ArticleCell reports2022
A specific type of Argonaute phosphorylation regulates binding to microRNAs during C. elegans development.
Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Decoding Argonaute specificity: insights fromRNA (New York, N.Y.) · 2026Review
- RG motifs promote piRNA-mediated gene silencing in C. elegans.Nucleic acids research · 2025Article
- Dipeptidyl peptidase DPF-3 is a gatekeeper of microRNA Argonaute compensation in animals.Nature communications · 2025Article
- Interaction between a J-domain co-chaperone and a specific Argonaute protein contributes to microRNA function in animals.Nucleic acids research · 2024Article
- Defining the contribution of microRNA-specific Argonautes with slicer capability in animals.Nucleic acids research · 2024Article
- An RNAi screen for conserved kinases that enhance microRNA activity after dauer in Caenorhabditis elegans.G3 (Bethesda, Md.) · 2024Article
- Recent advances in understanding microRNA function and regulation in C. elegans.Seminars in cell & developmental biology · 2024Review
- HRDE-2 drives small RNA specificity for the nuclear Argonaute protein HRDE-1.Nature communications · 2024Article
- Casein kinase 1 and 2 phosphorylate Argonaute proteins to regulate miRNA-mediated gene silencing.EMBO reports · 2023Article
- Small regulatory RNAs: from bench to bedside - a keystone symposia meeting report.RNA biology · 2023Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 4 countries.
Funding
Abstract
Argonaute proteins are at the core of the microRNA-mediated gene silencing pathway essential for animals. In C. elegans, the microRNA-specific Argonautes ALG-1 and ALG-2 regulate multiple processes required for proper animal developmental timing and viability. Here we identified a phosphorylation site on ALG-1 that modulates microRNA association. Mutating ALG-1 serine 642 into a phospho-mimicking residue impairs microRNA binding and causes embryonic lethality and post-embryonic phenotypes that are consistent with alteration of microRNA functions. Monitoring microRNA levels in alg-1 phosphorylation mutant animals shows that microRNA passenger strands increase in abundance but are not preferentially loaded into ALG-1, indicating that the miRNA binding defects could lead to microRNA duplex accumulation. Our genetic and biochemical experiments support protein kinase A (PKA) KIN-1 as the putative kinase that phosphorylates ALG-1 serine 642. Our data indicate that PKA triggers ALG-1 phosphorylation to regulate its microRNA association during C. elegans development.
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Registered trials
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