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A correction to this article has been published: Wang et al., J. Cell Biol. 172 (4) 635
Published 5 December 2005. doi:10.1083/jcb.200506006
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 5, 811-821
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Article

Dendritic BC1 RNA in translational control mechanisms



Huidong Wang1,2, Anna Iacoangeli1, Daisy Lin1,2, Keith Williams1, Robert B. Denman5, Christopher U.T. Hellen2,3, and Henri Tiedge1,2,4

1 Department of Physiology and Pharmacology, State University of New York, Health Science Center at Brooklyn, Brooklyn, NY 11203
2 Program in Molecular and Cellular Biology, State University of New York, Health Science Center at Brooklyn, Brooklyn, NY 11203
3 Department of Microbiology and Immunology, State University of New York, Health Science Center at Brooklyn, Brooklyn, NY 11203
4 Department of Neurology, State University of New York, Health Science Center at Brooklyn, Brooklyn, NY 11203
5 Department of Molecular Biology, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314

Correspondence to Henri Tiedge: htiedge{at}downstate.edu

Translational control at the synapse is thought to be a key determinant of neuronal plasticity. How is such control implemented? We report that small untranslated BC1 RNA is a specific effector of translational control both in vitro and in vivo. BC1 RNA, expressed in neurons and germ cells, inhibits a rate-limiting step in the assembly of translation initiation complexes. A translational repression element is contained within the unique 3' domain of BC1 RNA. Interactions of this domain with eukaryotic initiation factor 4A and poly(A) binding protein mediate repression, indicating that the 3' BC1 domain targets a functional interaction between these factors. In contrast, interactions of BC1 RNA with the fragile X mental retardation protein could not be documented. Thus, BC1 RNA modulates translation-dependent processes in neurons and germs cells by directly interacting with translation initiation factors.

H. Wang's present address is Laboratory of Molecular Neuro-Oncology, The Rockefeller University, New York, NY 10021.

Abbreviations used in this paper: AGESA, agarose gel electrophoresis assay; ANOVA, analysis of variance; BMPR, bone morphogenic protein receptor; CPE, cytoplasmic polyadenylation element; CSFV, classical swine fever virus; eEF1A, eukaryotic elongation factor 1A; eIF, eukaryotic initiation factor; EMSA, electrophoretic mobility shift assay; FMRP, fragile X mental retardation protein; IRES, internal ribosome entry site; PABP, poly(A) binding protein; RRL, rabbit reticulocyte lysate; RRM, RNA recognition motif; utRNA, untranslated RNA.


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