. 449-461
    • Antic, D.1    Lu, N.2    Keene, J.D.3
  • 3
    • 16844362149 scopus 로고    scopus 로고
    • Post-transcriptional regulation in cancer
    • Audic Y, Hartley RS (2004) Post-transcriptional regulation in cancer. Biol Cell 96: 479-498
    • (2004) Biol Cell , vol.96 , pp. 479-498
    • Audic, Y.1    Hartley, R.S.2
  • 4
    • 0038185346 scopus 로고    scopus 로고
    • Post-transcriptional regulation of gene expression by degradation of messenger RNAs
    • Bevilacqua A, Ceriani MC, Capaccioli S, Nicolin A (2003) Post-transcriptional regulation of gene expression by degradation of messenger RNAs. J Cell Physiol 195: 356-372
    • (2003) J Cell Physiol , vol.195 , pp. 356-372
    • Bevilacqua, A.1    Ceriani, M.C.2    Capaccioli, S.3    Nicolin, A.4
  • 5
    • 0033933196 scopus 로고    scopus 로고
    • Differential expression and localization of the mRNA binding proteins, AU-rich element mRNA binding protein (AUF1) and Hu antigen R (HuR), in neoplastic lung tissue
    • Blaxall BC, Dwyer-Nield LD, Bauer AK, Bohlmeyer TJ, Malkinson AM, Port JD (2000) Differential expression and localization of the mRNA binding proteins, AU-rich element mRNA binding protein (AUF1) and Hu antigen R (HuR), in neoplastic lung tissue. Mol Carcinog 28: 76-83
    • (2000) Mol Carcinog , vol.28 , pp. 76-83
    • Blaxall, B.C.1    Dwyer-Nield, L.D.2    Bauer, A.K.3    Bohlmeyer, T.J.4    Malkinson, A.M.5    Port, J.D.6
  • 9
    • 0025361155 scopus 로고
    • Detection of the anti-Hu antibody in the serum of patients with small cell lung cancer - A quantitative western blot analysis
    • Dalmau J, Furneaux HM, Gralla RJ, Kris MG, Posner JB (1990) Detection of the anti-Hu antibody in the serum of patients with small cell lung cancer-a quantitative western blot analysis. Ann Neurol 27: 544-552
    • (1990) Ann Neurol , vol.27 , pp. 544-552
    • Dalmau, J.1    Furneaux, H.M.2    Gralla, R.J.3    Kris, M.G.4    Posner, J.B.5
  • 11
    • 0027312521 scopus 로고
    • Differentiation-linked expression of prothymosin ot gene in human myeloid leukemic cells
    • Dosil M, Alvarez-Fernandez L, Gomez-Marquez J (1993) Differentiation- linked expression of prothymosin ot gene in human myeloid leukemic cells. Exp Cell Res 204: 94-101
    • (1993) Exp Cell Res , vol.204 , pp. 94-101
    • Dosil, M.1    Alvarez-Fernandez, L.2    Gomez-Marquez, J.3
  • 12
    • 4143141823 scopus 로고    scopus 로고
    • The immunobiology of cancer immunosurveillance and immunoediting
    • Dunn GP, Old LJ, Schreiber RD (2004) The immunobiology of cancer immunosurveillance and immunoediting. Immunity 21: 137-148
    • (2004) Immunity , vol.21 , pp. 137-148
    • Dunn, G.P.1    Old, L.J.2    Schreiber, R.D.3
  • 13
    • 0026099022 scopus 로고
    • The MYC protein activates transcription of the α-prothymosin gene
    • Eilers M, Schirm S, Bishop JM (1991) The MYC protein activates transcription of the α-prothymosin gene. EMBO J 10: 133-141
    • (1991) EMBO J , vol.10 , pp. 133-141
    • Eilers, M.1    Schirm, S.2    Bishop, J.M.3
  • 14
    • 0033964721 scopus 로고    scopus 로고
    • Functional discontinuities in prothymosin a caused by caspase cleavage in apoptotic cells
    • Enkemann SA, Wang RH, Trumbore MW, Berger SL (2000) Functional discontinuities in prothymosin a caused by caspase cleavage in apoptotic cells. J Cell Physiol 182: 256-268
    • (2000) J Cell Physiol , vol.182 , pp. 256-268
    • Enkemann, S.A.1    Wang, R.H.2    Trumbore, M.W.3    Berger, S.L.4
  • 16
    • 0346366983 scopus 로고    scopus 로고
    • Hyaluronic acid or TNF-α plus fibronectin triggers granulocyte macrophage-colony-stimulating factor mRNA stabilization in eosinophils yet engages differential intracellular pathways and mRNA binding proteins
    • Esnault S, Malter JS (2003) Hyaluronic acid or TNF-α plus fibronectin triggers granulocyte macrophage-colony-stimulating factor mRNA stabilization in eosinophils yet engages differential intracellular pathways and mRNA binding proteins. J Immunol 171: 6780-6787
    • (2003) J Immunol , vol.171 , pp. 6780-6787
    • Esnault, S.1    Malter, J.S.2
  • 20
    • 0035976612 scopus 로고    scopus 로고
    • Delineation of mRNA export pathways by the use of cell-permeable peptides
    • Gallouzi IE, Steitz JA (2001) Delineation of mRNA export pathways by the use of cell-permeable peptides. Science 294: 1895-1901
    • (2001) Science , vol.294 , pp. 1895-1901
    • Gallouzi, I.E.1    Steitz, J.A.2
  • 21
    • 2342573011 scopus 로고    scopus 로고
    • HuR in the mammalian genotoxic response: Post-transcriptional multitasking
    • Gorospe M (2003) HuR in the mammalian genotoxic response: post-transcriptional multitasking. Cell Cycle 2: 412-414
    • (2003) Cell Cycle , vol.2 , pp. 412-414
    • Gorospe, M.1
  • 22
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA (2000) The hallmarks of cancer. Cell 100: 57-70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 23
    • 0041305878 scopus 로고    scopus 로고
    • The thymosins Prothymosin α, parathymosin, and β-thymosins: Structure and function
    • Hannappel E, Huff T (2003) The thymosins Prothymosin α, parathymosin, and β-thymosins: structure and function. Vitam Horm 66: 257-296
    • (2003) Vitam Horm , vol.66 , pp. 257-296
    • Hannappel, E.1    Huff, T.2
  • 24
    • 0031038858 scopus 로고    scopus 로고
    • Ectopic expression of Hel-N1, an RNA-binding protein, increases glucose transporter (GLUT1) expression in 3T3-L1 adipocytes
    • Jain RG, Andrews LG, McGowan KM, Pekala PH, Keene JD (1997) Ectopic expression of Hel-N1, an RNA-binding protein, increases glucose transporter (GLUT1) expression in 3T3-L1 adipocytes. Mol Cell Biol 17: 954-962
    • (1997) Mol Cell Biol , vol.17 , pp. 954-962
    • Jain, R.G.1    Andrews, L.G.2    McGowan, K.M.3    Pekala, P.H.4    Keene, J.D.5
  • 27
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • Kaufman RJ (2002) Orchestrating the unfolded protein response in health and disease. J Clin Invest 110: 1389-1398
    • (2002) J Clin Invest , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 28
    • 0035575679 scopus 로고    scopus 로고
    • Programmed cell death: Alive and well in the new millennium Trends
    • Kaufmann SH, Hengartner MO (2001) Programmed cell death: alive and well in the new millennium Trends. Cell Biol 11: 526-534
    • (2001) Cell Biol , vol.11 , pp. 526-534
    • Kaufmann, S.H.1    Hengartner, M.O.2
  • 29
    • 3242699557 scopus 로고    scopus 로고
    • Global mRNA stabilization preferentially linked to translational repression during the endoplasmic reticulum stress response
    • Kawai T, Fan J, Mazan-Mamczarz K, Gorospe M (2004) Global mRNA stabilization preferentially linked to translational repression during the endoplasmic reticulum stress response. Mol Cell Biol 24: 6773-6787
    • (2004) Mol Cell Biol , vol.24 , pp. 6773-6787
    • Kawai, T.1    Fan, J.2    Mazan-Mamczarz, K.3    Gorospe, M.4
  • 30
    • 0036863320 scopus 로고    scopus 로고
    • Stress granules: Sites of mRNA triage that regulate mRNA stability and translatability
    • Kedersha N, Anderson P (2002) Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem Soc Trans 30: 963-969
    • (2002) Biochem Soc Trans , vol.30 , pp. 963-969
    • Kedersha, N.1    Anderson, P.2
  • 31
    • 0033524475 scopus 로고    scopus 로고
    • Why is Hu where? Shuttling of early-response-gene messenger RNA subsets
    • Keene JD (1999) Why is Hu where? Shuttling of early-response-gene messenger RNA subsets. Proc Natl Acad Sci USA 96: 5-7
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5-7
    • Keene, J.D.1
  • 32
    • 0035912793 scopus 로고    scopus 로고
    • Ribonucleoprotein infrastructure regulating the flow of genetic information between the genome and the proteome
    • Keene JD (2001) Ribonucleoprotein infrastructure regulating the flow of genetic information between the genome and the proteome. Proc Natl Acad Sci USA 98: 7018-7024
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7018-7024
    • Keene, J.D.1
  • 33
    • 0036894711 scopus 로고    scopus 로고
    • ELAV/Hu proteins inhibit p27 translation via an IRES element in the p27 5'UTR
    • Kullmann M, Gopfert U, Siewe B, Hengst L (2002) ELAV/Hu proteins inhibit p27 translation via an IRES element in the p27 5'UTR. Genes Dev 16: 3087-3099
    • (2002) Genes Dev , vol.16 , pp. 3087-3099
    • Kullmann, M.1    Gopfert, U.2    Siewe, B.3    Hengst, L.4
  • 34
    • 4143122397 scopus 로고    scopus 로고
    • Concurrent versus individual binding of HuR and AUF1 to common labile target mRNAs
    • Lal A, Mazan-Mamczarz K, Kawai T, Yang X, Martindale JL, Gorospe M (2004) Concurrent versus individual binding of HuR and AUF1 to common labile target mRNAs. EMBO J 23: 3092-3102
    • (2004) EMBO J , vol.23 , pp. 3092-3102
    • Lal, A.1    Mazan-Mamczarz, K.2    Kawai, T.3    Yang, X.4    Martindale, J.L.5    Gorospe, M.6
  • 37
    • 0032513043 scopus 로고    scopus 로고
    • Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR
    • Levy NS, Chung S, Furneaux H, Levy AP (1998) Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR. J Biol Chem 273: 6417-6423
    • (1998) J Biol Chem , vol.273 , pp. 6417-6423
    • Levy, N.S.1    Chung, S.2    Furneaux, H.3    Levy, A.P.4
  • 38
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X (1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91: 479-489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 41
    • 0029873536 scopus 로고    scopus 로고
    • Cloning and characterization of HuR, a ubiquitously expressed Elav-like protein
    • Ma WJ, Cheng S, Campbell C, Wright A, Furneaux H (1996) Cloning and characterization of HuR, a ubiquitously expressed Elav-like protein. J Biol Chem 271: 8144-8151
    • (1996) J Biol Chem , vol.271 , pp. 8144-8151
    • Ma, W.J.1    Cheng, S.2    Campbell, C.3    Wright, A.4    Furneaux, H.5
  • 42
    • 0031060705 scopus 로고    scopus 로고
    • Localization of the human HuR gene to chromosome 19p13.2
    • Ma WJ, Furneaux H (1997) Localization of the human HuR gene to chromosome 19p13.2. Hum Genet 99: 32-33
    • (1997) Hum Genet , vol.99 , pp. 32-33
    • Ma, W.J.1    Furneaux, H.2
  • 43
    • 0345803539 scopus 로고    scopus 로고
    • Tumour prothymosin α content, a potential prognostic marker for primary breast cancer
    • Magdalena C, Dominguez F, Loidi L, Puente JL (2000) Tumour prothymosin α content, a potential prognostic marker for primary breast cancer. Br J Cancer 82: 584-590
    • (2000) Br J Cancer , vol.82 , pp. 584-590
    • Magdalena, C.1    Dominguez, F.2    Loidi, L.3    Puente, J.L.4
  • 44
    • 0036778619 scopus 로고    scopus 로고
    • Comparative genomic hybridization analysis of primary cutaneous B-cell lymphomas: Identification of common genomic alterations in disease pathogenesis
    • Mao X, Lillington D, Child F, Russell-Jones R, Young B, Whittaker S (2002) Comparative genomic hybridization analysis of primary cutaneous B-cell lymphomas: identification of common genomic alterations in disease pathogenesis. Genes Chromosomes Cancer 35:144-155
    • (2002) Genes Chromosomes Cancer , vol.35 , pp. 144-155
    • Mao, X.1    Lillington, D.2    Child, F.3    Russell-Jones, R.4    Young, B.5    Whittaker, S.6
  • 46
    • 0033864096 scopus 로고    scopus 로고
    • A U-rich element in the 5′ untranslated region is necessary for the translation of p27 mRNA
    • Millard SS, Vidal A, Markus M, Koff A (2000) A U-rich element in the 5′ untranslated region is necessary for the translation of p27 mRNA. Mol Cell Biol 20: 5947-5959
    • (2000) Mol Cell Biol , vol.20 , pp. 5947-5959
    • Millard, S.S.1    Vidal, A.2    Markus, M.3    Koff, A.4
  • 48
    • 0035266295 scopus 로고    scopus 로고
    • HuR, a RNA stability factor, is expressed in malignant brain tumors and binds to adenine- and uridine-rich elements within the 3′ untranslated regions of cytokine and angiogenic factor mRNAs
    • Nabors LB, Gillespie GY, Harkins L, King PH (2001) HuR, a RNA stability factor, is expressed in malignant brain tumors and binds to adenine- and uridine-rich elements within the 3′ untranslated regions of cytokine and angiogenic factor mRNAs. Cancer Res 61: 2154-2161
    • (2001) Cancer Res , vol.61 , pp. 2154-2161
    • Nabors, L.B.1    Gillespie, G.Y.2    Harkins, L.3    King, P.H.4
  • 49
    • 0037428232 scopus 로고    scopus 로고
    • Apoptosis. Life and death decisions
    • Nicholson DW, Thornberry NA (2003) Apoptosis. Life and death decisions. Science 299: 214-215
    • (2003) Science , vol.299 , pp. 214-215
    • Nicholson, D.W.1    Thornberry, N.A.2
  • 50
    • 0038046166 scopus 로고    scopus 로고
    • Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation
    • Nijhawan D, Fang M, Traer E, Zhong Q, Gao W, Du F, Wang X (2003) Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation. Genes Dev 17: 1475-1486
    • (2003) Genes Dev , vol.17 , pp. 1475-1486
    • Nijhawan, D.1    Fang, M.2    Traer, E.3    Zhong, Q.4    Gao, W.5    Du, F.6    Wang, X.7
  • 51
    • 0035910515 scopus 로고    scopus 로고
    • Prothymosin α functions as a cellular oncoprotein by inducing transformation of rodent fibroblasts in vitro
    • Orre RS, Cotter II MA, Subramanian C, Robertson ES (2001) Prothymosin α functions as a cellular oncoprotein by inducing transformation of rodent fibroblasts in vitro. J Biol Chem 276: 1794-1799
    • (2001) J Biol Chem , vol.276 , pp. 1794-1799
    • Orre, R.S.1    Cotter II, M.A.2    Subramanian, C.3    Robertson, E.S.4
  • 52
    • 0033783289 scopus 로고    scopus 로고
    • Fifteen years of prothymosin α: Contradictory past and new horizons
    • Pineiro A, Cordero OJ, Nogueira M (2000) Fifteen years of prothymosin α: contradictory past and new horizons. Peptides 21: 1433-1446
    • (2000) Peptides , vol.21 , pp. 1433-1446
    • Pineiro, A.1    Cordero, O.J.2    Nogueira, M.3
  • 53
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and APAF-1 form an active holoenzyme
    • Rodriguez J, Lazebnik Y (1999) Caspase-9 and APAF-1 form an active holoenzyme. Genes Dev 13: 3179-3184
    • (1999) Genes Dev , vol.13 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 56
    • 0026018529 scopus 로고
    • Prothymosin α antisense oligomers inhibit myeloma cell division
    • Sburlati AR, Manrow RE, Berger SL (1991) Prothymosin α antisense oligomers inhibit myeloma cell division. Proc Natl Acad Sci USA 88: 253-257
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 253-257
    • Sburlati, A.R.1    Manrow, R.E.2    Berger, S.L.3
  • 57
    • 6044269455 scopus 로고    scopus 로고
    • Androgens regulate the binding of endogenous HuR to the AU-rich 3'UTRs of HIF-1α and EGF mRNA
    • Sheflin LG, Zou AP, Spaulding SW (2004) Androgens regulate the binding of endogenous HuR to the AU-rich 3'UTRs of HIF-1α and EGF mRNA. Biochem Biophys Res Commun 322: 644-651
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 644-651
    • Sheflin, L.G.1    Zou, A.P.2    Spaulding, S.W.3
  • 58
    • 0033230435 scopus 로고    scopus 로고
    • Regulation of translation initiation following stress
    • Sheikh MS, Fornace Jr AJ (1999) Regulation of translation initiation following stress. Oncogene 18: 6121-6128
    • (1999) Oncogene , vol.18 , pp. 6121-6128
    • Sheikh, M.S.1    Fornace Jr., A.J.2
  • 61
    • 0036363646 scopus 로고    scopus 로고
    • Mechanisms of transcription-coupled DNA repair
    • Svejstrup JQ (2002) Mechanisms of transcription-coupled DNA repair. Nat Rev Mol Cell Biol 3: 21-29
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 21-29
    • Svejstrup, J.Q.1
  • 62
    • 0026094583 scopus 로고
    • HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and Sex-lethal
    • Szabo A, Dalmau J, Manley G, Rosenfeld M, Wong E, Henson J, Posner JB, Furneaux HM (1991) HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and Sex-lethal. Cell 67: 325-333
    • (1991) Cell , vol.67 , pp. 325-333
    • Szabo, A.1    Dalmau, J.2    Manley, G.3    Rosenfeld, M.4    Wong, E.5    Henson, J.6    Posner, J.B.7    Furneaux, H.M.8
  • 64
    • 0034657686 scopus 로고    scopus 로고
    • HuR regulates cyclin A and cyclin B1 mRNA stability during the cell division cycle
    • Wang W, Lin S, Caldwell CM, Furneaux H, Gorospe M (2000b) HuR Regulates Cyclin A and cyclin B1 mRNA Stability During the Cell Division Cycle. EMBO J 19: 2340-2350
    • (2000) EMBO J , vol.19 , pp. 2340-2350
    • Wang, W.1    Lin, S.2    Caldwell, C.M.3    Furneaux, H.4    Gorospe, M.5
  • 69
    • 0036864153 scopus 로고    scopus 로고
    • AU-rich element-mediated translational control: Complexity and multiple activities of trans-activating factors
    • Zhang T, Kruys V, Huez G, Gueydan C (2002) AU-rich element-mediated translational control: complexity and multiple activities of trans-activating factors. Biochem Soc Trans 30: 952-958
    • (2002) Biochem Soc Trans , vol.30 , pp. 952-958
    • Zhang, T.1    Kruys, V.2    Huez, G.3    Gueydan, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.