Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1927809 | Biochemical and Biophysical Research Communications | 2016 | 6 Pages |
•Human GIGYF2 may be a novel component of the microRNA-induced silencing complex.•When tethered to a reporter mRNA, GIGYF2 exerts a dose-dependent silencing activity.•Translational repression and mRNA decay contribute to GIGYF2 silencing activity.
In mammalian post-transcriptional gene silencing, the Argonaute protein AGO2 indirectly recruits translation inhibitors, deadenylase complexes, and decapping factors to microRNA-targeted mRNAs, thereby repressing mRNA translation and accelerating mRNA decay. However, the exact composition and assembly pathway of the microRNA-induced silencing complex are not completely elucidated. As the GYF domain of human GIGYF2 was shown to bind AGO2 in pulldown experiments, we wondered whether GIGYF2 could be a novel protein component of the microRNA-induced silencing complex. Here we show that full-length GIGYF2 coimmunoprecipitates with AGO2 in human cells, and demonstrate that, upon tethering to a reporter mRNA, GIGYF2 exhibits strong, dose-dependent silencing activity, involving both mRNA destabilization and translational repression.