ArticleNature communications2023
Bombyx Vasa sequesters transposon mRNAs in nuage via phase separation requiring RNA binding and self-association.
Article in Nature communications, 2023. 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, 9 citations in OpenAlex.
- Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins.Nature communications · 2026Article
- Article
- Developmental expression of Ap-Vas proteins in aphids and flies reveals their evolutionary roles in insects.Insect molecular biology · 2026Article
- Germline factors, TDRD and Piwi, colocalize with Vasa on the mitotic apparatus during the embryogenesis of the sea urchin.Developmental biology · 2025Article
- piRNA processing within non-membrane structures is governed by constituent proteins and their functional motifs.The FEBS journal · 2025Review
- A model that integrates the different piRNA biogenesis pathways based on studies in silkwormCurrent research in insect science · 2025Review
- How germ granules promote germ cell fate.Nature reviews. Genetics · 2024Review
- Essential functions of RNA helicase Vasa in maintaining germline stem cells and piRNA-guidedFrontiers in cell and developmental biology · 2024Article
- RNA Helicase Vasa as a Multifunctional Conservative Regulator of Gametogenesis in Eukaryotes.Current issues in molecular biology · 2023Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bombyx Vasa (BmVasa) assembles non-membranous organelle, nuage or Vasa bodies, in germ cells, known as the center for Siwi-dependent transposon silencing and concomitant Ago3-piRISC biogenesis. However, details of the body assembly remain unclear. Here, we show that the N-terminal intrinsically disordered region (N-IDR) and RNA helicase domain of BmVasa are responsible for self-association and RNA binding, respectively, but N-IDR is also required for full RNA-binding activity. Both domains are essential for Vasa body assembly in vivo and droplet formation in vitro via phase separation. FAST-iCLIP reveals that BmVasa preferentially binds transposon mRNAs. Loss of Siwi function derepresses transposons but has marginal effects on BmVasa-RNA binding. This study shows that BmVasa assembles nuage by phase separation via its ability to self-associate and bind newly exported transposon mRNAs. This unique property of BmVasa allows transposon mRNAs to be sequestered and enriched in nuage, resulting in effective Siwi-dependent transposon repression and Ago3-piRISC biogenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.