메뉴 건너뛰기




Volumn 76, Issue 11, 2008, Pages 1395-1403

Post-transcriptional control of gene expression through subcellular relocalization of mRNA binding proteins

Author keywords

IRES; RNA binding protein; Signaling pathway; Splicing; Subcellular localization; Translation

Indexed keywords

RNA BINDING PROTEIN;

EID: 56149106691     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2008.05.022     Document Type: Article
Times cited : (21)

References (61)
  • 1
    • 0034791334 scopus 로고    scopus 로고
    • Distinct RNP complexes of shuttling hnrnp proteins with pre-mRNA and mRNA: candidate intermediates in formation and export of mRNA
    • Mili S., Shu H.J., Zhao Y., and Pinol-Roma S. Distinct RNP complexes of shuttling hnrnp proteins with pre-mRNA and mRNA: candidate intermediates in formation and export of mRNA. Mol Cell Biol 21 (2001) 7307-7319
    • (2001) Mol Cell Biol , vol.21 , pp. 7307-7319
    • Mili, S.1    Shu, H.J.2    Zhao, Y.3    Pinol-Roma, S.4
  • 2
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Pinol-Roma S., and Dreyfuss G. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 355 (1992) 730-732
    • (1992) Nature , vol.355 , pp. 730-732
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 3
    • 34547651351 scopus 로고    scopus 로고
    • Posttranscriptional orchestration of an anti-apoptotic program by HuR
    • Abdelmohsen K., Lal A., Kim H.H., and Gorospe M. Posttranscriptional orchestration of an anti-apoptotic program by HuR. Cell Cycle 6 (2007) 1288-1292
    • (2007) Cell Cycle , vol.6 , pp. 1288-1292
    • Abdelmohsen, K.1    Lal, A.2    Kim, H.H.3    Gorospe, M.4
  • 4
    • 20144389216 scopus 로고    scopus 로고
    • Cytoplasmic HuR expression is a prognostic factor in invasive ductal breast carcinoma
    • Heinonen M., Bono P., Narko K., Chang S.H., Lundin J., Joensuu H., et al. Cytoplasmic HuR expression is a prognostic factor in invasive ductal breast carcinoma. Cancer Res 65 (2005) 2157-2161
    • (2005) Cancer Res , vol.65 , pp. 2157-2161
    • Heinonen, M.1    Bono, P.2    Narko, K.3    Chang, S.H.4    Lundin, J.5    Joensuu, H.6
  • 5
    • 20744441183 scopus 로고    scopus 로고
    • Enhanced proliferation of cultured human vascular smooth muscle cells linked to increased function of RNA-binding protein HuR
    • Pullmann Jr. R., Juhaszova M., Lopez de Silanes I., Kawai T., Mazan-Mamczarz K., Halushka M.K., et al. Enhanced proliferation of cultured human vascular smooth muscle cells linked to increased function of RNA-binding protein HuR. J Biol Chem 280 (2005) 22819-22826
    • (2005) J Biol Chem , vol.280 , pp. 22819-22826
    • Pullmann Jr., R.1    Juhaszova, M.2    Lopez de Silanes, I.3    Kawai, T.4    Mazan-Mamczarz, K.5    Halushka, M.K.6
  • 7
    • 16944362335 scopus 로고    scopus 로고
    • Purification and characterization of a protein that permits early detection of lung cancer. Identification of heterogeneous nuclear ribonucleoprotein-A2/B1 as the antigen for monoclonal antibody 703D4
    • Zhou J., Mulshine J.L., Unsworth E.J., Scott F.M., Avis I.M., Vos M.D., et al. Purification and characterization of a protein that permits early detection of lung cancer. Identification of heterogeneous nuclear ribonucleoprotein-A2/B1 as the antigen for monoclonal antibody 703D4. J Biol Chem 271 (1996) 10760-10766
    • (1996) J Biol Chem , vol.271 , pp. 10760-10766
    • Zhou, J.1    Mulshine, J.L.2    Unsworth, E.J.3    Scott, F.M.4    Avis, I.M.5    Vos, M.D.6
  • 9
    • 14644445227 scopus 로고    scopus 로고
    • SRprises along a messenger's journey
    • Huang Y., and Steitz J.A. SRprises along a messenger's journey. Mol Cell 17 (2005) 613-615
    • (2005) Mol Cell , vol.17 , pp. 613-615
    • Huang, Y.1    Steitz, J.A.2
  • 10
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss G., Kim V.N., and Kataoka N. Messenger-RNA-binding proteins and the messages they carry. Nat Rev Mol Cell Biol 3 (2002) 195-205
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 11
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley B.R. Sorting out the complexity of SR protein functions. RNA 6 (2000) 1197-1211
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 12
    • 0031929940 scopus 로고    scopus 로고
    • A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm
    • Caceres J.F., Screaton G.R., and Krainer A.R. A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm. Genes Dev 12 (1998) 55-66
    • (1998) Genes Dev , vol.12 , pp. 55-66
    • Caceres, J.F.1    Screaton, G.R.2    Krainer, A.R.3
  • 13
    • 34249654182 scopus 로고    scopus 로고
    • Relocalization of the polypyrimidine tract-binding protein during PKA-induced neurite growth
    • Ma S., Liu G., Sun Y., and Xie J. Relocalization of the polypyrimidine tract-binding protein during PKA-induced neurite growth. Biochim Biophys Acta 1773 (2007) 912-923
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 912-923
    • Ma, S.1    Liu, G.2    Sun, Y.3    Xie, J.4
  • 14
    • 33645089191 scopus 로고    scopus 로고
    • cAMP-dependent phosphorylation of PTB1 promotes the expression of insulin secretory granule proteins in beta cells
    • Knoch K.P., Meisterfeld R., Kersting S., Bergert H., Altkruger A., Wegbrod C., et al. cAMP-dependent phosphorylation of PTB1 promotes the expression of insulin secretory granule proteins in beta cells. Cell Metab 3 (2006) 123-134
    • (2006) Cell Metab , vol.3 , pp. 123-134
    • Knoch, K.P.1    Meisterfeld, R.2    Kersting, S.3    Bergert, H.4    Altkruger, A.5    Wegbrod, C.6
  • 15
    • 0041806593 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein
    • Xie J., Lee J.A., Kress T.L., Mowry K.L., and Black D.L. Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein. Proc Natl Acad Sci USA 100 (2003) 8776-8781
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8776-8781
    • Xie, J.1    Lee, J.A.2    Kress, T.L.3    Mowry, K.L.4    Black, D.L.5
  • 16
    • 0035095885 scopus 로고    scopus 로고
    • ERK phosphorylation drives cytoplasmic accumulation of hnRNP-K and inhibition of mRNA translation
    • Habelhah H., Shah K., Huang L., Ostareck-Lederer A., Burlingame A.L., Shokat K.M., et al. ERK phosphorylation drives cytoplasmic accumulation of hnRNP-K and inhibition of mRNA translation. Nat Cell Biol 3 (2001) 325-330
    • (2001) Nat Cell Biol , vol.3 , pp. 325-330
    • Habelhah, H.1    Shah, K.2    Huang, L.3    Ostareck-Lederer, A.4    Burlingame, A.L.5    Shokat, K.M.6
  • 17
    • 34250362729 scopus 로고    scopus 로고
    • Protein kinase C alpha-dependent phosphorylation of the mRNA-stabilizing factor HuR: implications for posttranscriptional regulation of cyclooxygenase-2
    • Doller A., Huwiler A., Muller R., Radeke H.H., Pfeilschifter J., and Eberhardt W. Protein kinase C alpha-dependent phosphorylation of the mRNA-stabilizing factor HuR: implications for posttranscriptional regulation of cyclooxygenase-2. Mol Biol Cell 18 (2007) 2137-2148
    • (2007) Mol Biol Cell , vol.18 , pp. 2137-2148
    • Doller, A.1    Huwiler, A.2    Muller, R.3    Radeke, H.H.4    Pfeilschifter, J.5    Eberhardt, W.6
  • 18
    • 0037101633 scopus 로고    scopus 로고
    • Ischemia induces a translocation of the splicing factor tra2-beta 1 and changes alternative splicing patterns in the brain
    • Daoud R., Mies G., Smialowska A., Olah L., Hossmann K.A., and Stamm S. Ischemia induces a translocation of the splicing factor tra2-beta 1 and changes alternative splicing patterns in the brain. J Neurosci 22 (2002) 5889-5899
    • (2002) J Neurosci , vol.22 , pp. 5889-5899
    • Daoud, R.1    Mies, G.2    Smialowska, A.3    Olah, L.4    Hossmann, K.A.5    Stamm, S.6
  • 19
    • 33847795858 scopus 로고    scopus 로고
    • Cell stress modulates the function of splicing regulatory protein RBM4 in translation control
    • Lin J.C., Hsu M., and Tarn W.Y. Cell stress modulates the function of splicing regulatory protein RBM4 in translation control. Proc Natl Acad Sci USA 104 (2007) 2235-2240
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2235-2240
    • Lin, J.C.1    Hsu, M.2    Tarn, W.Y.3
  • 20
    • 0007570010 scopus 로고    scopus 로고
    • The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation
    • van der Houven van Oordt W., Diaz-Meco M.T., Lozano J., Krainer A.R., Moscat J., and Caceres J.F. The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation. J Cell Biol 149 (2000) 307-316
    • (2000) J Cell Biol , vol.149 , pp. 307-316
    • van der Houven van Oordt, W.1    Diaz-Meco, M.T.2    Lozano, J.3    Krainer, A.R.4    Moscat, J.5    Caceres, J.F.6
  • 21
    • 33746516731 scopus 로고    scopus 로고
    • hnRNP A1 relocalization to the stress granules reflects a role in the stress response
    • Guil S., Long J.C., and Caceres J.F. hnRNP A1 relocalization to the stress granules reflects a role in the stress response. Mol Cell Biol 26 (2006) 5744-5758
    • (2006) Mol Cell Biol , vol.26 , pp. 5744-5758
    • Guil, S.1    Long, J.C.2    Caceres, J.F.3
  • 22
    • 56149096075 scopus 로고    scopus 로고
    • Regulation of heterogenous nuclear ribonucleoprotein A1 transport by phosphorylation in cells stressed by osmotic shock
    • Allemand E., Guil S., Myers M., Moscat J., Caceres J.F., and Krainer A.R. Regulation of heterogenous nuclear ribonucleoprotein A1 transport by phosphorylation in cells stressed by osmotic shock. Proc Natl Acad Sci USA 28 (2005) 28
    • (2005) Proc Natl Acad Sci USA , vol.28 , pp. 28
    • Allemand, E.1    Guil, S.2    Myers, M.3    Moscat, J.4    Caceres, J.F.5    Krainer, A.R.6
  • 23
    • 56149088398 scopus 로고    scopus 로고
    • Nuclear efflux of heterogeneous nuclear ribonucleoprotein C1/C2 in apoptotic cells: a novel nuclear export dependent on Rho-associated kinase activation
    • Lee H.H., Chien C.L., Liao H.K., Chen Y.J., and Chang Z.F. Nuclear efflux of heterogeneous nuclear ribonucleoprotein C1/C2 in apoptotic cells: a novel nuclear export dependent on Rho-associated kinase activation. J Cell Sci 19 (2004) 19
    • (2004) J Cell Sci , vol.19 , pp. 19
    • Lee, H.H.1    Chien, C.L.2    Liao, H.K.3    Chen, Y.J.4    Chang, Z.F.5
  • 24
    • 17244383094 scopus 로고    scopus 로고
    • Stress alters the subcellular distribution of hSlu7 and thus modulates alternative splicing
    • Shomron N., Alberstein M., Reznik M., and Ast G. Stress alters the subcellular distribution of hSlu7 and thus modulates alternative splicing. J Cell Sci 118 (2005) 1151-1159
    • (2005) J Cell Sci , vol.118 , pp. 1151-1159
    • Shomron, N.1    Alberstein, M.2    Reznik, M.3    Ast, G.4
  • 25
    • 38749154721 scopus 로고    scopus 로고
    • Polyamines modulate the subcellular localization of RNA-binding protein HuR through AMP-activated protein kinase-regulated phosphorylation and acetylation of importin alpha1
    • Zou T., Liu L., Rao J.N., Marasa B.S., Chen J., Xiao L., et al. Polyamines modulate the subcellular localization of RNA-binding protein HuR through AMP-activated protein kinase-regulated phosphorylation and acetylation of importin alpha1. Biochem J 409 (2008) 389-398
    • (2008) Biochem J , vol.409 , pp. 389-398
    • Zou, T.1    Liu, L.2    Rao, J.N.3    Marasa, B.S.4    Chen, J.5    Xiao, L.6
  • 28
    • 0141640857 scopus 로고    scopus 로고
    • Stabilization of urokinase and urokinase receptor mRNAs by HuR is linked to its cytoplasmic accumulation induced by activated mitogen-activated protein kinase-activated protein kinase 2
    • Tran H., Maurer F., and Nagamine Y. Stabilization of urokinase and urokinase receptor mRNAs by HuR is linked to its cytoplasmic accumulation induced by activated mitogen-activated protein kinase-activated protein kinase 2. Mol Cell Biol 23 (2003) 7177-7188
    • (2003) Mol Cell Biol , vol.23 , pp. 7177-7188
    • Tran, H.1    Maurer, F.2    Nagamine, Y.3
  • 29
    • 0141521567 scopus 로고    scopus 로고
    • The yeast hnRNP-like protein Hrp1/Nab4 sccumulates in the cytoplasm after hyperosmotic stress: a novel Fps1-dependent response
    • Henry M.F., Mandel D., Routson V., and Henry P.A. The yeast hnRNP-like protein Hrp1/Nab4 sccumulates in the cytoplasm after hyperosmotic stress: a novel Fps1-dependent response. Mol Biol Cell 14 (2003) 3929-3941
    • (2003) Mol Biol Cell , vol.14 , pp. 3929-3941
    • Henry, M.F.1    Mandel, D.2    Routson, V.3    Henry, P.A.4
  • 30
    • 34347393968 scopus 로고    scopus 로고
    • Involvement of transportin 2-mediated HuR import in muscle cell differentiation
    • van der Giessen K., and Gallouzi I.E. Involvement of transportin 2-mediated HuR import in muscle cell differentiation. Mol Biol Cell 18 (2007) 2619-2629
    • (2007) Mol Biol Cell , vol.18 , pp. 2619-2629
    • van der Giessen, K.1    Gallouzi, I.E.2
  • 31
    • 0035863125 scopus 로고    scopus 로고
    • Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition
    • Gustin K.E., and Sarnow P. Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition. EMBO J 20 (2001) 240-249
    • (2001) EMBO J , vol.20 , pp. 240-249
    • Gustin, K.E.1    Sarnow, P.2
  • 32
    • 33745849149 scopus 로고    scopus 로고
    • Polyamine depletion increases cytoplasmic levels of RNA-binding protein HuR leading to stabilization of nucleophosmin and p53 mRNAs
    • Zou T., Mazan-Mamczarz K., Rao J.N., Liu L., Marasa B.S., Zhang A.H., et al. Polyamine depletion increases cytoplasmic levels of RNA-binding protein HuR leading to stabilization of nucleophosmin and p53 mRNAs. J Biol Chem 281 (2006) 19387-19394
    • (2006) J Biol Chem , vol.281 , pp. 19387-19394
    • Zou, T.1    Mazan-Mamczarz, K.2    Rao, J.N.3    Liu, L.4    Marasa, B.S.5    Zhang, A.H.6
  • 33
    • 37049030005 scopus 로고    scopus 로고
    • Cytoplasmic relocalization of heterogeneous nuclear ribonucleoprotein A1 controls translation initiation of specific mRNAs
    • Cammas A., Pileur F., Bonnal S., Lewis S.M., Leveque N., Holcik M., et al. Cytoplasmic relocalization of heterogeneous nuclear ribonucleoprotein A1 controls translation initiation of specific mRNAs. Mol Biol Cell 18 (2007) 5048-5059
    • (2007) Mol Biol Cell , vol.18 , pp. 5048-5059
    • Cammas, A.1    Pileur, F.2    Bonnal, S.3    Lewis, S.M.4    Leveque, N.5    Holcik, M.6
  • 34
    • 34247234065 scopus 로고    scopus 로고
    • Subcellular relocalization of a trans-acting factor regulates XIAP IRES-dependent translation
    • Lewis S.M., Veyrier A., Hosszu Ungureanu N., Bonnal S., Vagner S., and Holcik M. Subcellular relocalization of a trans-acting factor regulates XIAP IRES-dependent translation. Mol Biol Cell 18 (2007) 1302-1311
    • (2007) Mol Biol Cell , vol.18 , pp. 1302-1311
    • Lewis, S.M.1    Veyrier, A.2    Hosszu Ungureanu, N.3    Bonnal, S.4    Vagner, S.5    Holcik, M.6
  • 35
    • 36049032156 scopus 로고    scopus 로고
    • The cold-inducible RNA-binding protein migrates from the nucleus to cytoplasmic stress granules by a methylation-dependent mechanism and acts as a translational repressor
    • De Leeuw F., Zhang T., Wauquier C., Huez G., Kruys V., and Gueydan C. The cold-inducible RNA-binding protein migrates from the nucleus to cytoplasmic stress granules by a methylation-dependent mechanism and acts as a translational repressor. Exp Cell Res 313 (2007) 4130-4144
    • (2007) Exp Cell Res , vol.313 , pp. 4130-4144
    • De Leeuw, F.1    Zhang, T.2    Wauquier, C.3    Huez, G.4    Kruys, V.5    Gueydan, C.6
  • 36
    • 0036639425 scopus 로고    scopus 로고
    • Internal ribosome entry site-mediated translation of Smad5 in vivo: requirement for a nuclear event
    • Shiroki K., Ohsawa C., Sugi N., Wakiyama M., Miura K., Watanabe M., et al. Internal ribosome entry site-mediated translation of Smad5 in vivo: requirement for a nuclear event. Nucleic Acids Res 30 (2002) 2851-2861
    • (2002) Nucleic Acids Res , vol.30 , pp. 2851-2861
    • Shiroki, K.1    Ohsawa, C.2    Sugi, N.3    Wakiyama, M.4    Miura, K.5    Watanabe, M.6
  • 37
    • 0034141958 scopus 로고    scopus 로고
    • Analysis of the c-myc IRES; a potential role for cell-type specific trans-acting factors and the nuclear compartment
    • Stoneley M., Subkhankulova T., Le Quesne J.P., Coldwell M.J., Jopling C.L., Belsham G.J., et al. Analysis of the c-myc IRES; a potential role for cell-type specific trans-acting factors and the nuclear compartment. Nucleic Acids Res 28 (2000) 687-694
    • (2000) Nucleic Acids Res , vol.28 , pp. 687-694
    • Stoneley, M.1    Subkhankulova, T.2    Le Quesne, J.P.3    Coldwell, M.J.4    Jopling, C.L.5    Belsham, G.J.6
  • 38
    • 1642488249 scopus 로고    scopus 로고
    • Functional dissection of hnRNP D suggests that nuclear import is required before hnRNP D can modulate mRNA turnover in the cytoplasm
    • Chen C.Y., Xu N., Zhu W., and Shyu A.B. Functional dissection of hnRNP D suggests that nuclear import is required before hnRNP D can modulate mRNA turnover in the cytoplasm. RNA 10 (2004) 669-680
    • (2004) RNA , vol.10 , pp. 669-680
    • Chen, C.Y.1    Xu, N.2    Zhu, W.3    Shyu, A.B.4
  • 39
    • 0035658308 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of polypyrimidine tract-binding protein is uncoupled from RNA export
    • Kamath R.V., Leary D.J., and Huang S. Nucleocytoplasmic shuttling of polypyrimidine tract-binding protein is uncoupled from RNA export. Mol Biol Cell 12 (2001) 3808-3820
    • (2001) Mol Biol Cell , vol.12 , pp. 3808-3820
    • Kamath, R.V.1    Leary, D.J.2    Huang, S.3
  • 40
    • 1642560921 scopus 로고    scopus 로고
    • Control of nuclear export of hnRNP A1
    • Lichtenstein M., Guo W., and Tartakoff A.M. Control of nuclear export of hnRNP A1. Traffic 2 (2001) 261-267
    • (2001) Traffic , vol.2 , pp. 261-267
    • Lichtenstein, M.1    Guo, W.2    Tartakoff, A.M.3
  • 41
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M., and Sonenberg N. Translational control in stress and apoptosis. Nat Rev Mol Cell Biol 6 (2005) 318-327
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 42
    • 34547907409 scopus 로고    scopus 로고
    • A search for structurally similar cellular internal ribosome entry sites
    • Baird S.D., Lewis S.M., Turcotte M., and Holcik M. A search for structurally similar cellular internal ribosome entry sites. Nucleic Acids Res 35 (2007) 4664-4677
    • (2007) Nucleic Acids Res , vol.35 , pp. 4664-4677
    • Baird, S.D.1    Lewis, S.M.2    Turcotte, M.3    Holcik, M.4
  • 43
    • 20044389169 scopus 로고    scopus 로고
    • Internal ribosome entry segment-mediated translation during apoptosis: the role of IRES-trans-acting factors
    • Spriggs K.A., Bushell M., Mitchell S.A., and Willis A.E. Internal ribosome entry segment-mediated translation during apoptosis: the role of IRES-trans-acting factors. Cell Death Differ 12 (2005) 585-591
    • (2005) Cell Death Differ , vol.12 , pp. 585-591
    • Spriggs, K.A.1    Bushell, M.2    Mitchell, S.A.3    Willis, A.E.4
  • 44
    • 0036899079 scopus 로고    scopus 로고
    • Apoptosomes: engines for caspase activation
    • Adams J.M., and Cory S. Apoptosomes: engines for caspase activation. Curr Opin Cell Biol 14 (2002) 715-720
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 715-720
    • Adams, J.M.1    Cory, S.2
  • 46
    • 27644466946 scopus 로고    scopus 로고
    • Exon selection in alpha-tropomyosin mRNA is regulated by the antagonistic action of RBM4 and PTB
    • Lin J.C., and Tarn W.Y. Exon selection in alpha-tropomyosin mRNA is regulated by the antagonistic action of RBM4 and PTB. Mol Cell Biol 25 (2005) 10111-10121
    • (2005) Mol Cell Biol , vol.25 , pp. 10111-10121
    • Lin, J.C.1    Tarn, W.Y.2
  • 48
    • 0034657686 scopus 로고    scopus 로고
    • HuR regulates cyclin A and cyclin B1 mRNA stability during cell proliferation
    • Wang W., Caldwell M.C., Lin S., Furneaux H., and Gorospe M. HuR regulates cyclin A and cyclin B1 mRNA stability during cell proliferation. EMBO J 19 (2000) 2340-2350
    • (2000) EMBO J , vol.19 , pp. 2340-2350
    • Wang, W.1    Caldwell, M.C.2    Lin, S.3    Furneaux, H.4    Gorospe, M.5
  • 49
    • 0035861655 scopus 로고    scopus 로고
    • The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a protective role in the genotoxic stress response
    • Yang C., and Carrier F. The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a protective role in the genotoxic stress response. J Biol Chem 276 (2001) 47277-47284
    • (2001) J Biol Chem , vol.276 , pp. 47277-47284
    • Yang, C.1    Carrier, F.2
  • 51
    • 26444568259 scopus 로고    scopus 로고
    • Compartmentalization of hnRNP-K during cell cycle progression and its interaction with calponin in the cytoplasm
    • Laury-Kleintop L.D., Tresini M., and Hammond O. Compartmentalization of hnRNP-K during cell cycle progression and its interaction with calponin in the cytoplasm. J Cell Biochem 95 (2005) 1042-1056
    • (2005) J Cell Biochem , vol.95 , pp. 1042-1056
    • Laury-Kleintop, L.D.1    Tresini, M.2    Hammond, O.3
  • 52
    • 0027193593 scopus 로고
    • La autoantigen enhances and corrects aberrant translation of poliovirus RNA in reticulocyte lysate
    • Meerovitch K., Svitkin Y.V., Lee H.S., Lejbkowicz F., Kenan D.J., Chan E.K., et al. La autoantigen enhances and corrects aberrant translation of poliovirus RNA in reticulocyte lysate. J Virol 67 (1993) 3798-3807
    • (1993) J Virol , vol.67 , pp. 3798-3807
    • Meerovitch, K.1    Svitkin, Y.V.2    Lee, H.S.3    Lejbkowicz, F.4    Kenan, D.J.5    Chan, E.K.6
  • 53
    • 0028928016 scopus 로고
    • The RNA-binding protein TIAR is translocated from the nucleus to the cytoplasm during Fas-mediated apoptotic cell death
    • Taupin J.L., Tian Q., Kedersha N., Robertson M., and Anderson P. The RNA-binding protein TIAR is translocated from the nucleus to the cytoplasm during Fas-mediated apoptotic cell death. Proc Natl Acad Sci USA 92 (1995) 1629-1633
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1629-1633
    • Taupin, J.L.1    Tian, Q.2    Kedersha, N.3    Robertson, M.4    Anderson, P.5
  • 54
    • 35848932765 scopus 로고    scopus 로고
    • Polyamines regulate the stability of activating transcription factor-2 mRNA through RNA-binding protein HuR in intestinal epithelial cells
    • Xiao L., Rao J.N., Zou T., Liu L., Marasa B.S., Chen J., et al. Polyamines regulate the stability of activating transcription factor-2 mRNA through RNA-binding protein HuR in intestinal epithelial cells. Mol Biol Cell 18 (2007) 4579-4590
    • (2007) Mol Biol Cell , vol.18 , pp. 4579-4590
    • Xiao, L.1    Rao, J.N.2    Zou, T.3    Liu, L.4    Marasa, B.S.5    Chen, J.6
  • 55
    • 0347064348 scopus 로고    scopus 로고
    • ATP potentiates interleukin-1 beta-induced MMP-9 expression in mesangial cells via recruitment of the ELAV protein HuR
    • Huwiler A., Akool el S., Aschrafi A., Hamada F.M., Pfeilschifter J., and Eberhardt W. ATP potentiates interleukin-1 beta-induced MMP-9 expression in mesangial cells via recruitment of the ELAV protein HuR. J Biol Chem 278 (2003) 51758-51769
    • (2003) J Biol Chem , vol.278 , pp. 51758-51769
    • Huwiler, A.1    Akool el, S.2    Aschrafi, A.3    Hamada, F.M.4    Pfeilschifter, J.5    Eberhardt, W.6
  • 56
    • 24344496907 scopus 로고    scopus 로고
    • RNA-binding protein HuR is required for stabilization of SLC11A1 mRNA and SLC11A1 protein expression
    • Xu Y.Z., Di Marco S., Gallouzi I., Rola-Pleszczynski M., and Radzioch D. RNA-binding protein HuR is required for stabilization of SLC11A1 mRNA and SLC11A1 protein expression. Mol Cell Biol 25 (2005) 8139-8149
    • (2005) Mol Cell Biol , vol.25 , pp. 8139-8149
    • Xu, Y.Z.1    Di Marco, S.2    Gallouzi, I.3    Rola-Pleszczynski, M.4    Radzioch, D.5
  • 57
    • 0141643318 scopus 로고    scopus 로고
    • Chronic ethanol exposure increases the binding of HuR to the TNFalpha 3′-untranslated region in macrophages
    • McMullen M.R., Cocuzzi E., Hatzoglou M., and Nagy L.E. Chronic ethanol exposure increases the binding of HuR to the TNFalpha 3′-untranslated region in macrophages. J Biol Chem 278 (2003) 38333-38341
    • (2003) J Biol Chem , vol.278 , pp. 38333-38341
    • McMullen, M.R.1    Cocuzzi, E.2    Hatzoglou, M.3    Nagy, L.E.4
  • 58
    • 33845799125 scopus 로고    scopus 로고
    • Apigenin prevents UVB-induced cyclooxygenase 2 expression: coupled mRNA stabilization and translational inhibition
    • Tong X., Van Dross R.T., Abu-Yousif A., Morrison A.R., and Pelling J.C. Apigenin prevents UVB-induced cyclooxygenase 2 expression: coupled mRNA stabilization and translational inhibition. Mol Cell Biol 27 (2007) 283-296
    • (2007) Mol Cell Biol , vol.27 , pp. 283-296
    • Tong, X.1    Van Dross, R.T.2    Abu-Yousif, A.3    Morrison, A.R.4    Pelling, J.C.5
  • 59
    • 4544348925 scopus 로고    scopus 로고
    • Stability of A+U-rich element binding factor 1 (AUF1)-binding messenger ribonucleic acid correlates with the subcellular relocalization of AUF1 in the rat uterus upon estrogen treatment
    • Arao Y., Kikuchi A., Kishida M., Yonekura M., Inoue A., Yasuda S., et al. Stability of A+U-rich element binding factor 1 (AUF1)-binding messenger ribonucleic acid correlates with the subcellular relocalization of AUF1 in the rat uterus upon estrogen treatment. Mol Endocrinol 18 (2004) 2255-2267
    • (2004) Mol Endocrinol , vol.18 , pp. 2255-2267
    • Arao, Y.1    Kikuchi, A.2    Kishida, M.3    Yonekura, M.4    Inoue, A.5    Yasuda, S.6
  • 61
    • 0029046727 scopus 로고
    • Identification of heterogeneous ribonucleoprotein A1 as a novel substrate for protein kinase C zeta
    • Municio M.M., Lozano J., Sanchez P., Moscat J., and Diaz-Meco M.T. Identification of heterogeneous ribonucleoprotein A1 as a novel substrate for protein kinase C zeta. J Biol Chem 270 (1995) 15884-15891
    • (1995) J Biol Chem , vol.270 , pp. 15884-15891
    • Municio, M.M.1    Lozano, J.2    Sanchez, P.3    Moscat, J.4    Diaz-Meco, M.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.