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Lee, Hyung Chul,Jung, Seung Hee,Hwang, Hyun Jung,Kang, Donghee,De, Supriyo,Dudekula, Dawood B.,Martindale, Jennifer L.,Park, Byungkyu,Park, Seung Kuk,Lee, Eun Kyung,Lee, Jeong-Hwa,Jeong, Sunjoo,Han, K Oxford University Press 2017 Nucleic acids research Vol.45 No.11
<P><B>Abstract</B></P><P>RNA-binding proteins (RBPs) are involved in mRNA splicing, maturation, transport, translation, storage and turnover. Here, we identified <I>ACOT7</I> mRNA as a novel target of human WIG1. <I>ACOT7</I> mRNA decay was triggered by the microRNA miR-9 in a WIG1-dependent manner via classic recruitment of Argonaute 2 (AGO2). Interestingly, AGO2 was also recruited to <I>ACOT7</I> mRNA in a WIG1-dependent manner in the absence of miR-9, which indicates an alternative model whereby WIG1 controls AGO2-mediated gene silencing. The WIG1–AGO2 complex attenuated translation initiation via an interaction with translation initiation factor 5B (eIF5B). These results were confirmed using a WIG1 tethering system based on the MS2 bacteriophage coat protein and a reporter construct containing an MS2-binding site, and by immunoprecipitation of WIG1 and detection of WIG1-associated proteins using liquid chromatography-tandem mass spectrometry. We also identified WIG1-binding motifs using photoactivatable ribonucleoside-enhanced crosslinking and immunoprecipitation analyses. Altogether, our data indicate that WIG1 governs the miRNA-dependent and the miRNA-independent recruitment of AGO2 to lower the stability of and suppress the translation of <I>ACOT7</I> mRNA.</P>