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Volumn 343, Issue 1, 2006, Pages 57-68

Identification of FUSE-binding proteins as interacting partners of TIA proteins

Author keywords

RNA binding proteins; Stress granules

Indexed keywords

BINDING PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; FUSE BINDING PROTEIN; MESSENGER RNA; PROTEIN TIA 1; PROTEIN TIAR; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 33645103357     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.02.112     Document Type: Article
Times cited : (26)

References (46)
  • 1
    • 0029810447 scopus 로고    scopus 로고
    • Structure, tissue distribution and genomic organization of the murine RRM-type RNA binding proteins TIA-1 and TIAR
    • A.R. Beck, Q.G. Medley, S. O'Brien, P. Anderson, and M. Streuli Structure, tissue distribution and genomic organization of the murine RRM-type RNA binding proteins TIA-1 and TIAR Nucleic Acids Res. 24 1996 3829 3835
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3829-3835
    • Beck, A.R.1    Medley, Q.G.2    O'Brien, S.3    Anderson, P.4    Streuli, M.5
  • 3
    • 0033838148 scopus 로고    scopus 로고
    • The RNA-binding protein TIA-1 is a novel mammalian splicing regulator acting through intron sequences adjacent to a 5′ splice site
    • F. Gatto-Konczak, C.F. Bourgeois, C. Le Guiner, L. Kister, M.C. Gesnel, J. Stevenin, and R. Breathnach The RNA-binding protein TIA-1 is a novel mammalian splicing regulator acting through intron sequences adjacent to a 5′ splice site Mol. Cell. Biol. 20 2000 6287 6299
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6287-6299
    • Gatto-Konczak, F.1    Bourgeois, C.F.2    Le Guiner, C.3    Kister, L.4    Gesnel, M.C.5    Stevenin, J.6    Breathnach, R.7
  • 4
    • 0042971860 scopus 로고    scopus 로고
    • U1 snRNP-dependent function of TIAR in the regulation of alternative RNA processing of the human calcitonin/CGRP pre-mRNA
    • H. Zhu, R.A. Hasman, K.M. Young, N.L. Kedersha, and H. Lou U1 snRNP-dependent function of TIAR in the regulation of alternative RNA processing of the human calcitonin/CGRP pre-mRNA Mol. Cell. Biol. 23 2003 5959 5971
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5959-5971
    • Zhu, H.1    Hasman, R.A.2    Young, K.M.3    Kedersha, N.L.4    Lou, H.5
  • 5
    • 0037121924 scopus 로고    scopus 로고
    • The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5′ splice sites
    • P. Forch, O. Puig, C. Martinez, B. Seraphin, and J. Valcarcel The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5′ splice sites EMBO J. 21 2002 6882 6892
    • (2002) EMBO J. , vol.21 , pp. 6882-6892
    • Forch, P.1    Puig, O.2    Martinez, C.3    Seraphin, B.4    Valcarcel, J.5
  • 8
    • 0037449716 scopus 로고    scopus 로고
    • Translational repression of human matrix metalloproteinases-13 by an alternatively spliced form of T-cell-restricted intracellular antigen-related protein (TIAR)
    • Q. Yu, S.J. Cok, C. Zeng, and A.R. Morrison Translational repression of human matrix metalloproteinases-13 by an alternatively spliced form of T-cell-restricted intracellular antigen-related protein (TIAR) J. Biol. Chem. 278 2003 1579 1584
    • (2003) J. Biol. Chem. , vol.278 , pp. 1579-1584
    • Yu, Q.1    Cok, S.J.2    Zeng, C.3    Morrison, A.R.4
  • 9
    • 12544258221 scopus 로고    scopus 로고
    • Translational control of beta2-adrenergic receptor mRNA by T-cell-restricted intracellular antigen-related protein
    • K. Kandasamy, K. Joseph, K. Subramaniam, J.R. Raymond, and B.G. Tholanikunnel Translational control of beta2-adrenergic receptor mRNA by T-cell-restricted intracellular antigen-related protein J. Biol. Chem. 280 2005 1931 1943
    • (2005) J. Biol. Chem. , vol.280 , pp. 1931-1943
    • Kandasamy, K.1    Joseph, K.2    Subramaniam, K.3    Raymond, J.R.4    Tholanikunnel, B.G.5
  • 10
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • N.L. Kedersha, M. Gupta, W. Li, I. Miller, and P. Anderson RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules J. Cell Biol. 147 1999 1431 1442
    • (1999) J. Cell Biol. , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 12
    • 0020826867 scopus 로고
    • Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves
    • L. Nover, K.D. Scharf, and D. Neumann Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves Mol. Cell. Biol. 3 1983 1648 1655
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 1648-1655
    • Nover, L.1    Scharf, K.D.2    Neumann, D.3
  • 13
    • 0024639409 scopus 로고
    • Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs
    • L. Nover, K.D. Scharf, and D. Neumann Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs Mol. Cell. Biol. 9 1989 1298 1308
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1298-1308
    • Nover, L.1    Scharf, K.D.2    Neumann, D.3
  • 14
    • 0036154218 scopus 로고    scopus 로고
    • Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules
    • N. Kedersha, S. Chen, N. Gilks, W. Li, I.J. Miller, J. Stahl, and P. Anderson Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules Mol. Biol. Cell 13 2002 195 210
    • (2002) Mol. Biol. Cell , vol.13 , pp. 195-210
    • Kedersha, N.1    Chen, S.2    Gilks, N.3    Li, W.4    Miller, I.J.5    Stahl, J.6    Anderson, P.7
  • 15
    • 23344454050 scopus 로고    scopus 로고
    • Novel DNA-binding properties of the RNA-binding protein TIAR
    • E.A. Suswam, Y.Y. Li, H. Mahtani, and P.H. King Novel DNA-binding properties of the RNA-binding protein TIAR Nucleic Acids Res. 33 2005 4507 4518
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4507-4518
    • Suswam, E.A.1    Li, Y.Y.2    Mahtani, H.3    King, P.H.4
  • 16
    • 0026639625 scopus 로고
    • Protein interaction cloning in yeast: Identification of mammalian proteins that react with the leucine zipper of Jun
    • P.M. Chevray, and D. Nathans Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun Proc. Natl. Acad. Sci. USA 89 1992 5789 5793
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5789-5793
    • Chevray, P.M.1    Nathans, D.2
  • 17
    • 2342668459 scopus 로고    scopus 로고
    • A protein linked to mitochondrion development in Trypanosoma brucei
    • D. Perez-Morga, and E. Pays A protein linked to mitochondrion development in Trypanosoma brucei Mol. Biochem. Parasitol. 101 1999 161 172
    • (1999) Mol. Biochem. Parasitol. , vol.101 , pp. 161-172
    • Perez-Morga, D.1    Pays, E.2
  • 18
    • 0344737844 scopus 로고    scopus 로고
    • Identification of BOIP, a novel cDNA highly expressed during spermatogenesis that encodes a protein interacting with the orange domain of the hairy-related transcription factor HRT1/Hey1 in Xenopus and mouse
    • R. Van Wayenbergh, V. Taelman, B. Pichon, A. Fischer, S. Kricha, M. Gessler, D. Christophe, and E.J. Bellefroid Identification of BOIP, a novel cDNA highly expressed during spermatogenesis that encodes a protein interacting with the orange domain of the hairy-related transcription factor HRT1/Hey1 in Xenopus and mouse Dev. Dyn. 228 2003 716 725
    • (2003) Dev. Dyn. , vol.228 , pp. 716-725
    • Van Wayenbergh, R.1    Taelman, V.2    Pichon, B.3    Fischer, A.4    Kricha, S.5    Gessler, M.6    Christophe, D.7    Bellefroid, E.J.8
  • 19
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • P. James, J. Halladay, and E.A. Craig Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast Genetics 144 1996 1425 1436
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 22
    • 0029783099 scopus 로고    scopus 로고
    • Engagement of tumor necrosis factor mRNA by an endotoxin-inducible cytoplasmic protein
    • C. Gueydan, L. Houzet, A. Marchant, A. Sels, G. Huez, and V. Kruys Engagement of tumor necrosis factor mRNA by an endotoxin-inducible cytoplasmic protein Mol. Med. 2 1996 479 488
    • (1996) Mol. Med. , vol.2 , pp. 479-488
    • Gueydan, C.1    Houzet, L.2    Marchant, A.3    Sels, A.4    Huez, G.5    Kruys, V.6
  • 23
    • 0037033786 scopus 로고    scopus 로고
    • A predominantly nuclear protein affecting cytoplasmic localization of beta-actin mRNA in fibroblasts and neurons
    • W. Gu, F. Pan, H. Zhang, G.J. Bassell, and R.H. Singer A predominantly nuclear protein affecting cytoplasmic localization of beta-actin mRNA in fibroblasts and neurons J. Cell Biol. 156 2002 41 51
    • (2002) J. Cell Biol. , vol.156 , pp. 41-51
    • Gu, W.1    Pan, F.2    Zhang, H.3    Bassell, G.J.4    Singer, R.H.5
  • 24
    • 0034669314 scopus 로고    scopus 로고
    • Nuclear targeting determinants of the far upstream element binding protein, a c-myc transcription factor
    • L. He, A. Weber, and D. Levens Nuclear targeting determinants of the far upstream element binding protein, a c-myc transcription factor Nucleic Acids Res. 28 2000 4558 4565
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4558-4565
    • He, L.1    Weber, A.2    Levens, D.3
  • 25
    • 0019570066 scopus 로고
    • Monoclonal antibodies to nucleic acid-containing cellular constituents: Probes for molecular biology and autoimmune disease
    • E.A. Lerner, M.R. Lerner, C.A. Janeway Jr., and J.A. Steitz Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease Proc. Natl. Acad. Sci. USA 78 1981 2737 2741
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2737-2741
    • Lerner, E.A.1    Lerner, M.R.2    Janeway Jr., C.A.3    Steitz, J.A.4
  • 28
    • 24144499990 scopus 로고    scopus 로고
    • Involvement of KSRP in the post-transcriptional regulation of human iNOS expression-complex interplay of KSRP with TTP and HuR
    • K. Linker, A. Pautz, M. Fechir, T. Hubrich, J. Greeve, and H. Kleinert Involvement of KSRP in the post-transcriptional regulation of human iNOS expression-complex interplay of KSRP with TTP and HuR Nucleic Acids Res. 33 2005 4813 4827
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4813-4827
    • Linker, K.1    Pautz, A.2    Fechir, M.3    Hubrich, T.4    Greeve, J.5    Kleinert, H.6
  • 29
    • 2942612333 scopus 로고    scopus 로고
    • A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery
    • R. Gherzi, K.Y. Lee, P. Briata, D. Wegmuller, C. Moroni, M. Karin, and C.Y. Chen A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery Mol. Cell 14 2004 571 583
    • (2004) Mol. Cell , vol.14 , pp. 571-583
    • Gherzi, R.1    Lee, K.Y.2    Briata, P.3    Wegmuller, D.4    Moroni, C.5    Karin, M.6    Chen, C.Y.7
  • 30
    • 0028206551 scopus 로고
    • A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif
    • R. Duncan, L. Bazar, G. Michelotti, T. Tomonaga, H. Krutzsch, M. Avigan, and D. Levens A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif Genes Dev. 8 1994 465 480
    • (1994) Genes Dev. , vol.8 , pp. 465-480
    • Duncan, R.1    Bazar, L.2    Michelotti, G.3    Tomonaga, T.4    Krutzsch, H.5    Avigan, M.6    Levens, D.7
  • 31
    • 0030969572 scopus 로고    scopus 로고
    • A new regulatory protein, KSRP, mediates exon inclusion through an intronic splicing enhancer
    • H. Min, C.W. Turck, J.M. Nikolic, and D.L. Black A new regulatory protein, KSRP, mediates exon inclusion through an intronic splicing enhancer Genes Dev. 11 1997 1023 1036
    • (1997) Genes Dev. , vol.11 , pp. 1023-1036
    • Min, H.1    Turck, C.W.2    Nikolic, J.M.3    Black, D.L.4
  • 32
    • 0036724607 scopus 로고    scopus 로고
    • Molecular characterization of MARTA1, a protein interacting with the dendritic targeting element of MAP2 mRNAs
    • M. Rehbein, K. Wege, F. Buck, M. Schweizer, D. Richter, and S. Kindler Molecular characterization of MARTA1, a protein interacting with the dendritic targeting element of MAP2 mRNAs J. Neurochem. 82 2002 1039 1046
    • (2002) J. Neurochem. , vol.82 , pp. 1039-1046
    • Rehbein, M.1    Wege, K.2    Buck, F.3    Schweizer, M.4    Richter, D.5    Kindler, S.6
  • 33
    • 0030724031 scopus 로고    scopus 로고
    • Compartmentalization of eukaryotic gene expression: Causes and effects
    • R.H. Singer, and M.R. Green Compartmentalization of eukaryotic gene expression: causes and effects Cell 91 1997 291 294
    • (1997) Cell , vol.91 , pp. 291-294
    • Singer, R.H.1    Green, M.R.2
  • 34
    • 0029112561 scopus 로고
    • The nuclear matrix phosphoprotein p255 associates with splicing complexes as part of the [U4/U6.U5] tri-snRNP particle
    • B. Chabot, S. Bisotto, and M. Vincent The nuclear matrix phosphoprotein p255 associates with splicing complexes as part of the [U4/U6.U5] tri-snRNP particle Nucleic Acids Res. 23 1995 3206 3213
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3206-3213
    • Chabot, B.1    Bisotto, S.2    Vincent, M.3
  • 35
    • 0028867814 scopus 로고
    • The generally expressed hnRNP F is involved in a neural-specific pre-mRNA splicing event
    • H. Min, R.C. Chan, and D.L. Black The generally expressed hnRNP F is involved in a neural-specific pre-mRNA splicing event Genes Dev. 9 1995 2659 2671
    • (1995) Genes Dev. , vol.9 , pp. 2659-2671
    • Min, H.1    Chan, R.C.2    Black, D.L.3
  • 36
    • 0026718947 scopus 로고
    • Identification and developmental expression of Src+ mRNAs in Xenopus laevis
    • J.W. Collett, and R.E. Steele Identification and developmental expression of Src+ mRNAs in Xenopus laevis Dev. Biol. 152 1992 194 198
    • (1992) Dev. Biol. , vol.152 , pp. 194-198
    • Collett, J.W.1    Steele, R.E.2
  • 38
    • 1942471656 scopus 로고    scopus 로고
    • MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay
    • G. Stoecklin, T. Stubbs, N. Kedersha, S. Wax, W.F. Rigby, T.K. Blackwell, and P. Anderson MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay EMBO J. 23 2004 1313 1324
    • (2004) EMBO J. , vol.23 , pp. 1313-1324
    • Stoecklin, G.1    Stubbs, T.2    Kedersha, N.3    Wax, S.4    Rigby, W.F.5    Blackwell, T.K.6    Anderson, P.7
  • 39
    • 0033593448 scopus 로고    scopus 로고
    • Identification of TIAR as a protein binding to the translational regulatory AU-rich element of tumor necrosis factor alpha mRNA
    • C. Gueydan, L. Droogmans, P. Chalon, G. Huez, D. Caput, and V. Kruys Identification of TIAR as a protein binding to the translational regulatory AU-rich element of tumor necrosis factor alpha mRNA J. Biol. Chem. 274 1999 2322 2326
    • (1999) J. Biol. Chem. , vol.274 , pp. 2322-2326
    • Gueydan, C.1    Droogmans, L.2    Chalon, P.3    Huez, G.4    Caput, D.5    Kruys, V.6
  • 40
    • 0141815718 scopus 로고    scopus 로고
    • The proximal region of the 3′-untranslated region of cyclooxygenase-2 is recognized by a multimeric protein complex containing HuR, TIA-1, TIAR, and the heterogeneous nuclear ribonucleoprotein U
    • S.J. Cok, S.J. Acton, and A.R. Morrison The proximal region of the 3′-untranslated region of cyclooxygenase-2 is recognized by a multimeric protein complex containing HuR, TIA-1, TIAR, and the heterogeneous nuclear ribonucleoprotein U J. Biol. Chem. 278 2003 36157 36162
    • (2003) J. Biol. Chem. , vol.278 , pp. 36157-36162
    • Cok, S.J.1    Acton, S.J.2    Morrison, A.R.3
  • 41
    • 1242337338 scopus 로고    scopus 로고
    • Structural and functional dissection of a conserved destabilizing element of cyclo-oxygenase-2 mRNA: Evidence against the involvement of AUF-1 [AU-rich element/poly(U)-binding/degradation factor-1], AUF-2, tristetraprolin, HuR (Hu antigen R) or FBP1 (far-upstream-sequence-element-binding protein 1)
    • G. Sully, J.L. Dean, R. Wait, L. Rawlinson, T. Santalucia, J. Saklatvala, and A.R. Clark Structural and functional dissection of a conserved destabilizing element of cyclo-oxygenase-2 mRNA: evidence against the involvement of AUF-1 [AU-rich element/poly(U)-binding/degradation factor-1], AUF-2, tristetraprolin, HuR (Hu antigen R) or FBP1 (far-upstream-sequence- element-binding protein 1) Biochem. J. 377 2004 629 639
    • (2004) Biochem. J. , vol.377 , pp. 629-639
    • Sully, G.1    Dean, J.L.2    Wait, R.3    Rawlinson, L.4    Santalucia, T.5    Saklatvala, J.6    Clark, A.R.7
  • 43
    • 0033103805 scopus 로고    scopus 로고
    • Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU-rich elements: Implications for joint and gut-associated immunopathologies
    • D. Kontoyiannis, M. Pasparakis, T.T. Pizarro, F. Cominelli, and G. Kollias Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU-rich elements: implications for joint and gut-associated immunopathologies Immunity 10 1999 387 398
    • (1999) Immunity , vol.10 , pp. 387-398
    • Kontoyiannis, D.1    Pasparakis, M.2    Pizarro, T.T.3    Cominelli, F.4    Kollias, G.5
  • 44
    • 0034697027 scopus 로고    scopus 로고
    • Post-transcriptional control of cyclooxygenase-2 gene expression. the role of the 3′-untranslated region
    • D.A. Dixon, C.D. Kaplan, T.M. McIntyre, G.A. Zimmerman, and S.M. Prescott Post-transcriptional control of cyclooxygenase-2 gene expression. The role of the 3′-untranslated region J. Biol. Chem. 275 2000 11750 11757
    • (2000) J. Biol. Chem. , vol.275 , pp. 11750-11757
    • Dixon, D.A.1    Kaplan, C.D.2    McIntyre, T.M.3    Zimmerman, G.A.4    Prescott, S.M.5
  • 45
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin
    • E. Carballo, W.S. Lai, and P.J. Blackshear Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin Science 281 1998 1001 1005
    • (1998) Science , vol.281 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3


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