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MicroRNA binding by wildtype Ago2 and mutant Ago2 in human cells

ABSTRACT: Ago2 binds mature microRNAs (miRNAs) to regulate gene expression. A mutant Ago2 is constructed to render it unable to bind miRNAs and inhibit mRNA translation.

ORGANISM(S): Caenorhabditis elegans Rattus norvegicus Mus musculus Danio rerio Homo sapiens Drosophila melanogaster

PROVIDER: GSE37941 | GEO | 2013/03/01

SECONDARY ACCESSION(S): PRJNA165711

REPOSITORIES: GEO

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microRNA binding by wildtype Ago2 and mutant Ago2 in human cells

Project description:Ago2 binds mature microRNAs (miRNAs) to regulate gene expression. A mutant Ago2 is constructed to render it unable to bind miRNAs and inhibit mRNA translation. Human 293T cells were transiently transfected with a plasmid that encoded a FLAG-tagged wildtype human Ago2 or mutant Ago2. FLAG IP was preformed, and assoicated RNA was isolated and subjected miRNA microarray analysis.

2013-03-01 | E-GEOD-37941 | biostudies-arrayexpress

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Project description:As a core RISC component, Ago2 associates with miRNAs and target mRNAs. To identify these mRNAs, we ran lysate from HEK293T cells over a FLAG resin from 2 conditions: +FLAG-Ago2, +mock transfection. To identify mRNAs associated with specific miRNAs, we ran lysate from HEK293T cells over a FLAG resin from 2 conditions: +FLAG-Ago2 & miR-1, and +FLAG-Ago2 & miR-124. Set of arrays that are part of repeated experiments Compound Based Treatment: mock transfected Keywords: Biological Replicate

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mRNAs associated with Ago2: Ago2, Ago2+miR-1, Ago2+miR-124, mock transfected

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Project description:In this study we aimed to uncover which miRNAs are changed in the Ago2-amygdala complex following chronic social defeat in mice We used microarrays to determine which miRNAs are changed in the Ago2-amygdala complexof mice following chronic social defeat compared to control

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Loss of Lamin A leads to the nuclear translocation of AGO2 and compromised RNA interference

Project description:In mammals, RNA interference (RNAi) is mostly studied as a cytoplasmic event, however, numerous reports convincingly show nuclear localization of the AGO proteins. Nevertheless, the mechanism of nuclear entry remains to be fully elucidated, and the extent of nuclear RNAi further explored. We found that reduced Lamin A levels significantly induced nuclear influx of AGO2 in SHSY5Y neuroblastoma and A375 melanoma cancer cell lines, which normally have no nuclear AGO2. The translocation of AGO2 was accompanied by aggravated cell proliferation and we further found that the loss of Lamin A leads to EGFR and Src kinase activation, which regulates the turnover and stability of cytoplasmic AGO2. Furthermore, Lamin A KO significantly reduced the activity of nuclear RNAi. This was evident by AGO fPAR-CLIP in WT and Lamin A KO cells, where we observed ca 60% less efficiency of RNAi. Mass spectrometry of AGO interactome, from the nuclear fraction, indicated that AGO2 is in complex with FAM120A, a known interactor of AGO2 that reduces the activity of RNAi by competing with AGO2 transcript binding. Therefore, loss of Lamin A starts a signaling cascade that mediates nuclear AGO2 translocation to rapidly inhibit RNAi in order to facilitate cancer proliferation

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