ArticleMolecular and cellular biology2010
Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3 ligase specificity receptors.
Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- Essential functions of RNA helicase Vasa in maintaining germline stem cells and piRNA-guidedFrontiers in cell and developmental biology · 2024Article
- A conserved node in the regulation of Vasa between an induced and an inherited program of primordial germ cell specification.Developmental biology · 2022Article
- An Interaction Network of RNA-Binding Proteins Involved inMolecular & cellular proteomics : MCP · 2020Article
- FBXO45-MYCBP2 regulates mitotic cell fate by targeting FBXW7 for degradation.Cell death and differentiation · 2020Article
- TheFrontiers in physiology · 2020Article
- Article
- 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
- An unregulated regulator: Vasa expression in the development of somatic cells and in tumorigenesis.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
- SPSB1, a Novel Negative Regulator of the Transforming Growth Factor-β Signaling Pathway Targeting the Type II Receptor.The Journal of biological chemistry · 2015Article
- Analysis of RNA Interference Lines Identifies New Functions of Maternally-Expressed Genes Involved in Embryonic Patterning in Drosophila melanogaster.G3 (Bethesda, Md.) · 2015Article
- In vivo mapping of the functional regions of the DEAD-box helicase Vasa.Biology open · 2015Article
- The biology of the germ line in echinoderms.Molecular reproduction and development · 2014Review
- Protein degradation machinery is present broadly during early development in the sea urchin.Gene expression patterns : GEP · 2014Article
- Piwi regulates Vasa accumulation during embryogenesis in the sea urchin.Developmental dynamics : an official publication of the American Association of Anatomists · 2014Article
- Maternal loss of miRNAs leads to increased variance in primordial germ cell numbers in Drosophila melanogaster.G3 (Bethesda, Md.) · 2013Article
- Structure and function of the SPRY/B30.2 domain proteins involved in innate immunity.Protein science : a publication of the Protein Society · 2013Review
- Post-translational regulation by gustavus contributes to selective Vasa protein accumulation in multipotent cells during embryogenesis.Developmental biology · 2011Article
- Small micromeres contribute to the germline in the sea urchin.Development (Cambridge, England) · 2011Article
- A conserved germline multipotency program.Development (Cambridge, England) · 2010Article
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 3 countries.
Funding
Abstract
In Drosophila species, molecular asymmetries guiding embryonic development are established maternally. Vasa, a DEAD-box RNA helicase, accumulates in the posterior pole plasm, where it is required for embryonic germ cell specification. Maintenance of Vasa at the posterior pole requires the deubiquitinating enzyme Fat facets, which protects Vasa from degradation. Here, we found that Gustavus (Gus) and Fsn, two ubiquitin Cullin-RING E3 ligase specificity receptors, bind to the same motif on Vasa through their paralogous B30.2/SPRY domains. Both Gus and Fsn accumulate in the pole plasm in a Vasa-dependent manner. Posterior Vasa accumulation is precocious in Fsn mutant oocytes; Fsn overexpression reduces ovarian Vasa levels, and embryos from Fsn-overexpressing females form fewer primordial germ cells (PGCs); thus, Fsn destabilizes Vasa. In contrast, endogenous Gus may promote Vasa activity in the pole plasm, as gus females produce embryos with fewer PGCs, and posterior accumulation of Vas is delayed in gus mutant oocytes that also lack one copy of cullin-5. We propose that Fsn- and Gus-containing E3 ligase complexes contribute to establishing a fine-tuned steady state of Vasa ubiquitination that influences the kinetics of posterior Vasa deployment.
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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.