메뉴 건너뛰기




Volumn 250, Issue 2, 1999, Pages 439-451

Characterization of the 2A7 antigen as a 85-kDa human nucleocytoplasmic shuttling protein

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; DEOXYRIBONUCLEASE; MONOCLONAL ANTIBODY; RIBONUCLEASE; RNA;

EID: 0033179062     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4523     Document Type: Article
Times cited : (2)

References (58)
  • 1
    • 0021717131 scopus 로고
    • Movement of a karyophilic protein through the nuclear pores of oocytes
    • Feldherr C. M., Kallenbach E., Shultz N. Movement of a karyophilic protein through the nuclear pores of oocytes. J. Cell Biol. 99:1984;2216-2222.
    • (1984) J. Cell Biol. , vol.99 , pp. 2216-2222
    • Feldherr, C.M.1    Kallenbach, E.2    Shultz, N.3
  • 2
    • 0026909329 scopus 로고
    • Molecular trafficking across the nuclear pore complex
    • Gerace L. Molecular trafficking across the nuclear pore complex. Curr. Opin. Cell Biol. 4:1992;637-645.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 637-645
    • Gerace, L.1
  • 3
    • 0024999077 scopus 로고
    • An essential signalling role for the m3G cap in the transport of U1 snRNP to the nucleus
    • Fischer U., Lührmann R. An essential signalling role for the m3G cap in the transport of U1 snRNP to the nucleus. Science. 249:1990;786-790.
    • (1990) Science , vol.249 , pp. 786-790
    • Fischer, U.1    Lührmann, R.2
  • 4
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - A consensus
    • Dingwall C., Laskey R. A. Nuclear targeting sequences - A consensus. Trends Biochem. Sci. 16:1991;478-481.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 7
    • 0028559537 scopus 로고
    • Cytosolic factors in nuclear transport: What's importin
    • Powers M. A., Forbes D. J. Cytosolic factors in nuclear transport: What's importin. Cell. 79:1994;931-934.
    • (1994) Cell , vol.79 , pp. 931-934
    • Powers, M.A.1    Forbes, D.J.2
  • 9
    • 0029984570 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic transport
    • Görlich D., Mattaj I. W. Nucleo-cytoplasmic transport. Science. 271:1996;1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Görlich, D.1    Mattaj, I.W.2
  • 10
    • 0025110034 scopus 로고
    • Cytoplasmic transport of ribosomal subunits microinjected into the Xenopus laevis oocyte nucleus: A generalized, facilitated process
    • Bataillé N., Helser T., Fried H. M. Cytoplasmic transport of ribosomal subunits microinjected into the Xenopus laevis oocyte nucleus: A generalized, facilitated process. J. Cell Biol. 111:1990;1571-1582.
    • (1990) J. Cell Biol. , vol.111 , pp. 1571-1582
    • Bataillé, N.1    Helser, T.2    Fried, H.M.3
  • 11
    • 0026636221 scopus 로고
    • Export of mRNA from microinjected nuclei of Xenopus laevis oocytes
    • Dargemont C., Kühn L. C. Export of mRNA from microinjected nuclei of Xenopus laevis oocytes. J. Cell Biol. 118:1992;1-9.
    • (1992) J. Cell Biol. , vol.118 , pp. 1-9
    • Dargemont, C.1    Kühn, L.C.2
  • 12
    • 0024966024 scopus 로고
    • Major nucleolar proteins shuttle between nucleus and cytoplasm
    • Borer R. A., Lehner C. F., Eppenberger H. M., Nigg E. A. Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell. 56:1989;379-390.
    • (1989) Cell , vol.56 , pp. 379-390
    • Borer, R.A.1    Lehner, C.F.2    Eppenberger, H.M.3    Nigg, E.A.4
  • 13
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Piñol-Roma S., Dreyfuss G. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature. 355:1992;730-732.
    • (1992) Nature , vol.355 , pp. 730-732
    • Piñol-Roma, S.1    Dreyfuss, G.2
  • 14
    • 0027411587 scopus 로고
    • HnRNP proteins: Localization and transport between the nucleus and the cytoplasm
    • Piñol-Roma S., Dreyfuss G. hnRNP proteins: Localization and transport between the nucleus and the cytoplasm. Trends Cell Biol. 3:1993;151-155.
    • (1993) Trends Cell Biol. , vol.3 , pp. 151-155
    • Piñol-Roma, S.1    Dreyfuss, G.2
  • 15
    • 0027164642 scopus 로고
    • Nuclear export of proteins: The role of nuclear retention
    • Schmidt-Zachmann M. S., Dargemont C., Kühn L. C., Nigg E. A. Nuclear export of proteins: The role of nuclear retention. Cell. 74:1993;493-504.
    • (1993) Cell , vol.74 , pp. 493-504
    • Schmidt-Zachmann, M.S.1    Dargemont, C.2    Kühn, L.C.3    Nigg, E.A.4
  • 16
    • 0023369370 scopus 로고
    • A constitutive nucleolar protein identified as a member of the nucleoplasmin family
    • Schmidt-Zachmann M. S., Hügle-Dorr B., Franke W. W. A constitutive nucleolar protein identified as a member of the nucleoplasmin family. EMBO J. 6:1987;1881-1890.
    • (1987) EMBO J. , vol.6 , pp. 1881-1890
    • Schmidt-Zachmann, M.S.1    Hügle-Dorr, B.2    Franke, W.W.3
  • 17
    • 0029128923 scopus 로고
    • Characterization of the 2H12 antigen as a nonshuttling human isoelectric variant of the nucleolar protein B23
    • Paulin-Levasseur M., Julien M., Horner M., Chen G. Characterization of the 2H12 antigen as a nonshuttling human isoelectric variant of the nucleolar protein B23. Exp. Cell Res. 219:1995;514-526.
    • (1995) Exp. Cell Res. , vol.219 , pp. 514-526
    • Paulin-Levasseur, M.1    Julien, M.2    Horner, M.3    Chen, G.4
  • 18
    • 0023937192 scopus 로고
    • The function of the nuclear envelope in nuclear protein accumulation
    • Zimmer F. J., Dreyer C., Hausen P. The function of the nuclear envelope in nuclear protein accumulation. J. Cell Biol. 106:1988;1435-1444.
    • (1988) J. Cell Biol. , vol.106 , pp. 1435-1444
    • Zimmer, F.J.1    Dreyer, C.2    Hausen, P.3
  • 19
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer U., Huber J., Boelens W. C., Mattaj I. W., Lührmann R. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell. 82:1995;475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Lührmann, R.5
  • 21
    • 0028845313 scopus 로고
    • A nuclear export signal in hnRNP A1: A signal-mediated, temperature dependent nuclear protein export pathway
    • Michael W. M., Choi M., Dreyfuss G. A nuclear export signal in hnRNP A1: A signal-mediated, temperature dependent nuclear protein export pathway. Cell. 83:1995;415-422.
    • (1995) Cell , vol.83 , pp. 415-422
    • Michael, W.M.1    Choi, M.2    Dreyfuss, G.3
  • 22
    • 0028963968 scopus 로고
    • Nucleo-cytoplasmic distribution of human hnRNP proteins: Search for the targeting domains in hnRNP A1
    • Weighardt F., Biamonti G., Riva S. Nucleo-cytoplasmic distribution of human hnRNP proteins: Search for the targeting domains in hnRNP A1. J. Cell Sci. 108:1995;545-555.
    • (1995) J. Cell Sci. , vol.108 , pp. 545-555
    • Weighardt, F.1    Biamonti, G.2    Riva, S.3
  • 23
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen W., Meinboth J. L., Tsien R. Y., Taylor S. S. Identification of a signal for rapid export of proteins from the nucleus. Cell. 82:1995;463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinboth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 24
    • 0029894726 scopus 로고    scopus 로고
    • Protein sequence requirements for function of the human T-cell leukemia virus type Rex nuclear export signal delineated by a novel in vivo randomization-selection assay
    • Bogerd H. P., Fridell R. E., Benson R. E., Hua J., Cullen B. R. Protein sequence requirements for function of the human T-cell leukemia virus type Rex nuclear export signal delineated by a novel in vivo randomization-selection assay. Mol. Cell. Biol. 16:1996;4207-4214.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4207-4214
    • Bogerd, H.P.1    Fridell, R.E.2    Benson, R.E.3    Hua, J.4    Cullen, B.R.5
  • 26
    • 0029121296 scopus 로고
    • Nuclear export signals and the fast track to the cytoplasm
    • Gerace L. Nuclear export signals and the fast track to the cytoplasm. Cell. 82:1995;341-344.
    • (1995) Cell , vol.82 , pp. 341-344
    • Gerace, L.1
  • 27
    • 0022976650 scopus 로고
    • Cellular and biochemical events in mammalian cells during and after recovery from physiological stress
    • Welch W. J., Suhan J. P. Cellular and biochemical events in mammalian cells during and after recovery from physiological stress. J. Cell Biol. 103:1986;2035-2052.
    • (1986) J. Cell Biol. , vol.103 , pp. 2035-2052
    • Welch, W.J.1    Suhan, J.P.2
  • 28
    • 0024102365 scopus 로고
    • Lack of lamins A and C in mammalian hemopoietic cell lines devoid of intermediate filament proteins
    • Paulin-Levasseur M., Scherbarth A., Traub U., Traub P. Lack of lamins A and C in mammalian hemopoietic cell lines devoid of intermediate filament proteins. Eur. J. Cell Biol. 47:1988;121-131.
    • (1988) Eur. J. Cell Biol. , vol.47 , pp. 121-131
    • Paulin-Levasseur, M.1    Scherbarth, A.2    Traub, U.3    Traub, P.4
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell P. Z., Goodman H. M., O'Farrell P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell. 12:1977;1133-1142.
    • (1977) Cell , vol.12 , pp. 1133-1142
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 32
    • 0020335268 scopus 로고
    • Gene expression in Acetabularia. 1. Calibration of wheat germ cell-free translation system proteins as internal references for two-dimensional electrophoresis
    • Shoeman R. L., Schweiger H. G. Gene expression in Acetabularia. 1. Calibration of wheat germ cell-free translation system proteins as internal references for two-dimensional electrophoresis. J. Cell Sci. 58:1982;23-33.
    • (1982) J. Cell Sci. , vol.58 , pp. 23-33
    • Shoeman, R.L.1    Schweiger, H.G.2
  • 33
    • 0020394235 scopus 로고
    • A new method for partial peptide mapping using N-chlorosuccinimide/urea and peptide silver staining in sodium dodecyl sulfate-polyacrylamide gels
    • Lischwe M. A., Ochs D. A new method for partial peptide mapping using N-chlorosuccinimide/urea and peptide silver staining in sodium dodecyl sulfate-polyacrylamide gels. Anal. Biochem. 127:1982;453-457.
    • (1982) Anal. Biochem. , vol.127 , pp. 453-457
    • Lischwe, M.A.1    Ochs, D.2
  • 34
    • 0022254614 scopus 로고
    • Localization of nuclear antigens during preparation of nuclear matrices in situ
    • Chaly N., Little J. E., Brown D. L. Localization of nuclear antigens during preparation of nuclear matrices in situ. Can. J. Biochem. Cell Biol. 63:1985;644-653.
    • (1985) Can. J. Biochem. Cell Biol. , vol.63 , pp. 644-653
    • Chaly, N.1    Little, J.E.2    Brown, D.L.3
  • 36
    • 0026339487 scopus 로고
    • Transcription-dependent and transcription-independent nuclear transport of hnRNP proteins
    • Piñol-Roma S., Dreyfuss G. Transcription-dependent and transcription-independent nuclear transport of hnRNP proteins. Science. 253:1991;312-314.
    • (1991) Science , vol.253 , pp. 312-314
    • Piñol-Roma, S.1    Dreyfuss, G.2
  • 37
    • 0023609206 scopus 로고
    • Heat shock-induced changes in the structural stability of proteinaceous karyoskeletal elements in vitro and morphological effects in situ
    • McConnell M., Whalen A. M., Smith D. E., Fisher P. A. Heat shock-induced changes in the structural stability of proteinaceous karyoskeletal elements in vitro and morphological effects in situ. J. Cell Biol. 105:1987;1087-1098.
    • (1987) J. Cell Biol. , vol.105 , pp. 1087-1098
    • McConnell, M.1    Whalen, A.M.2    Smith, D.E.3    Fisher, P.A.4
  • 38
    • 0027157984 scopus 로고
    • 1 mammalian cells following heat shock: Resinless section electron microscopy, biochemical, and immunofluorescence studies
    • 1 mammalian cells following heat shock: Resinless section electron microscopy, biochemical, and immunofluorescence studies. J. Cell. Physiol. 155:1993;615-634.
    • (1993) J. Cell. Physiol. , vol.155 , pp. 615-634
    • Wachsberger, P.R.1    Coss, R.A.2
  • 39
    • 0022531458 scopus 로고
    • RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis
    • Yost H. J., Lindquist S. RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis. Cell. 45:1986;185-193.
    • (1986) Cell , vol.45 , pp. 185-193
    • Yost, H.J.1    Lindquist, S.2
  • 40
    • 0023650891 scopus 로고
    • Expression of intron-containing C. elegans heat shock genes in mouse cells demonstrates divergence of 3′ splice recognition sequences between nematodes and vertebrates, and an inhibitory effect of heat shock on the mammalian splicing apparatus
    • Kay R. J., Russnak R. H., Jones D., Mathias C., Candido E. P. M. Expression of intron-containing C. elegans heat shock genes in mouse cells demonstrates divergence of 3′ splice recognition sequences between nematodes and vertebrates, and an inhibitory effect of heat shock on the mammalian splicing apparatus. Nucleic Acids Res. 15:1987;3723-3741.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 3723-3741
    • Kay, R.J.1    Russnak, R.H.2    Jones, D.3    Mathias, C.4    Candido, E.P.M.5
  • 41
    • 0024114933 scopus 로고
    • Heat shock but not other stress inducers leads to the disruption of a sub-set of snRNPs and inhibition of in vitro splicing in HeLa cells
    • Bond U. Heat shock but not other stress inducers leads to the disruption of a sub-set of snRNPs and inhibition of in vitro splicing in HeLa cells. EMBO J. 7:1988;3509-3518.
    • (1988) EMBO J. , vol.7 , pp. 3509-3518
    • Bond, U.1
  • 44
    • 0031053676 scopus 로고    scopus 로고
    • Identification of human common nuclear-matrix proteins as heterogeneous nuclear ribonucleoprotein-H and ribonucleoprotein-H′ by sequencing and mass spectroscopy
    • Holzmann K., Korosec T., Gerner C., Grim R., Sauermann G. Identification of human common nuclear-matrix proteins as heterogeneous nuclear ribonucleoprotein-H and ribonucleoprotein-H′ by sequencing and mass spectroscopy. Eur. J. Biochem. 244:1997;479-486.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 479-486
    • Holzmann, K.1    Korosec, T.2    Gerner, C.3    Grim, R.4    Sauermann, G.5
  • 45
    • 0022521416 scopus 로고
    • The nonchromatin substructure of the nucleus: The ribonucleoprotein (RNP)-containing and RNP-depleted matrices analyzed by sequential fractionating and resineless section electron microscopy
    • Fey E. G., Krochmalinik G., Penman S. The nonchromatin substructure of the nucleus: The ribonucleoprotein (RNP)-containing and RNP-depleted matrices analyzed by sequential fractionating and resineless section electron microscopy. J. Cell Biol. 102:1986;1654-1665.
    • (1986) J. Cell Biol. , vol.102 , pp. 1654-1665
    • Fey, E.G.1    Krochmalinik, G.2    Penman, S.3
  • 46
    • 0022555399 scopus 로고
    • Protein composition of nuclear matrix preparations from HeLa cells: An immunochemical approach
    • Verheijen R., Kuijpers H., Vooijs P., van Venrooij W., Ramaekers F. Protein composition of nuclear matrix preparations from HeLa cells: An immunochemical approach. J. Cell Sci. 80:1986;103-122.
    • (1986) J. Cell Sci. , vol.80 , pp. 103-122
    • Verheijen, R.1    Kuijpers, H.2    Vooijs, P.3    Van Venrooij, W.4    Ramaekers, F.5
  • 48
    • 0023522645 scopus 로고
    • Changes in heterogeneous nuclear RNP core polypeptide complements during the cell cycle
    • Leser G. P., Martin T. E. Changes in heterogeneous nuclear RNP core polypeptide complements during the cell cycle. J. Cell Biol. 105:1987;2083-2094.
    • (1987) J. Cell Biol. , vol.105 , pp. 2083-2094
    • Leser, G.P.1    Martin, T.E.2
  • 49
    • 0024465162 scopus 로고
    • Rapid effect of heat shock on two heterogeneous nuclear ribonucleoprotein-associated antigens in HeLa cells
    • Mähl P., Lutz Y., Puvion E., Fuchs J.-P. Rapid effect of heat shock on two heterogeneous nuclear ribonucleoprotein-associated antigens in HeLa cells. J. Cell Biol. 109:1989;1921-1935.
    • (1989) J. Cell Biol. , vol.109 , pp. 1921-1935
    • Mähl, P.1    Lutz, Y.2    Puvion, E.3    Fuchs, J.-P.4
  • 50
    • 0029934811 scopus 로고    scopus 로고
    • The human hnRNP-M proteins: Structure and relation with early heat shock-induced splicing arrest and chromosome mapping
    • Gattoni R., Mahé D., Mahl P., Fischer N., Mattei M.-G., Stévenin J., Fuchs J.-P. The human hnRNP-M proteins: Structure and relation with early heat shock-induced splicing arrest and chromosome mapping. Nucleic Acids Res. 24:1996;2535-2542.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2535-2542
    • Gattoni, R.1    Mahé, D.2    Mahl, P.3    Fischer, N.4    Mattei, M.-G.5    Stévenin, J.6    Fuchs, J.-P.7
  • 51
    • 0025786160 scopus 로고
    • Discrete nuclear domains of poly (A) RNA and their relationship to the functional organization of the nucleus
    • Carter K. C., Taneja K. L., Lawrence J. B. Discrete nuclear domains of poly (A) RNA and their relationship to the functional organization of the nucleus. J. Cell Biol. 115:1991;1191-1202.
    • (1991) J. Cell Biol. , vol.115 , pp. 1191-1202
    • Carter, K.C.1    Taneja, K.L.2    Lawrence, J.B.3
  • 52
    • 0026660025 scopus 로고
    • HnRNP1, the polypyrimidine tract-binding protein: Distinct nuclear localization and association with hnRNAs
    • Ghetti A., Piñol-Roma S., Michael W. M., Morandi C., Dreyfuss G. hnRNP1, the polypyrimidine tract-binding protein: Distinct nuclear localization and association with hnRNAs. Nucleic Acids Res. 20:1992;3671-3678.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3671-3678
    • Ghetti, A.1    Piñol-Roma, S.2    Michael, W.M.3    Morandi, C.4    Dreyfuss, G.5
  • 53
    • 0027256020 scopus 로고
    • Nucleolar localization of myc transcripts
    • Bond V. C., Wold B. Nucleolar localization of myc transcripts. Mol. Cell. Biol. 13:1993;3221-3230.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3221-3230
    • Bond, V.C.1    Wold, B.2
  • 54
    • 0029042024 scopus 로고
    • MRNA transport in yeast: Time to reinvestigate the functions of the nucleolus
    • Schneiter R., Kadowaki T., Tartakoff A. M. mRNA transport in yeast: Time to reinvestigate the functions of the nucleolus. Mol. Biol. Cell. 6:1995;357-370.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 357-370
    • Schneiter, R.1    Kadowaki, T.2    Tartakoff, A.M.3
  • 55
    • 0030064309 scopus 로고    scopus 로고
    • + RNA in heat-shocked yeast cells: Implication of nucleolar involvement in mRNA transport
    • + RNA in heat-shocked yeast cells: Implication of nucleolar involvement in mRNA transport. Mol. Biol. Cell. 7:1996;173-192.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 173-192
    • Tani, T.1    Derby, R.J.2    Hiraoka, Y.3    Spector, D.L.4
  • 56
    • 0024498788 scopus 로고
    • Highly localized tracks of specific transcripts within interphase nuclei visualized by in situ hybridization
    • Lawrence J. B., Singer R. H., Marselle L. M. Highly localized tracks of specific transcripts within interphase nuclei visualized by in situ hybridization. Cell. 57:1989;493-502.
    • (1989) Cell , vol.57 , pp. 493-502
    • Lawrence, J.B.1    Singer, R.H.2    Marselle, L.M.3
  • 57
    • 0025719396 scopus 로고
    • Nascent pre-mRNA transcripts are associated with nuclear regions enriched in splicing factors
    • Huang S., Spector D. L. Nascent pre-mRNA transcripts are associated with nuclear regions enriched in splicing factors. Genes Dev. 5:1991;2288-2302.
    • (1991) Genes Dev. , vol.5 , pp. 2288-2302
    • Huang, S.1    Spector, D.L.2
  • 58
    • 0026773097 scopus 로고
    • Nopp140 shuttles on tracks between nucleolus and cytoplasm
    • Meier U. T., Blobel G. Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell. 70:1992;127-138.
    • (1992) Cell , vol.70 , pp. 127-138
    • Meier, U.T.1    Blobel, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.