Human Molecular Genetics, 2002, Vol. 11, No. 24 3007-3017
© 2002 Oxford University Press
Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression
Unité de Recherche en Génétique Humaine et Moléculaire, Centre de recherche Hôpital Saint François d'Assise, Québec and Département de biologie médicale, Faculté de médecine, Université Laval, Québec, Canada
Received July 11, 2002; Accepted September 13, 2002
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.
* To whom correspondence should be addressed at: URGHM, Centre de recherche Hôpital St François d'Assise, 10 rue de l'Espinay, Québec G1L 3L5, PQ, Canada. Tel: +1 4185254402; Fax: +1 4185254195; Email: edward.khandjian{at}crsfa.ulaval.ca
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Y. J. Sung, N. Dolzhanskaya, S. L. Nolin, T. Brown, J. R. Currie, and R. B. Denman The Fragile X Mental Retardation Protein FMRP Binds Elongation Factor 1A mRNA and Negatively Regulates Its Translation in Vivo J. Biol. Chem., April 25, 2003; 278(18): 15669 - 15678. [Abstract] [Full Text] [PDF]
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