ArticlePLoS genetics2012
The Drosophila melanogaster seminal fluid protease "seminase" regulates proteolytic and post-mating reproductive processes.
Article in PLoS genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 165 citations in OpenAlex.
- Male-derived PBP4 is essential for sperm competition by mediating sperm motility in moths.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Gene age shapes functional and evolutionary properties of theProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Maturation of Eupyrene Sperm upon Ejaculation Is Influenced by a Male Accessory Gland-Derived Serine Protease inInsects · 2025Article
- An orphan gene is essential for efficient sperm entry into eggs in Drosophila melanogaster.Genetics · 2025Article
- An orphan gene is essential for efficient sperm entry into eggs inbioRxiv : the preprint server for biology · 2024Article
- The seminal odorant binding protein Obp56g is required for mating plug formation and male fertility ineLife · 2023Article
- SPSL1 is essential for spermatophore formation and sperm activation in Spodoptera frugiperda.PLoS genetics · 2023Article
- Knockout ofInternational journal of molecular sciences · 2023Article
- Review
- Genome-Wide Analysis ofInternational journal of molecular sciences · 2023Article
- Female factors modulate Sex Peptide's association with sperm in Drosophila melanogaster.BMC biology · 2022Article
- On how to identify a seminal fluid protein: A commentary on Hurtado et al.Insect molecular biology · 2022Article
- CRISPR/Cas9 Mediated Disruption of Seminal Fluid Protein Sfp62 Induces Male Sterility inBiology · 2022Article
- The life history ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Seminal fluid gene expression and reproductive fitness in Drosophila melanogaster.BMC ecology and evolution · 2022Article
- Single-nucleus transcriptomes reveal evolutionary and functional properties of cell types in the Drosophila accessory gland.Genetics · 2022Article
- Structural and evolutionary insights into astacin metallopeptidases.Frontiers in molecular biosciences · 2022Article
- Discovering novel reproductive genes in a non-model fly usingFrontiers in genetics · 2022Article
- CRISPR/Cas9-mediatedFrontiers in physiology · 2022Article
- Proteolysis in Reproduction: Lessons From Gene-Modified Organism Studies.Frontiers in endocrinology · 2022Review
13 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Proteases and protease inhibitors have been identified in the ejaculates of animal taxa ranging from invertebrates to mammals and form a major protein class among Drosophila melanogaster seminal fluid proteins (SFPs). Other than a single protease cascade in mammals that regulates seminal clot liquefaction, no proteolytic cascades (i.e. pathways with at least two proteases acting in sequence) have been identified in seminal fluids. In Drosophila, SFPs are transferred to females during mating and, together with sperm, are necessary for the many post-mating responses elicited in females. Though several SFPs are proteolytically cleaved either during or after mating, virtually nothing is known about the proteases involved in these cleavage events or the physiological consequences of proteolytic activity in the seminal fluid on the female. Here, we present evidence that a protease cascade acts in the seminal fluid of Drosophila during and after mating. Using RNAi to knock down expression of the SFP CG10586, a predicted serine protease, we show that it acts upstream of the SFP CG11864, a predicted astacin protease, to process SFPs involved in ovulation and sperm entry into storage. We also show that knockdown of CG10586 leads to lower levels of egg laying, higher rates of sexual receptivity to subsequent males, and abnormal sperm usage patterns, processes that are independent of CG11864. The long-term phenotypes of females mated to CG10586 knockdown males are similar to those of females that fail to store sex peptide, an important elicitor of long-term post-mating responses, and indicate a role for CG10586 in regulating sex peptide. These results point to an important role for proteolysis among insect SFPs and suggest that protease cascades may be a mechanism for precise temporal regulation of multiple post-mating responses in females.
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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.