메뉴 건너뛰기




Volumn 38, Issue 22, 2010, Pages 8001-8014

Heterogeneous ribonucleoprotein C displays a repressor activity mediated by T-cell intracellular antigen-1-related/like protein to modulate Fas exon 6 splicing through a mechanism involving Hu antigen R

Author keywords

[No Author keywords available]

Indexed keywords

FAS ANTIGEN; FIBROBLAST GROWTH FACTOR RECEPTOR 2; GREEN FLUORESCENT PROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN C; HU ANTIGEN; HU ANTIGEN R; LEUCINE ZIPPER PROTEIN; RECOMBINANT PROTEIN; RED FLUORESCENT PROTEIN; T CELL INTRACELLULAR ANTIGEN 1 LIKE PROTEIN; T LYMPHOCYTE ANTIGEN; UNCLASSIFIED DRUG;

EID: 78650434686     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq698     Document Type: Article
Times cited : (40)

References (58)
  • 2
    • 56749098074 scopus 로고    scopus 로고
    • Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing
    • Pan, Q., Shai, O., Lee, L.J., Frey, B.J. and Blencowe, B.J. (2008) Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing. Nat. Genet., 40, 1413-1415.
    • (2008) Nat. Genet. , vol.40 , pp. 1413-1415
    • Pan, Q.1    Shai, O.2    Lee, L.J.3    Frey, B.J.4    Blencowe, B.J.5
  • 3
    • 75849145292 scopus 로고    scopus 로고
    • Expansion of the eukaryotic proteome by alternative splicing
    • Nilsen, T.W. and Graveley, B.R. (2010) Expansion of the eukaryotic proteome by alternative splicing. Nature, 463, 457-463.
    • (2010) Nature , vol.463 , pp. 457-463
    • Nilsen, T.W.1    Graveley, B.R.2
  • 4
    • 70350569286 scopus 로고    scopus 로고
    • Mechanisms of alternative splicing regulation: Insights from molecular and genomics approaches
    • Chen, M. and Manley, J.L. (2009) Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches. Nat. Rev. Mol. Cell Biol., 10, 741-754.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 741-754
    • Chen, M.1    Manley, J.L.2
  • 5
    • 60149093432 scopus 로고    scopus 로고
    • RNA and disease
    • Cooper, T.A., Wan, L. and Dreyfuss, G. (2009) RNA and disease. Cell, 136, 777-793.
    • (2009) Cell , vol.136 , pp. 777-793
    • Cooper, T.A.1    Wan, L.2    Dreyfuss, G.3
  • 6
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss, G., Kim, V.N. and Kataoka, N. (2002) Messenger-RNA-binding proteins and the messages they carry. Nat. Rev. Mol. Cell. Biol., 3, 195-205.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 7
    • 70350010120 scopus 로고    scopus 로고
    • Depletion of T-cell intracellular antigen proteins promotes cell proliferation
    • Reyes, R., Alcalde, J. and Izquierdo, J.M. (2009) Depletion of T-cell intracellular antigen proteins promotes cell proliferation. Genome Biol., 10, R87.
    • (2009) Genome Biol. , vol.10
    • Reyes, R.1    Alcalde, J.2    Izquierdo, J.M.3
  • 8
    • 0026091180 scopus 로고
    • A polyadenylate binding protein localized to the granules of cytolytic lymphocytes induces DNA fragmentation in target cells
    • Tian, Q., Streuli, M., Saito, H., Schlossman, S.F. and Anderson, P. (1991) A polyadenylate binding protein localized to the granules of cytolytic lymphocytes induces DNA fragmentation in target cells. Cell, 67, 629-639.
    • (1991) Cell , vol.67 , pp. 629-639
    • Tian, Q.1    Streuli, M.2    Saito, H.3    Schlossman, S.F.4    Anderson, P.5
  • 9
    • 0030027575 scopus 로고    scopus 로고
    • Individual RNA recognition motifs of TIA-1 and TIAR have different RNA binding specificities
    • Dember, L.M., Kim, N.D., Liu, K.Q. and Anderson, P. (1996) Individual RNA recognition motifs of TIA-1 and TIAR have different RNA binding specificities. J. Biol. Chem., 271, 2783-2788.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2783-2788
    • Dember, L.M.1    Kim, N.D.2    Liu, K.Q.3    Anderson, P.4
  • 13
  • 19
    • 35648933435 scopus 로고    scopus 로고
    • T-cell intracellular antigen-1 (TIA-1)-induced translational silencing promotes the decay of selected mRNAs
    • Yamasaki, S., Stoecklin, G., Kedersha, N., Simarro, M. and Anderson, P. (2007) T-cell intracellular antigen-1 (TIA-1)-induced translational silencing promotes the decay of selected mRNAs. J. Biol. Chem., 282, 30070-30077.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30070-30077
    • Yamasaki, S.1    Stoecklin, G.2    Kedersha, N.3    Simarro, M.4    Anderson, P.5
  • 20
    • 34547111077 scopus 로고    scopus 로고
    • Two isoforms of the T-cell intracellular antigen 1 (TIA-1) splicing factor display distinct splicing regulation activities. Control of TIA-1 isoform ratio by TIA-1-related protein
    • Izquierdo, J.M. and Valcarcel, J. (2007) Two isoforms of the T-cell intracellular antigen 1 (TIA-1) splicing factor display distinct splicing regulation activities. Control of TIA-1 isoform ratio by TIA-1-related protein. J. Biol. Chem., 282, 19410-19417.
    • (2007) J. Biol. Chem. , vol.282 , pp. 19410-19417
    • Izquierdo, J.M.1    Valcarcel, J.2
  • 21
    • 33847308702 scopus 로고    scopus 로고
    • Fas-activated serine/ threonine kinase (FAST K) synergizes with TIA-1/TIAR proteins to regulate Fas alternative splicing
    • Izquierdo, J.M. and Valcarcel, J. (2007) Fas-activated serine/ threonine kinase (FAST K) synergizes with TIA-1/TIAR proteins to regulate Fas alternative splicing. J. Biol. Chem., 282, 1539-1543.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1539-1543
    • Izquierdo, J.M.1    Valcarcel, J.2
  • 22
    • 49649128843 scopus 로고    scopus 로고
    • Hu antigen R (HuR) functions as an alternative pre-mRNA splicing regulator of Fas apoptosis-promoting receptor on exon definition
    • Izquierdo, J.M. (2008) Hu antigen R (HuR) functions as an alternative pre-mRNA splicing regulator of Fas apoptosis-promoting receptor on exon definition. J. Biol. Chem., 283, 19077-19084.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19077-19084
    • Izquierdo, J.M.1
  • 24
    • 54249164720 scopus 로고    scopus 로고
    • Fas splicing regulation during early apoptosis is linked to caspase-mediated cleavage of U2AF65
    • Izquierdo, J.M. (2008) Fas splicing regulation during early apoptosis is linked to caspase-mediated cleavage of U2AF65. Mol. Biol. Cell., 19, 3299-3307.
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 3299-3307
    • Izquierdo, J.M.1
  • 25
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Schevchenko, A., Wilm, M., Vorm, O. and Mann, M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem., 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Schevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 27
    • 34447559956 scopus 로고    scopus 로고
    • Downregulation of hnRNP C1/C2 by siRNA sensitizes HeLa cells to various stresses
    • Hossain, M.N., Fuji, M., Miki, K., Endoh, M. and Ayusawa, D. (2007) Downregulation of hnRNP C1/C2 by siRNA sensitizes HeLa cells to various stresses. Mol. Cell. Biochem., 296, 151-157.
    • (2007) Mol. Cell. Biochem. , vol.296 , pp. 151-157
    • Hossain, M.N.1    Fuji, M.2    Miki, K.3    Endoh, M.4    Ayusawa, D.5
  • 29
    • 33847352972 scopus 로고    scopus 로고
    • An essential function of the SRC-3 coactivator in suppression of cytokine mRNA translation and inflammatory response
    • Yu, C., York, B., Wang, S., Feng, Q., Xu, J. and O'Malley, B.W. (2007) An essential function of the SRC-3 coactivator in suppression of cytokine mRNA translation and inflammatory response. Mol. Cell, 25, 765-778.
    • (2007) Mol. Cell , vol.25 , pp. 765-778
    • Yu, C.1    York, B.2    Wang, S.3    Feng, Q.4    Xu, J.5    O'Malley, B.W.6
  • 30
    • 12644261402 scopus 로고    scopus 로고
    • RNA-dependent phosphorylation of a nuclear RNA binding protein
    • Fung, P.A., Labrecque, R. and Pederson, T. (1997) RNA-dependent phosphorylation of a nuclear RNA binding protein. Proc. Natl. Acad. Sci., 94, 1064-1068.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 1064-1068
    • Fung, P.A.1    Labrecque, R.2    Pederson, T.3
  • 31
    • 0027992089 scopus 로고
    • The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins
    • Gorlach, M., Burd, C. and Dreyfuss, G. (1994) The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins. J. Biol. Chem., 269, 23074-23078.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23074-23078
    • Gorlach, M.1    Burd, C.2    Dreyfuss, G.3
  • 32
    • 0029862801 scopus 로고    scopus 로고
    • A major determinant of hnRNP C protein binding to RNA is a novel bZIP-like RNA binding domain
    • McAfee, J., Shahied-Milam, L., Soltaninassab, S. and LeStourgeon, W. (1996) A major determinant of hnRNP C protein binding to RNA is a novel bZIP-like RNA binding domain. RNA, 2, 1139-1152.
    • (1996) RNA , vol.2 , pp. 1139-1152
    • McAfee, J.1    Shahied-Milam, L.2    Soltaninassab, S.3    Lestourgeon, W.4
  • 33
    • 0037125231 scopus 로고    scopus 로고
    • Interaction of hnRNP-C1/C2 proteins with RNA: Analysis using the yeast three-hybrid system
    • Koloteva-Levine, N., Amichay, M. and Elroy-Stein, O. (2002) Interaction of hnRNP-C1/C2 proteins with RNA: analysis using the yeast three-hybrid system. FEBS Lett., 523, 73-78.
    • (2002) FEBS Lett. , vol.523 , pp. 73-78
    • Koloteva-Levine, N.1    Amichay, M.2    Elroy-Stein, O.3
  • 34
    • 0029797247 scopus 로고    scopus 로고
    • The hnRNP C proteins contain a nuclear retention sequence that can override nuclear export signals
    • Nakielny, S. and Dreyfuss, G. (1996) The hnRNP C proteins contain a nuclear retention sequence that can override nuclear export signals. J. Cell Biol., 134, 1365-1373.
    • (1996) J. Cell Biol. , vol.134 , pp. 1365-1373
    • Nakielny, S.1    Dreyfuss, G.2
  • 35
    • 76849085628 scopus 로고    scopus 로고
    • Extensive association of HuR with hnRNP proteins within immunoselected hnRNP and mRNP complexes
    • Papadopoulou, C., Patrinou-Georgoula, M. and Guialis, A. (2010) Extensive association of HuR with hnRNP proteins within immunoselected hnRNP and mRNP complexes. Biochim. Biophys. Acta, 1804, 692-703.
    • (2010) Biochim. Biophys. Acta , pp. 692-703
    • Papadopoulou, C.1    Patrinou-Georgoula, M.2    Guialis, A.3
  • 36
    • 34250363024 scopus 로고    scopus 로고
    • SR proteins function in coupling RNAP II transcription to pre-mRNA splicing
    • Das, R., Yu, J., Zhang, Z., Gygi, M.P., Krainer, A.R., Gygi, S.P. and Reed, R. (2007) SR proteins function in coupling RNAP II transcription to pre-mRNA splicing. Mol. Cell, 26, 867-881.
    • (2007) Mol. Cell , vol.26 , pp. 867-881
    • Das, R.1    Yu, J.2    Zhang, Z.3    Gygi, M.P.4    Krainer, A.R.5    Gygi, S.P.6    Reed, R.7
  • 37
    • 32344437827 scopus 로고    scopus 로고
    • Novel modes of splicing repression by PTB
    • Spellman, R. and Smith, C.W. (2006) Novel modes of splicing repression by PTB. Trends Biochem. Sci., 31, 73-76.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 73-76
    • Spellman, R.1    Smith, C.W.2
  • 40
    • 75149150660 scopus 로고    scopus 로고
    • HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer
    • David, C.J., Chen, M., Assanah, M., Canoll, P. and Manley, J.L. (2010) HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer. Nature, 463, 364-368.
    • (2010) Nature , vol.463 , pp. 364-368
    • David, C.J.1    Chen, M.2    Assanah, M.3    Canoll, P.4    Manley, J.L.5
  • 41
    • 76649102764 scopus 로고    scopus 로고
    • The alternative splicing repressors hnRNP A1/A2 and PTB influence pyruvate kinase isoform expression and cell metabolism
    • Clower, C.V., Chatterjee, D., Wang, Z., Cantley, L.C., Vander Heiden, M.G. and Krainer, A.R. (2010) The alternative splicing repressors hnRNP A1/A2 and PTB influence pyruvate kinase isoform expression and cell metabolism. Proc. Natl. Acad. Sci., 107, 1894-1899.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 1894-1899
    • Clower, C.V.1    Chatterjee, D.2    Wang, Z.3    Cantley, L.C.4    Vander Heiden, M.G.5    Krainer, A.R.6
  • 42
    • 38949098620 scopus 로고    scopus 로고
    • Regulation of neuron-specific alternative splicing of neurofibromatosis type 1 pre-mRNA
    • Zhu, H., Hinman, M.N., Hasman, R.A., Mehta, P. and Lou, H. (2008) Regulation of neuron-specific alternative splicing of neurofibromatosis type 1 pre-mRNA. Mol. Cell. Biol., 28, 1240-1251.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1240-1251
    • Zhu, H.1    Hinman, M.N.2    Hasman, R.A.3    Mehta, P.4    Lou, H.5
  • 43
    • 0027275553 scopus 로고
    • Cell cycle-regulated phosphorylation of the pre-mRNA-binding (heterogeneous nuclear ribonucleoprotein) C proteins
    • Pinol-Roma, S. and Dreyfuss, G. (1993) Cell cycle-regulated phosphorylation of the pre-mRNA-binding (heterogeneous nuclear ribonucleoprotein) C proteins. Mol. Cell. Biol., 13, 5762-5770.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5762-5770
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 44
    • 0037432070 scopus 로고    scopus 로고
    • Basal and hydrogen peroxide stimulated sites of phosphorylation in heterogeneous nuclear ribonucleoprotein C1/C2
    • Stone, J.R., Maki, J.L. and Collins, T. (2003) Basal and hydrogen peroxide stimulated sites of phosphorylation in heterogeneous nuclear ribonucleoprotein C1/C2. Biochemistry, 42, 1301-1308.
    • (2003) Biochemistry , vol.42 , pp. 1301-1308
    • Stone, J.R.1    Maki, J.L.2    Collins, T.3
  • 45
    • 17644379405 scopus 로고    scopus 로고
    • Protein kinase CK1alpha regulates mRNA binding by heterogeneous nuclear ribonucleoprotein C in response to physiologic levels of hydrogen peroxide
    • Kattapuram, T., Yang, S., Maki, J.L. and Stone, J.R. (2005) Protein kinase CK1alpha regulates mRNA binding by heterogeneous nuclear ribonucleoprotein C in response to physiologic levels of hydrogen peroxide. J. Biol. Chem., 280, 15340-15347.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15340-15347
    • Kattapuram, T.1    Yang, S.2    Maki, J.L.3    Stone, J.R.4
  • 48
    • 69949132191 scopus 로고    scopus 로고
    • Chromatin organization marks exon-intron structure
    • Schwartz, S., Meshorer, E. and Ast, G. (2009) Chromatin organization marks exon-intron structure. Nat. Struct. Mol. Biol., 16, 990-996.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 990-996
    • Schwartz, S.1    Meshorer, E.2    Ast, G.3
  • 51
    • 27244449015 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF form a chromatin remodeling complex at the beta-globin locus control region
    • Mahajan, M.C., Narlikar, G.J., Boyapaty, G., Kingston, R.E. and Weissman, S.M. (2005) Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF form a chromatin remodeling complex at the beta-globin locus control region. Proc. Natl Acad. Sci., 102, 15012-15017.
    • (2005) Proc. Natl Acad. Sci. , vol.102 , pp. 15012-15017
    • Mahajan, M.C.1    Narlikar, G.J.2    Boyapaty, G.3    Kingston, R.E.4    Weissman, S.M.5
  • 52
    • 30044441988 scopus 로고    scopus 로고
    • The human SWI/ SNF subunit Brm is a regulator of alternative splicing
    • Batsche, E., Yaniv, M. and Muchardt, C. (2006) The human SWI/ SNF subunit Brm is a regulator of alternative splicing. Nat. Struct. Mol. Biol., 13, 22-29.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 22-29
    • Batsche, E.1    Yaniv, M.2    Muchardt, C.3
  • 53
    • 33748351186 scopus 로고    scopus 로고
    • Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells
    • Listerman, I., Sapra, A.K. and Neugebauer, K.M. (2006) Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells. Nat. Struct. Mol. Biol., 13, 815-822.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 815-822
    • Listerman, I.1    Sapra, A.K.2    Neugebauer, K.M.3
  • 56
    • 53149145051 scopus 로고    scopus 로고
    • RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition
    • Bonnal, S., Martnez, C., Forch, P., Bachi, A., Wilm, M. and Valcarcel, J. (2008) RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition. Mol. Cell, 32, 81-95.
    • (2008) Mol. Cell , vol.32 , pp. 81-95
    • Bonnal, S.1    Martnez, C.2    Forch, P.3    Bachi, A.4    Wilm, M.5    Valcarcel, J.6
  • 57
    • 26944489645 scopus 로고    scopus 로고
    • Building specificity with nonspecific RNA-binding proteins
    • Singh, R. and Valcarcel, J. (2005) Building specificity with nonspecific RNA-binding proteins. Nat. Struct. Mol. Biol., 12, 645-653.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 645-653
    • Singh, R.1    Valcarcel, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.