ArticleBiochemical and biophysical research communications2017
Drosophila Argonaute2 turnover is regulated by the ubiquitin proteasome pathway.
Article in Biochemical and biophysical research communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Regulatory Mechanisms of miRNA Turnover: Insights into ZSWIM8-Mediated Target-Directed MicroRNA Degradation.Biomedicines · 2025Review
- Argonaute 2 targets viral transcripts but not genomes of RNA viruses during antiviral RNA interference in Drosophila.PLoS pathogens · 2025Article
- What goes up must come down: off switches for regulatory RNAs.Genes & development · 2024Review
- PSMC3 promotes RNAi by maintaining AGO2 stability through USP14.Cellular & molecular biology letters · 2022Article
- Transposable element landscapes in aging Drosophila.PLoS genetics · 2022Article
- Identification of protein quality control regulators using a Drosophila model of TPI deficiency.Neurobiology of disease · 2021Article
- RanBP2/Nup358 enhances miRNA activity by sumoylating Argonautes.PLoS genetics · 2021Article
- The Role of Dynamic miRISC During Neuronal Development.Frontiers in molecular biosciences · 2020Review
- Topoisomerase 3β interacts with RNAi machinery to promote heterochromatin formation and transcriptional silencing in Drosophila.Nature communications · 2018Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Argonaute (AGO) proteins play a central role in the RNA interference (RNAi) pathway, which is a cytoplasmic mechanism important for post-transcriptional regulation of gene expression. In Drosophila, AGO2 also functions in the nucleus to regulate chromatin insulator activity and transcription. Although there are a number of studies focused on AGO2 function, the regulation of AGO2 turnover is not well understood. We found that mutation of T1149 or R1158 in the conserved PIWI domain causes AGO2 protein instability, but only T1149 affects RNAi activity. Mass spec analysis shows that several proteasome components co-purify with both wildtype and mutant AGO2, and knockdown of two proteasome pathway components results in AGO2 protein accumulation. Finally, AGO2 protein levels increase after treatment with the proteasome inhibitor MG132. Our results indicate that the ubiquitin-proteasome pathway is involved in AGO2 protein turnover.
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