메뉴 건너뛰기




Volumn 1, Issue 1, 1997, Pages 109-118

FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association

Author keywords

[No Author keywords available]

Indexed keywords

FMR1 PROTEIN, HUMAN; FRAGILE X MENTAL RETARDATION PROTEIN; MESSENGER RIBONUCLEOPROTEIN; MESSENGER RNA; NERVE PROTEIN; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN;

EID: 0031310667     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80012-X     Document Type: Article
Times cited : (423)

References (47)
  • 1
    • 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. (1993a). 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
  • 3
    • 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
  • 4
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C.G., and Dreyfuss, G. (1994). Conserved structures and diversity of functions of RNA-binding proteins. Science 265, 615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 6
    • 0025280892 scopus 로고
    • Reversal of creatine kinase translational repression by 3′ untranslated sequences
    • Ch'ng, J.L.C., Shoemaker, D.L., Schimmel, P., and Holmes, E.W. (1990). Reversal of creatine kinase translational repression by 3′ untranslated sequences. Science 248, 1003-1005.
    • (1990) Science , vol.248 , pp. 1003-1005
    • Ch'ng, J.L.C.1    Shoemaker, D.L.2    Schimmel, P.3    Holmes, E.W.4
  • 8
    • 0030760613 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is associated with poly(A)+ mRNA in actively translating polyribosomes
    • Corbin, F., Bouillon, M., Fortin, A., Morin, S., Rousseau, F., and Khandjian, E.W. (1997). The fragile X mental retardation protein is associated with poly(A)+ mRNA in actively translating polyribosomes. Hum. Mol. Genet. 6, 1465-1472.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1465-1472
    • Corbin, F.1    Bouillon, M.2    Fortin, A.3    Morin, S.4    Rousseau, F.5    Khandjian, E.W.6
  • 10
    • 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. Nat. Genet. 4, 335-340.
    • (1993) Nat. Genet. , vol.4 , pp. 335-340
    • Devys, D.1    Lutz, Y.2    Rouyer, N.3    Bellocq, J.-P.4    Mandel, J.-L.5
  • 12
    • 0029816723 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals
    • Eberhart, D.E., Malter, H.E., Feng, Y., and Warren, S.T. (1996). The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals. Hum. Mol. Genet. 5, 1083-1091.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1083-1091
    • Eberhart, D.E.1    Malter, H.E.2    Feng, Y.3    Warren, S.T.4
  • 13
    • 0030428905 scopus 로고    scopus 로고
    • Molecular basis of fragile X syndrome
    • CoId Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Eberhart, D.E., and Warren, S.T. (1996). Molecular basis of fragile X syndrome. In Cold Spring Harbor Symposia on Quantitative Biology Vol. LXI(CoId Spring Harbor, New York: Cold Spring Harbor Laboratory Press), pp. 679-687.
    • (1996) Cold Spring Harbor Symposia on Quantitative Biology , vol.61 , pp. 679-687
    • Eberhart, D.E.1    Warren, S.T.2
  • 14
    • 0028979161 scopus 로고
    • Quantitative comparison of FMR1 gene expression in normal and premutation alleles
    • Feng, Y., Lakkis, L., Devys, D., and Warren, S.T. (1995). Quantitative comparison of FMR1 gene expression in normal and premutation alleles. Am. J. Hum. Genet. 56, 106-113.
    • (1995) Am. J. Hum. Genet. , vol.56 , pp. 106-113
    • Feng, Y.1    Lakkis, L.2    Devys, D.3    Warren, S.T.4
  • 15
    • 0031046778 scopus 로고    scopus 로고
    • Fragile X mental retardation protein: Nucleocytoplasmic shuttling and association with somatodendritic ribosomes
    • Feng, Y., Gutekunst, C.A., Eberhart, D.E., Yi, H., Warren, S.T., and Hersch, S.M. (1997). Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes. J. Neurosci. 17, 1539-1547.
    • (1997) J. Neurosci. , vol.17 , pp. 1539-1547
    • Feng, Y.1    Gutekunst, C.A.2    Eberhart, D.E.3    Yi, H.4    Warren, S.T.5    Hersch, S.M.6
  • 16
    • 0029818460 scopus 로고    scopus 로고
    • A nuclear role for the fragile X mental retardation protein
    • Fridell, R.A., Benson, R.E., Hua, J., Bogerd, H.P., and Cullen, B.R. (1996). A nuclear role for the fragile X mental retardation protein. EMBO J. 15, 5408-5414.
    • (1996) EMBO J. , vol.15 , pp. 5408-5414
    • Fridell, R.A.1    Benson, R.E.2    Hua, J.3    Bogerd, H.P.4    Cullen, B.R.5
  • 18
    • 0029790377 scopus 로고    scopus 로고
    • Inducers of erythroleukemic differentiation cause messenger RNAs that lack poly(A)-binding protein to accumulate in translationally inactive, salt-labile 80S ribosomal complexes
    • Hensold, J.O., Barth-Baus, D., and Stratton, C.A. (1996). Inducers of erythroleukemic differentiation cause messenger RNAs that lack poly(A)-binding protein to accumulate in translationally inactive, salt-labile 80S ribosomal complexes. J. Biol. Chem. 271, 23246-23254.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23246-23254
    • Hensold, J.O.1    Barth-Baus, D.2    Stratton, C.A.3
  • 20
    • 0023772605 scopus 로고
    • Importance of polysomal mRNA-associated polypeptides for protein synthesis initiation in yeast
    • Herrera, F., Triana, L., and Bosch, I. (1988). Importance of polysomal mRNA-associated polypeptides for protein synthesis initiation in yeast. Eur. J. Biochem. 175, 87-92.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 87-92
    • Herrera, F.1    Triana, L.2    Bosch, I.3
  • 21
    • 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
  • 22
    • 0025720084 scopus 로고
    • Analysis of neocortex in three males with the fragile X syndrome
    • Hinton, V.J., Brown, W.T., Wisniewski, K., and Rudelli, R.D. (1991). Analysis of neocortex in three males with the fragile X syndrome. Am. J. Med. Genet. 41, 289-294.
    • (1991) Am. J. Med. Genet. , vol.41 , pp. 289-294
    • Hinton, V.J.1    Brown, W.T.2    Wisniewski, K.3    Rudelli, R.D.4
  • 24
    • 0028169728 scopus 로고
    • Elongation factor-1α mRNA is selectively translated following mitogenic stimulation
    • Jefferies, H.B.J., Thomas, G., and Thomas, G. (1994). Elongation factor-1α mRNA is selectively translated following mitogenic stimulation. J. Biol. Chem. 269, 4367-4372.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4367-4372
    • Jefferies, H.B.J.1    Thomas, G.2    Thomas, G.3
  • 25
    • 0029015430 scopus 로고
    • Mutations in gld-1, a female germ cell-specific tumor suppresser gene in Caenorhabditis elegans, affect a conserved domain also found in Src-associated protein sam68
    • Jones, A.J., and Schedl, T. (1995). Mutations in gld-1, a female germ cell-specific tumor suppresser gene in Caenorhabditis elegans, affect a conserved domain also found in Src-associated protein Sam68. EMBO J. 9, 1491-1504.
    • (1995) EMBO J. , vol.9 , pp. 1491-1504
    • Jones, A.J.1    Schedl, T.2
  • 26
    • 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. Nat. Genet. 12, 91-93.
    • (1996) Nat. Genet. , vol.12 , pp. 91-93
    • Khandjian, E.W.1    Corbin, F.2    Woerly, S.3    Rousseau, F.4
  • 27
    • 0029125496 scopus 로고
    • Identification of two KH domain proteins in the α-globin mRNP stability complex
    • Kiledjian, M., Wang, X., and Liebhaber, S.A. (1995). Identification of two KH domain proteins in the α-globin mRNP stability complex. EMBO J. 14, 4357-4364.
    • (1995) EMBO J. , vol.14 , pp. 4357-4364
    • Kiledjian, M.1    Wang, X.2    Liebhaber, S.A.3
  • 28
    • 0029076374 scopus 로고
    • Characterization of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains
    • Leffers, H., Dejgaard, K., and Celis, J.E. (1995). Characterization of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains. Eur. J. Biochem. 230, 447-453.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 447-453
    • Leffers, H.1    Dejgaard, K.2    Celis, J.E.3
  • 29
    • 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. Nat. Genet. 10, 483-485.
    • (1995) Nat. 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
  • 30
    • 0029030017 scopus 로고
    • Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA binding motif of FMR1
    • Mahone, M., Saffman, E.E., and Lasko, P.F. (1995). Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA binding motif of FMR1. EMBO J. 14, 2043-2055.
    • (1995) EMBO J. , vol.14 , pp. 2043-2055
    • Mahone, M.1    Saffman, E.E.2    Lasko, P.F.3
  • 32
    • 0029988528 scopus 로고    scopus 로고
    • Three-dimensional structure and stability of the KH domain: Molecular insights into the fragile X syndrome
    • Musco, G., Stier, G., Joseph, C., Morelli, M.A.C., Nilges, M., Gibson, T.J., and Pastore, A. (1996). Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell 85, 237-245.
    • (1996) Cell , vol.85 , pp. 237-245
    • Musco, G.1    Stier, G.2    Joseph, C.3    Morelli, M.A.C.4    Nilges, M.5    Gibson, T.J.6    Pastore, A.7
  • 33
    • 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, E.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, E.A.5
  • 34
    • 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
  • 37
    • 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
  • 38
    • 0028236525 scopus 로고
    • Essential role for KH domains in RNA binding: Impaired RNA binding by a mutation in the KH domain of FMR1 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 FMR1 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
  • 40
    • 0029972935 scopus 로고    scopus 로고
    • Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them
    • Siomi, M.C., Zhang, Y., Siomi, H., and Dreyfuss, G. (1996). Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them. Mol. Cell. Biol. 16, 3825-3832.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3825-3832
    • Siomi, M.C.1    Zhang, Y.2    Siomi, H.3    Dreyfuss, G.4
  • 41
    • 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
  • 44
    • 0029087624 scopus 로고
    • Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by crosslinking studies
    • Urlaub, H., Kruft, V., Biscof, O., Mueller, E.C., and Wittmann-Liebold, B. (1995). Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by crosslinking studies. EMBO J. 14, 4578-4588.
    • (1995) EMBO J. , vol.14 , pp. 4578-4588
    • Urlaub, H.1    Kruft, V.2    Biscof, O.3    Mueller, E.C.4    Wittmann-Liebold, B.5
  • 45
    • 0025905795 scopus 로고
    • Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome
    • Verkerk, A.J.M.H., Pieretti, M., Sutcliffe, J.S., Fu, Y.-H., Kuhl, D.P.A., Pizutti, A., Reiner, O., Richards, S., Victoria, M.F., Zhang, F., et al. (1991). Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome. Cell 65, 905-914.
    • (1991) Cell , vol.65 , pp. 905-914
    • Verkerk, A.J.M.H.1    Pieretti, M.2    Sutcliffe, J.S.3    Fu, Y.-H.4    Kuhl, D.P.A.5    Pizutti, A.6    Reiner, O.7    Richards, S.8    Victoria, M.F.9    Zhang, F.10
  • 46
    • 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. J. Am. Med. Assoc. 271, 536-542.
    • (1994) J. Am. Med. Assoc. , vol.271 , pp. 536-542
    • Warren, S.T.1    Nelson, D.L.2
  • 47
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.