ArticleBiology open2015
In vivo mapping of the functional regions of the DEAD-box helicase Vasa.
Article in Biology open, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins.Nature communications · 2026Article
- Conserved RNA helicase Vasa regulates ribonucleoprotein condensate dynamics and mRNA localization.iScience · 2026Article
- Article
- Combinatorial tagging generates a multi-purpose knock-in mouse model revealing phase separation-dependent germ granules in RNA homeostasis and germline development.Cell death and differentiation · 2025Article
- Review
- 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
- Vasa, a regulator of localized mRNA translation on the spindle.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Review
- Building RNA-protein germ granules: insights from the multifaceted functions of DEAD-box helicase Vasa/Ddx4 in germline development.Cellular and molecular life sciences : CMLS · 2021Review
- Article
- Article
- Germ Cell Lineage Homeostasis inGenetics · 2019Article
- piRNA Biogenesis in Drosophila melanogaster.Trends in genetics : TIG · 2017Review
- dFmr1 Plays Roles in Small RNA Pathways of Drosophila melanogaster.International journal of molecular sciences · 2017Review
- The LOTUS domain is a conserved DEAD-box RNA helicase regulator essential for the recruitment of Vasa to the germ plasm and nuage.Genes & development · 2017Article
- C-terminal residues specific to Vasa among DEAD-box helicases are required for its functions in piRNA biogenesis and embryonic patterning.Development genes and evolution · 2016Article
- Loss of function of the Drosophila Ninein-related centrosomal protein Bsg25D causes mitotic defects and impairs embryonic development.Biology open · 2016Article
- An unregulated regulator: Vasa expression in the development of somatic cells and in tumorigenesis.Developmental biology · 2016Review
- Germ Plasm Biogenesis--An Oskar-Centric Perspective.Current topics in developmental biology · 2016Review
- Germ plasm localisation of the HELICc of Vasa in Drosophila: analysis of domain sufficiency and amino acids critical for localisation.Scientific reports · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The maternally expressed Drosophila melanogaster DEAD-box helicase Vasa (Vas) is necessary for many cellular and developmental processes, including specification of primordial germ cells (pole cells), posterior patterning of the embryo, piRNA-mediated repression of transposon-encoded mRNAs, translational activation of gurken (grk) mRNA, and completion of oogenesis itself. Vas protein accumulates in the perinuclear nuage in nurse cells soon after their specification, and then at stage 10 Vas translocates to the posterior pole plasm of the oocyte. We produced a series of transgenic constructs encoding eGFP-Vas proteins carrying mutations affecting different regions of the protein, and analyzed in vivo which Vas functions each could support. We identified novel domains in the N- and C-terminal regions of the protein that are essential for localization, transposon repression, posterior patterning, and pole cell specification. One such functional region, the most C-terminal seven amino acids, is specific to Vas orthologues and is thus critical to distinguishing Vas from other closely related DEAD-box helicases. Surprisingly, we also found that many eGFP-Vas proteins carrying mutations that would be expected to abrogate DEAD-box helicase function localized to the nuage and posterior pole, and retained the capacity to support oogenesis, although they did not function in embryonic patterning, pole cell specification, grk activation, or transposon repression. We conclude from these experiments that Vas, a multifunctional protein, uses different domains and different molecular associations to carry out its various cellular and developmental roles.
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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.