ArticleAnimal bioscience2025
Intracellular domain of CATSPER1 could serve as a cytoplasmic platform for redox processes in mammalian sperm.
Article in Animal bioscience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- CATSPERε extracellular domains are essential for sperm calcium channel assembly and activity modulation.Science advances · 2026Article
- Calcium Channels and Modulators as Potential Therapeutic Targets for Contraceptives and Male Fertility: A Scoping Review.Open access journal of contraception · 2025Review
- A comparative study of capacitation-mediated changes in whole mouse sperm proteome.Animal cells and systems · 2025Article
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2 authors.
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Abstract
objectiveMammalian sperm acquire fertilizing ability in the female reproductive tract and develop hyperactivated motility, which is indispensable for male fertility. Hyperactivated motility is initiated by Ca2+ influx via the sperm-specific ion channel, CatSper. CATSPER1, a CatSper pore subunit, possesses a long N-terminal intracellular domain and its degradation correlates with unsuccessful sperm migration in the female tract. However, the cellular function and molecular significance of the CATSPER1 N-terminal domain are not well understood. Here, we identify the interactome of the CATSPER1 N-terminal domain and propose a function for the intracellular domain in mammalian sperm.
methodsTo identify CATSPER1 N-terminus interactome, we produced recombinant CATSPER1-N-terminus in bacterial system. The purified protein was incubated with testicular lysates and eluted together with testicular interacting proteins. The elutes were subjected to proteomic analysis and CATSPER1-N-terminus interactome was profiled. Identified proteins were further analyzed by functional annotation.
resultsWe purified the partial CATSPER1 N-terminal domain and identified 57 testicular proteins as domain interactomes using mass spectrometry analysis. Functional annotation analysis revealed that 106 gene ontologies were significantly enriched, 16 of which were related to redox processes. We found that antioxidant enzymes, such as PARK7 and PRDX2, 4, and 6, were included in the enriched redox-related gene ontologies.
conclusionThese results suggest that the CATSPER1 N-terminus could function in defending against oxidative stress to support the successful migration of mammalian sperm to fertilizing sites in the female reproductive tract.
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