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Title:	Dicer-2 promotes mRNA activation through cytoplasmic polyadenylation
Author:	Coll, Olga; Guitart, Tanit; Villalba, Ana; Papin, Catherine; Simonelig, Martine; Gebauer, Fátima
Abstract:	Cytoplasmic polyadenylation is a widespread mechanism to regulate mRNA translation. In vertebrates, this process requires two sequence elements in target 3' UTRs: the U-rich cytoplasmic polyadenylation element and the AAUAAA hexanucleotide. In Drosophila melanogaster, cytoplasmic polyadenylation of Toll mRNA occurs independently of these canonical elements and requires a machinery that remains to be characterized. Here we identify Dicer-2 as a component of this machinery. Dicer-2, a factor previously involved in RNA interference (RNAi), interacts with the cytoplasmic poly(A) polymerase Wispy. Depletion of Dicer-2 from polyadenylation-competent embryo extracts and analysis of wispy mutants indicate that both factors are necessary for polyadenylation and translation of Toll mRNA. We further identify r2d2 mRNA, encoding a Dicer-2 partner in RNAi, as a Dicer-2 polyadenylation target. Our results uncover a novel function of Dicer-2 in activation of mRNA translation through cytoplasmic polyadenylation.
Abstract:	This work was supported by MINECO and the European Regional Development Fund (ERDF) under BFU2012-37135, BFU2015-68741, and Consolider CSD2009-00080 grants to F.G., and by the CNRS UMR9002, ANR (ANR-2010-BLAN-1201-01 and ANR-15-CE12-0019-01), and FRM (Equipe FRM 2013 DEQ20130326534) to M.S. We acknowledge support of MINECO “Centro de Excelencia Severo Ochoa 2013-2017,” SEV-2012-0208.
Subject(s):	-Dicer-2 -Wispy -Cytoplasmic polyadenylation -Translation
Rights:	© 2018 Coll et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society. This article, published in RNA, is available under a Creative Commons License (Attribution 4.0 International), as described at http://creativecommons.org/licenses/by/4.0/. http://creativecommons.org/licenses/by/4.0/
Document type:	Article Article - Published version
Published by:	Cold Spring Harbor Laboratory Press (CSHL Press)
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