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J. Biol. Chem., Vol. 280, Issue 52, 43131-43140, December 30, 2005

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Mammalian Smaug Is a Translational Repressor That Forms Cytoplasmic Foci Similar to Stress Granules^*

From the Fundación Instituto Leloir, IIBBA CONICET and IIB Facultad de Ciencias Exactas y Naturales, University of Buenos Aires, C1405BWE Buenos Aires, Argentina

Cytoplasmic events depending on RNA-binding proteins contribute to the fine-tuning of gene expression. Sterile motif-containing RNA-binding proteins constitute a novel family of post-transcriptional regulators that recognize a specific RNA sequence motif known as Smaug recognition element (SRE). The Drosophila member of this family, dSmaug, triggers the translational repression and deadenylation of maternal mRNAs by independent mechanisms, and the yeast homologue Vts1 stimulates degradation of SRE-containing messengers. Two homologous genes are present in the mammalian genome. Here we showed that hSmaug 1, encoded in human chromosome 14, represses the translation of reporter transcripts carrying SRE motifs. When expressed in fibroblasts, hSmaug 1 forms cytoplasmic granules that contain polyadenylated mRNA and the RNA-binding proteins Staufen, TIAR, TIA-1, and HuR. Smaug 1 foci are distinct from degradation foci. The murine protein mSmaug 1 is expressed in the central nervous system and is abundant in post-synaptic densities, a subcellular region where translation is tightly regulated by synaptic stimulation. Biochemical analysis indicated that mSmaug 1 is present in synaptoneurosomal 20 S particles. These results suggest a role for mammalian Smaug 1 in RNA granule formation and translation regulation in neurons.

Received for publication, August 1, 2005 , and in revised form, September 19, 2005.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) DQ278487 [GenBank] .

^* This work was supported by Agencia Nacional de Promoción Científica y Tecnológica Grant PICT 01-08691, Argentina, National Institutes of Health-Fogarty International Research Collaboration Award 1 RO3 TW 006037-01A1, and The Wadsworth Foundation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Figs. S1 and S2.

¹ Fellow of the Consejo Nacional de Investigaciones Científicas y Tecnológicas, Argentina.

² To whom correspondence should be addressed: Fundación Instituto Leloir, Patricias Argentinas 435 (C1405BWE) Ciudad de Buenos Aires, Argentina. Tel.: 5411-5238-7500; Fax: 5411-5238-7501; E-mail: gboccaccio{at}leloir.org.ar.

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