ArticleDevelopment (Cambridge, England)2025
A sperm-oocyte protein partnership required for egg activation in Caenorhabditis elegans.
Article in Development (Cambridge, England), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
5 citing papers in PubMed.
- SPSP-1 is a sperm protein required for C. elegans hermaphrodite sperm production and embryogenesis.Biology open · 2026Article
- Functional requirement for Dicer helicase arginine methylation in 26 G siRNA biogenesis and oocyte meiotic program.Nature communications · 2026Article
- The intrinsically disordered protein SPE-56 is required for acrosomal-like exocytosis and fertility in Caenorhabditis elegans.Scientific reports · 2026Article
- Oocyte surface proteins EGG-1 and EGG-2 are required for eggshell integrity in Caenorhabditis elegans.G3 (Bethesda, Md.) · 2026Article
- Oocyte surface proteins EGG-1 and EGG-2 are required for eggshell integrity inbioRxiv : the preprint server for biology · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Fertilization triggers the completion of female meiosis and launches the oocyte-to-embryo transition. Caenorhabditis elegans spe-11 is one of the few known paternal-effect embryonic lethal genes. We report that the sperm protein SPE-11 forms a complex with an oocyte protein, OOPS-1 (Oocyte Partner of SPE-11) at fertilization, and that the protein complex is required for the completion of meiosis, the block to polyspermy, and eggshell formation. Consistent with the molecular interaction of their encoded proteins, oops-1 and spe-11 exhibit indistinguishable null phenotypes in which fertilized oocytes arrest in meiosis I or meiosis II or fail to complete the actin-based process of meiotic cytokinesis. Biochemical analysis shows that the complex binds F-actin in the absence of other proteins and inhibits the nucleation of actin filaments at substoichiometric concentrations. Both OOPS-1 and SPE-11 are intrinsically disordered proteins that are highly phosphorylated, and biochemical and genetic experiments define interactions with the sperm-specific protein phosphatase 1 homologs GSP-3/4. Genetic results suggest that the cortical EGG complex recruits the OOPS-1-SPE-11 complex at fertilization, which promotes meiotic cytokinesis and in turn activates synthesis of the eggshell.
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Registered trials
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