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Volumn 5, Issue 8, 1996, Pages 1083-1091

The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN;

EID: 0029816723     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/5.8.1083     Document Type: Article
Times cited : (336)

References (53)
  • 1
    • 0028904864 scopus 로고
    • Triplet repeat expansion mutations: The example of fragile X syndrome
    • Warren, S.T. and Ashley, C.T. (1995) Triplet repeat expansion mutations: the example of fragile X syndrome. Annu. Rev. Neurosci. 18, 77-99.
    • (1995) Annu. Rev. Neurosci. , vol.18 , pp. 77-99
    • Warren, S.T.1    Ashley, C.T.2
  • 2
    • 84942947953 scopus 로고
    • Advances in molecular analysis of fragile X syndrome
    • Warren, S.T. and Nelson, D.L. (1994) Advances in molecular analysis of fragile X syndrome. JAMA 271, 536-542.
    • (1994) JAMA , vol.271 , pp. 536-542
    • Warren, S.T.1    Nelson, D.L.2
  • 3
    • 0027377155 scopus 로고
    • High resolution methylation analysis of the FMR1 gene trinucleotide repeat region in fragile X syndrome
    • Hornstra, I.K., Nelson, D.L., Warren, S.T. and Yang, T.P. (1993) High resolution methylation analysis of the FMR1 gene trinucleotide repeat region in fragile X syndrome. Hum. Mol. Genet. 2, 1659-1665.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 1659-1665
    • Hornstra, I.K.1    Nelson, D.L.2    Warren, S.T.3    Yang, T.P.4
  • 8
    • 0029123145 scopus 로고
    • Intragenic loss of function mutations demonstrate the primary role of FMR1 in fragile X syndrome
    • Lugenbeel, K.A., Peier, A.M., Carson, N.L., Chudley, A.E. and Nelson, D.L. (1995) Intragenic loss of function mutations demonstrate the primary role of FMR1 in fragile X syndrome. Nature Genet. 10, 483-485.
    • (1995) Nature Genet. , vol.10 , pp. 483-485
    • Lugenbeel, K.A.1    Peier, A.M.2    Carson, N.L.3    Chudley, A.E.4    Nelson, D.L.5
  • 11
    • 0030023275 scopus 로고    scopus 로고
    • The chicken FMR1 gene is highly conserved with a CCT 5′ untranslated repeat and encodes an RNA-binding protein
    • Price, D.K., Zhang, F., Ashley, C.T. and Warren, S.T. (1996) The chicken FMR1 gene is highly conserved with a CCT 5′ untranslated repeat and encodes an RNA-binding protein. Genomics 31, 3-12.
    • (1996) Genomics , vol.31 , pp. 3-12
    • Price, D.K.1    Zhang, F.2    Ashley, C.T.3    Warren, S.T.4
  • 14
    • 0027377580 scopus 로고
    • FMR1 protein: Conserved RNP family domains and selective RNA binding
    • Ashley, C.T., Wilkinson, K.D., Reines, D. and Warren, S.T. (1993) FMR1 protein: conserved RNP family domains and selective RNA binding. Science 262, 563-566.
    • (1993) Science , vol.262 , pp. 563-566
    • Ashley, C.T.1    Wilkinson, K.D.2    Reines, D.3    Warren, S.T.4
  • 15
    • 0027327486 scopus 로고
    • The protein product of the fragile X gene, FMR1, has characteristics of an RNA binding protein
    • Siomi, H., Siomi, M.C., Nussbaum, R.L. and Dreyfuss, G. (1993) The protein product of the fragile X gene, FMR1, has characteristics of an RNA binding protein. Cell 74, 291-298.
    • (1993) Cell , vol.74 , pp. 291-298
    • Siomi, H.1    Siomi, M.C.2    Nussbaum, R.L.3    Dreyfuss, G.4
  • 18
    • 0028236525 scopus 로고
    • Essential role for KH domains in RNA binding: Impaired RNA binding by a mutation in the KH domain of FMRI that causes fragile X syndrome
    • Siomi, H., Choi, M., Siomi, M.C., Nussbaum, R.L. and Dreyfuss, G. (1994) Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMRI that causes fragile X syndrome. Cell 77, 33-39.
    • (1994) Cell , vol.77 , pp. 33-39
    • Siomi, H.1    Choi, M.2    Siomi, M.C.3    Nussbaum, R.L.4    Dreyfuss, G.5
  • 22
    • 0027397928 scopus 로고
    • Tissue specific expression of FMR1 provides evidence for a functional role in fragile X syndrome
    • Hinds, H.L., Ashley, C.T., Nelson, D.L., Warren, S.T., Housman, D.E. and Schalling, M. (1993) Tissue specific expression of FMR1 provides evidence for a functional role in fragile X syndrome. Nature Genet. 3, 36-43.
    • (1993) Nature Genet. , vol.3 , pp. 36-43
    • Hinds, H.L.1    Ashley, C.T.2    Nelson, D.L.3    Warren, S.T.4    Housman, D.E.5    Schalling, M.6
  • 23
    • 0027300283 scopus 로고
    • Nucleus basalis magnocellularis and hippocampus are the major sites of FMR-1 expression in the human fetal brain
    • Abitbol, M., Menini, C., Delezoide, A.-L., Rhyner, T., Vekemans, M. and Mallet, J. (1993) Nucleus basalis magnocellularis and hippocampus are the major sites of FMR-1 expression in the human fetal brain. Nature Genet. 4, 147-152.
    • (1993) Nature Genet. , vol.4 , pp. 147-152
    • Abitbol, M.1    Menini, C.2    Delezoide, A.-L.3    Rhyner, T.4    Vekemans, M.5    Mallet, J.6
  • 26
    • 0027176361 scopus 로고
    • The FMR-1 protein is cytoplasmic, most abundant in neurons, and appears normal in carriers of the fragile X premutation
    • Devys, D., Lutz, Y., Rouyer, N., Bellocq, J.-P. and Mandel, J-L. (1993) The FMR-1 protein is cytoplasmic, most abundant in neurons, and appears normal in carriers of the fragile X premutation. Nature Genet. 4, 335-340.
    • (1993) Nature Genet. , vol.4 , pp. 335-340
    • Devys, D.1    Lutz, Y.2    Rouyer, N.3    Bellocq, J.-P.4    Mandel, J.-L.5
  • 27
    • 0030059545 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is associated with ribosomes
    • Khandjian, E.W., Corbin, F., Woerly, S. and Rousseau, F. (1996) The fragile X mental retardation protein is associated with ribosomes. Nature Genet. 12, 91-93.
    • (1996) Nature Genet. , vol.12 , pp. 91-93
    • Khandjian, E.W.1    Corbin, F.2    Woerly, S.3    Rousseau, F.4
  • 28
    • 0027234076 scopus 로고
    • Use of a general purpose mammalian expression vector for studying intracellular protein targeting: Identification of critical residues in the nuclear lamin A/C nuclear localization signal
    • Frangioni, J.V. and Neel, B.G. (1993) Use of a general purpose mammalian expression vector for studying intracellular protein targeting: identification of critical residues in the nuclear lamin A/C nuclear localization signal. J. Cell Sci. 105, 481-488.
    • (1993) J. Cell Sci. , vol.105 , pp. 481-488
    • Frangioni, J.V.1    Neel, B.G.2
  • 29
    • 0027365762 scopus 로고
    • Nuclear localization signals (NLS)
    • Boulikas, T. (1993) Nuclear localization signals (NLS). CRC Crit. Rev. Euk. Gene Expr. 3, 193-227.
    • (1993) CRC Crit. Rev. Euk. Gene Expr. , vol.3 , pp. 193-227
    • Boulikas, T.1
  • 30
    • 0026751769 scopus 로고
    • Intracellular distribution of the U1A protein depends on active transport and nuclear binding to U1 snRNA
    • Kambach, C. and Mattaj, I.W. (1992) Intracellular distribution of the U1A protein depends on active transport and nuclear binding to U1 snRNA. J Cell Biol. 118, 11-21.
    • (1992) J Cell Biol. , vol.118 , pp. 11-21
    • Kambach, C.1    Mattaj, I.W.2
  • 31
    • 0028930155 scopus 로고
    • A nuclear localization domain in the hnRNP A1 protein
    • Siomi, H. and Dreyfuss, G. (1995) A nuclear localization domain in the hnRNP A1 protein. J. Cell Biol. 129, 551-560.
    • (1995) J. Cell Biol. , vol.129 , pp. 551-560
    • Siomi, H.1    Dreyfuss, G.2
  • 32
    • 0030051618 scopus 로고    scopus 로고
    • Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms
    • Sittler, A., Devys, D., Weber, C. and Mandel, J.-L. (1996) Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms. Hum. Mol. Genet. 5, 95-102.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 95-102
    • Sittler, A.1    Devys, D.2    Weber, C.3    Mandel, J.-L.4
  • 33
    • 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. and Luhrmann, R. (1995) The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82, 475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 34
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., Meinkoth, J.L., Tsien, R.Y. and Taylor, S.S. (1995) Identification of a signal for rapid export of proteins from the nucleus. Cell 82, 463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 35
    • 0029121296 scopus 로고
    • Nuclear export signals and the fast track to the cytoplasm
    • Gerace, L. (1995) Nuclear export signals and the fast track to the cytoplasm. Cell 82, 341-344.
    • (1995) Cell , vol.82 , pp. 341-344
    • Gerace, L.1
  • 36
    • 0028845313 scopus 로고
    • A nuclear export signal in hnRNP A1: A signal-mediated, temperature-dependent nuclear protein export pathway
    • Michael, W.M., Choi, M. and Dreyfuss, G. (1995) A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway. Cell 83, 415-422.
    • (1995) Cell , vol.83 , pp. 415-422
    • Michael, W.M.1    Choi, M.2    Dreyfuss, G.3
  • 37
    • 0030034421 scopus 로고    scopus 로고
    • A pre-mRNA-binding protein accom7 panies the RNA from the gene through the nuclear pores and into polysomes
    • Visa, N., Alzhanova-Ericsson, A.T., Sun, X., Kiseleva, E., Bjorkroth, B., Wurtz, T. and Daneholt, B. (1996) A pre-mRNA-binding protein accom7 panies the RNA from the gene through the nuclear pores and into polysomes. Cell 84, 253-264.
    • (1996) Cell , vol.84 , pp. 253-264
    • Visa, N.1    Alzhanova-Ericsson, A.T.2    Sun, X.3    Kiseleva, E.4    Bjorkroth, B.5    Wurtz, T.6    Daneholt, B.7
  • 38
    • 0026649409 scopus 로고
    • The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
    • Nelson, R.J., Ziegelhoffer, T., Nicolet, C., Werner-Washburne, M. and Craig, H.A. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71, 97-105.
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.J.1    Ziegelhoffer, T.2    Nicolet, C.3    Werner-Washburne, M.4    Craig, H.A.5
  • 39
    • 0028982138 scopus 로고
    • Growth-dependent translation of IGF-II mRNA by a rapamycin-sensitive pathway
    • Nielsen, F., Ostergaard, L., Nielsen, J. and Christiansen, J. (1995) Growth-dependent translation of IGF-II mRNA by a rapamycin-sensitive pathway. Nature 377, 358-362.
    • (1995) Nature , vol.377 , pp. 358-362
    • Nielsen, F.1    Ostergaard, L.2    Nielsen, J.3    Christiansen, J.4
  • 40
    • 0025007578 scopus 로고
    • Translational discrimination of mRNAs coding for human insulin-like growth factor II
    • Nielsen, F., Gammeltoft, S. and Christiansen, J. (1990) Translational discrimination of mRNAs coding for human insulin-like growth factor II. J. Biol. Chem. 265, 13431-13434.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13431-13434
    • Nielsen, F.1    Gammeltoft, S.2    Christiansen, J.3
  • 41
    • 0026022910 scopus 로고
    • How proteins enter the nucleus
    • Silver, P.A. (1991) How proteins enter the nucleus. Cell 64, 489-497.
    • (1991) Cell , vol.64 , pp. 489-497
    • Silver, P.A.1
  • 42
    • 0023055373 scopus 로고
    • Fluorescence microphotolysis to measure nucleocytoplasmic transport and intracellular mobility
    • Peters, R. (1986) Fluorescence microphotolysis to measure nucleocytoplasmic transport and intracellular mobility. Biochim. Biophys. Acta 864, 305-359.
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 305-359
    • Peters, R.1
  • 43
    • 0023669094 scopus 로고
    • The effect of protein context on nuclear location signal function
    • Roberts, B.L., Richardson, W.D. and Smith, A.E. (1987) The effect of protein context on nuclear location signal function. Cell 50, 465-475.
    • (1987) Cell , vol.50 , pp. 465-475
    • Roberts, B.L.1    Richardson, W.D.2    Smith, A.E.3
  • 44
    • 0024616796 scopus 로고
    • Context affects nuclear protein localization in Saccharomyces cerevisiae
    • Nelson, M. and Silver, P. (1989) Context affects nuclear protein localization in Saccharomyces cerevisiae. Mol. Cell. Biol. 9, 384-389.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 384-389
    • Nelson, M.1    Silver, P.2
  • 45
    • 0029098538 scopus 로고
    • A human nucleoporin-like protein that specifically interacts with HIV Rev
    • Fritz, C.C., Zapp. M.L. and Green, M.R. (1995) A human nucleoporin-like protein that specifically interacts with HIV Rev. Nature 376, 530-533.
    • (1995) Nature , vol.376 , pp. 530-533
    • Fritz, C.C.1    Zapp, M.L.2    Green, M.R.3
  • 46
    • 0029149833 scopus 로고
    • Identification of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory proteins
    • Bogerd, H.B., Fridell, R.A., Madore, S. and Cullen, B. (1995) Identification of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory proteins. Cell 82, 485-494.
    • (1995) Cell , vol.82 , pp. 485-494
    • Bogerd, H.B.1    Fridell, R.A.2    Madore, S.3    Cullen, B.4
  • 47
    • 0029122732 scopus 로고
    • Identification of a novel nuclear pore-associated protein as a functional target of the HIV-1 Rev protein in yeast
    • Stutz, F., Neville, M. and Rosbash, M. (1995) Identification of a novel nuclear pore-associated protein as a functional target of the HIV-1 Rev protein in yeast. Cell 82, 495-506.
    • (1995) Cell , vol.82 , pp. 495-506
    • Stutz, F.1    Neville, M.2    Rosbash, M.3
  • 48
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Gorlich, D. and Mattaj, I. (1996) Nucleocytoplasmic transport. Science 271, 1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Gorlich, D.1    Mattaj, I.2
  • 49
    • 0028880051 scopus 로고
    • Highly conserved 3′ UTR and expression pattern of FXR1 points to a divergent gene regulation of FXR1 and FMR1
    • Coy, J.F., Sedlacek, Z-S., Bachner, D., Hameister, H., Joos, S., Lichter, P., Delius, H., and Poustka, A. (1995) Highly conserved 3′ UTR and expression pattern of FXR1 points to a divergent gene regulation of FXR1 and FMR1. Hum. Mol. Genet. 4, 2209-2218.
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 2209-2218
    • Coy, J.F.1    Sedlacek, Z.-S.2    Bachner, D.3    Hameister, H.4    Joos, S.5    Lichter, P.6    Delius, H.7    Poustka, A.8
  • 50
    • 0028971722 scopus 로고
    • The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2
    • Zhang, Y., O'Connor, J.P., Siomi, M.C., Srinivasan, S., Dutra, A., Nussbaum, R.L. and Dreyfuss, G. (1995) The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2. EMBO J. 14, 5358-5366.
    • (1995) EMBO J. , vol.14 , pp. 5358-5366
    • Zhang, Y.1    O'Connor, J.P.2    Siomi, M.C.3    Srinivasan, S.4    Dutra, A.5    Nussbaum, R.L.6    Dreyfuss, G.7
  • 51
    • 0022857615 scopus 로고
    • Structure and function of nuclear and cytoplasmic ribonucleoprotein particles
    • Dreyfuss, G. (1986) Structure and function of nuclear and cytoplasmic ribonucleoprotein particles. Annu. Rev. Cell Biol. 2, 459-498.
    • (1986) Annu. Rev. Cell Biol. , vol.2 , pp. 459-498
    • Dreyfuss, G.1
  • 52
    • 0022637742 scopus 로고
    • The human 18S ribosomal RNA gene: Evolution and stability
    • Gonzalez, I. and Schmickel, R. (1986) The human 18S ribosomal RNA gene: evolution and stability. Am. J. Hum. Genet. 38, 419-427.
    • (1986) Am. J. Hum. Genet. , vol.38 , pp. 419-427
    • Gonzalez, I.1    Schmickel, R.2
  • 53
    • 0024447165 scopus 로고
    • Antiribosomal S10 antibodies in humans and MRL/lpr mice with systemic lupus erythematosus
    • Bonfa, E., Parnassa, A.P., Rhoads, D.D., Roufa, D.J., Wool, I.G. and Elkon, K.B. (1989) Antiribosomal S10 antibodies in humans and MRL/lpr mice with systemic lupus erythematosus. Arthritis Rheum. 32, 1252-1261.
    • (1989) Arthritis Rheum. , vol.32 , pp. 1252-1261
    • Bonfa, E.1    Parnassa, A.P.2    Rhoads, D.D.3    Roufa, D.J.4    Wool, I.G.5    Elkon, K.B.6


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