Cytoplasmic polyadenylation of mRNAs promotes their translation in a wide variety of biological contexts. The conserved RNA-binding protein family CPEB has been shown to mediate canonical cytoplasmic polyadenylation of target transcripts. We have previously reported evidence for RNA-interference factor Dicer-2 as a component of a non-canonical complex, that operates independent of CPEB in Drosophila. In this study, we investigated Dicer-2 mRNA targets and protein co-factors in cytoplasmic polyadenylation. We identified hundreds of novel Dicer-2 target transcripts, ~50% of which were previously found as targets of the cytoplasmic poly(A) polymerase Wispy, suggesting widespread roles of Dicer-2 in cytoplasmic polyadenylation. Large-scale immunoprecipitation and mass spectrometry revealed Ataxin-2 and Twenty-four among the high-confidence interactors of Dicer-2. Functional analysis indicates that both factors form an RNA-independent complex with Dicer-2 and are required for cytoplasmic polyadenylation of Dicer-2 targets. Our results reveal the composition of a novel cytoplasmic polyadenylation complex that operates during Drosophila early embryogenesis.