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É. Khandjian, B. Bardoni, F. Corbin, A. Sittler, S. Giroux, D. Heitz, S. Tremblay, C. Pinset, D. Montarras, François Rousseau, J. Mandel (1998)
Novel isoforms of the fragile X related protein FXR1P are expressed during myogenesis.Human molecular genetics, 7 13
REFERENCES
P. Opal, H. Paulson (1998)
Genetic Instabilities and Hereditary Neurological DiseasesAmerican Journal of Human Genetics, 63
Marc-Étienne Huot, R. Mazroui, Pierre Leclerc, É. Khandjian (2001)
Developmental expression of the fragile X-related 1 proteins in mouse testis: association with microtubule elements.Human molecular genetics, 10 24
B. Laggerbauer, D. Ostareck, Eva‐Maria Keidel, A. Ostareck-Lederer, U. Fischer (2001)
Evidence that fragile X mental retardation protein is a negative regulator of translation.Human molecular genetics, 10 4
D. Eberhart, H. Malter, Yue Feng, S. Warren (1996)
The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals.Human molecular genetics, 5 8
I. Weiler, S. Irwin, A. Klintsova, C. Spencer, Anthony Brazelton, K. Miyashiro, T. Comery, B. Patel, J. Eberwine, W. Greenough (1997)
Fragile X mental retardation protein is translated near synapses in response to neurotransmitter activation.Proceedings of the National Academy of Sciences of the United States of America, 94 10
N. Collier, J. Heuser, M. Levy, M. Schlesinger (1988)
Ultrastructural and biochemical analysis of the stress granule in chicken embryo fibroblastsThe Journal of Cell Biology, 106
G. Dreyfuss, M. Matunis, S. Piñol-Roma, C. Burd (1993)
hnRNP proteins and the biogenesis of mRNA.Annual review of biochemistry, 62
Yong Zhang, A. Bailey, Heinrich Matthies, Robert Renden, Mark Smith, S. Speese, G. Rubin, K. Broadie (2001)
Drosophila Fragile X-Related Gene Regulates the MAP1B Homolog Futsch to Control Synaptic Structure and FunctionCell, 107
É. Khandjian, J. Gauchat (1988)
One single burst of SV40 gene expression induces cell proliferation in transforming infection of mouse cells.Oncogene, 3 2
B. Bardoni, J. Mandel (2002)
Advances in understanding of fragile X pathogenesis and FMRP function, and in identification of X linked mental retardation genes.Current opinion in genetics & development, 12 3
I. Weiler, W. Greenough (1993)
Metabotropic glutamate receptors trigger postsynaptic protein synthesis.Proceedings of the National Academy of Sciences of the United States of America, 90 15
E. Davydova, V. Evdokimova, Lev Ovchinnikov, John Hershey (1997)
Overexpression in COS cells of p50, the major core protein associated with mRNA, results in translation inhibition.Nucleic acids research, 25 14
I. Gallouzi, C. Brennan, Myrna Stenberg, M. Swanson, Ashley Eversole, N. Maizels, J. Steitz (2000)
HuR binding to cytoplasmic mRNA is perturbed by heat shock.Proceedings of the National Academy of Sciences of the United States of America, 97 7
The Consorthium, C. Bakker, C. Verheij, R. Willemsen, R. Helm, F. Oerlemans, M. Vermey, A. Bygrave, A. Hoogeveen, B. Oostra, E. Reyniers, Kristel Boule, R. D'Hooge, P. Cras, D. Velzen, G. Nagels, Jean-Jacques Martin, P. Deyn, J. Darby, P. Willems (1994)
Fmr1 knockout mice: A model to study fragile X mental retardationCell, 78
L. Nover, K. Scharf, D. Neumann (1989)
Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAsMolecular and Cellular Biology, 9
D. Devys, Y. Lutz, N. Rouyer, J. Bellocq, J. Mandel (1993)
The FMR–1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutationNature Genetics, 4
C. Schaeffer, B. Bardoni, J. Mandel, B. Ehresmann, C. Ehresmann, H. Moine (2001)
The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motifThe EMBO Journal, 20
Marthe Dubé, Marc-Étienne Huot, É. Khandjian (2000)
Muscle Specific Fragile X Related Protein 1 Isoforms are Sequestered in the Nucleus of Undifferentiated MyoblastBMC Genetics, 1
N. Kedersha, Samantha Chen, Natalie Gilks, Wei Li, Ira Miller, J. Stahl, P. Anderson (2002)
Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules.Molecular biology of the cell, 13 1
S. Ceman, V. Brown, S. Warren (1999)
Isolation of an FMRP-Associated Messenger Ribonucleoprotein Particle and Identification of Nucleolin and the Fragile X-Related Proteins as Components of the ComplexMolecular and Cellular Biology, 19
S. Ceman, R. Nelson, Stephen Warren (2000)
Identification of mouse YB1/p50 as a component of the FMRP-associated mRNP particle.Biochemical and biophysical research communications, 279 3
G. Schochetman, R. Perry (1972)
Characterization of the messenger RNA released from L cell polyribosomes as a result of temperature shock.Journal of molecular biology, 63 3
Martin Köhrmann, Ming Luo, C. Kaether, L. DesGroseillers, C. Dotti, M. Kiebler (1999)
Microtubule-dependent recruitment of Staufen-green fluorescent protein into large RNA-containing granules and subsequent dendritic transport in living hippocampal neurons.Molecular biology of the cell, 10 9
R. Fridell, R. Benson, J. Hua, H. Bogerd, B. Cullen (1996)
A nuclear role for the Fragile X mental retardation protein.The EMBO Journal, 15
N. Kedersha, M. Cho, Wei Li, P. Yacono, Samantha Chen, Natalie Gilks, D. Golan, P. Anderson (2000)
Dynamic Shuttling of Tia-1 Accompanies the Recruitment of mRNA to Mammalian Stress GranulesThe Journal of Cell Biology, 151
Veronica Hinton, Veronica Hinton, W. Brown, K. Wisniewski, R. Rudelli (1991)
Analysis of neocortex in three males with the fragile X syndrome.American journal of medical genetics, 41 3
Yan Zhang, James O'Connor, M. Siomi, S. Srinivasan, A. Dutra, R. Nussbaum, G. Dreyfuss (1995)
The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2.The EMBO Journal, 14
S. McKenzie, S. Henikoff, M. Meselson (1975)
Localization of RNA from heat-induced polysomes at puff sites in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America, 72 3
W. Greenough, A. Klintsova, S. Irwin, R. Galvez, Kathy Bates, I. Weiler (2001)
Synaptic regulation of protein synthesis and the fragile X proteinProceedings of the National Academy of Sciences of the United States of America, 98
L. Wan, T. Dockendorff, T. Jongens, G. Dreyfuss (2000)
Characterization of dFMR1, a Drosophila melanogaster Homolog of the Fragile X Mental Retardation ProteinMolecular and Cellular Biology, 20
R. Knowles, James Sabry, M. Martone, T. Deerinck, Mark Ellisman, G. Bassell, K. Kosik (1996)
Translocation of RNA Granules in Living NeuronsThe Journal of Neuroscience, 16
William McCormick, S. Penman (1969)
Regulation of protein synthesis in HeLa cells: translation at elevated temperatures.Journal of molecular biology, 39 2
Yue Feng, D. Absher, D. Eberhart, V. Brown, H. Malter, S. Warren (1997)
FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association.Molecular cell, 1 1
P. Anderson, N. Kedersha (2002)
Visibly stressed: the role of eIF2, TIA-1, and stress granules in protein translation, 7
W. O'donnell, S. Warren (2002)
A decade of molecular studies of fragile X syndrome.Annual review of neuroscience, 25
Barbara Bardoni, A. Sittler, Yan Shen, Jean-Louis Mandel (1997)
Analysis of Domains Affecting Intracellular Localization of the FMRP ProteinNeurobiology of Disease, 4
F. Corbin, M. Bouillon, A. Fortin, Stanislas Morin, François Rousseau, É. Khandjian (1997)
The fragile X mental retardation protein is associated with poly(A)+ mRNA in actively translating polyribosomes.Human molecular genetics, 6 9
N. Kedersha, M. Gupta, Wei Li, Ira Miller, P. Anderson (1999)
RNA-Binding Proteins Tia-1 and Tiar Link the Phosphorylation of Eif-2α to the Assembly of Mammalian Stress GranulesThe Journal of Cell Biology, 147
F. Tamanini, L. Unen, C. Bakker, N. Sacchi, H. Galjaard, B. Oostra, A. Hoogeveen (1999)
Oligomerization properties of fragile-X mental-retardation protein (FMRP) and the fragile-X-related proteins FXR1P and FXR2P.The Biochemical journal, 343 Pt 3
É. Khandjian, F. Anny, A. Thibodeau, S. Tremblay, F. Côté, D. Devys, J.-L. Mandel, F. Rousseau (1995)
A heterogeneous set of FMR1 proteins is widely distributed in mouse tissues and is modulated in cell culture.Human molecular genetics, 4 5
I. Gantois, C. Bakker, E. Reyniers, R. Willemsen, R. D'Hooge, P. Deyn, B. Oostra, R. Kooy (2001)
Restoring the phenotype of fragile X syndrome: insight from the mouse model.Current molecular medicine, 1 4
É. Khandjian, F. Corbin, S. Woerly, F. Rousseau (1996)
The fragile X mental retardation protein is associated with ribosomesNature Genetics, 12
Hyejin Kang, E. Schuman (1996)
A Requirement for Local Protein Synthesis in Neurotrophin-Induced Hippocampal Synaptic PlasticityScience, 273
Anna Krichevsky, K. Kosik (2001)
Neuronal RNA Granules A Link between RNA Localization and Stimulation-Dependent TranslationNeuron, 32
É. Khandjian (1999)
Biology of the fragile X mental retardation protein, an RNA-binding protein.Biochemistry and cell biology = Biochimie et biologie cellulaire, 77 4
T. Comery, J. Harris, P. Willems, B. Oostra, S. Irwin, I. Weiler, W. Greenough (1997)
Abnormal dendritic spines in fragile X knockout mice: maturation and pruning deficits.Proceedings of the National Academy of Sciences of the United States of America, 94 10
R. Duncan, J. Hershey (1984)
Heat shock-induced translational alterations in HeLa cells. Initiation factor modifications and the inhibition of translation.The Journal of biological chemistry, 259 19
A. Sittler, D. Devys, C. Weber, J. Mandel (1996)
Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms.Human molecular genetics, 5 1
S. Irwin, B. Patel, Madhuri Idupulapati, J. Harris, Ralph Crisostomo, Brian Larsen, F. Kooy, P. Willems, P. Cras, Piotr Kozlowski, R. Swain, I. Weiler, W. Greenough (2001)
Abnormal dendritic spine characteristics in the temporal and visual cortices of patients with fragile-X syndrome: a quantitative examination.American journal of medical genetics, 98 2
M. Chicurel, D. Terrian, H. Potter (1993)
mRNA at the synapse: analysis of a synaptosomal preparation enriched in hippocampal dendritic spines, 13
M. Kiebler, L. DesGroseillers (2000)
Molecular Insights into mRNA Transport and Local Translation in the Mammalian Nervous SystemNeuron, 25
Zhenzhong Li, Youyi Zhang, Li Ku, K. Wilkinson, S. Warren, Yue Feng (2001)
The fragile X mental retardation protein inhibits translation via interacting with mRNA.Nucleic acids research, 29 11
E. Nimchinsky, A. Oberlander, K. Svoboda (2001)
Abnormal Development of Dendritic Spines inFMR1 Knock-Out MiceThe Journal of Neuroscience, 21
J. Darnell, K. Jensen, P. Jin, V. Brown, S. Warren, R. Darnell (2001)
Fragile X Mental Retardation Protein Targets G Quartet mRNAs Important for Neuronal FunctionCell, 107
M. Siomi, H. Siomi, W. Sauer, S. Srinivasan, R. Nussbaum, G. Dreyfuss (1995)
FXR1, an autosomal homolog of the fragile X mental retardation gene.The EMBO Journal, 14
A. Peier, K. McIlwain, A. Kenneson, S. Warren, R. Paylor, D. Nelson (2000)
(Over)correction of FMR1 deficiency with YAC transgenics: behavioral and physical features.Human molecular genetics, 9 8
Absence of Fragile X Mental Retardation Protein (FMRP), an RNA-binding protein, is responsible for the Fragile X syndrome, the most common form of inherited mental retardation. FMRP is a cytoplasmic protein associated with mRNP complexes containing poly(A)+mRNA. As a step towards understanding FMRP function(s), we have established the immortal STEK Fmr1 KO cell line and showed by transfection assays with FMR1 -expressing vectors that newly synthesized FMRP accumulates into cytoplasmic granules. These structures contain mRNAs and several other RNA-binding proteins. The formation of these cytoplasmic granules is dependent on determinants located in the RGG domain. We also provide evidence that FMRP acts as a translation repressor following co-transfection with reporter genes. The FMRP-containing mRNPs are dynamic structures that oscillate between polyribosomes and cytoplasmic granules reminiscent of the Stress Granules that contain repressed mRNAs. We speculate that, in neurons, FMRP plays a role as a mRNA repressor in incompetent mRNP granules that have to be translocated from the cell body to distal locations such as dendritic spines and synaptosomes. « Previous | Next Article » Table of Contents This Article Hum. Mol. Genet. (2002) 11 (24): 3007-3017. doi: 10.1093/hmg/11.24.3007 » Abstract Free Full Text (HTML) Free Full Text (PDF) Free Classifications Article Services Article metrics Alert me when cited Alert me if corrected Find similar articles Similar articles in Web of Science Similar articles in PubMed Add to my archive Download citation Request Permissions Citing Articles Load citing article information Citing articles via CrossRef Citing articles via Scopus Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Mazroui, R. Articles by Khandjian, E. W. Search for related content PubMed PubMed citation Articles by Mazroui, R. Articles by Huot, M. E. Articles by Tremblay, S. 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Human Molecular Genetics – Oxford University Press
Published: Nov 15, 2002
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