ArticleDevelopment (Cambridge, England)2016
The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm.
Article in Development (Cambridge, England), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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.
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Who cites it
50 citing papers in PubMed, 99 citations in OpenAlex.
- Ion Channels as Gatekeepers of Fertility: From Uterine Kir7.1 to Sperm CatSper.Physiology (Bethesda, Md.) · 2026Review
- Large cyclic AMP-dependent increases in tyrosine-phosphorylated proteins are not absolutely necessary for the induction of full-type hyperactivation and penetration into eggs in ejaculated boar spermatozoa in vitro.The Journal of reproduction and development · 2026Article
- Mitochondria beyond boundaries: from cellular powerhouses to intercellular messengers in health and disease.Science China. Life sciences · 2026Review
- The Fer Tyrosine Kinase Mediates EGFR Activation in Sperm Capacitation.International journal of molecular sciences · 2025Article
- Time to revise: impact of methodology on boar sperm capacitation in vitro via phosphotyrosine patterns.BMC veterinary research · 2025Review
- Advances in Molecular Biology and Immunology of Spermatozoa and Fertilization in Domestic Animals: Implications for Infertility and Assisted Reproduction.Current molecular medicine · 2025Review
- A comparative study of capacitation-mediated changes in whole mouse sperm proteome.Animal cells and systems · 2025Article
- Increased reproductive outcomes after optimized sperm preparation.Frontiers in cell and developmental biology · 2025Article
- Dual role of valosin-containing protein (VCP/p97) in mouse sperm during capacitation.Reproduction (Cambridge, England) · 2024Article
- Conservation of Protein Kinase A Substrates in the Cnidarian Coral Spermatozoa Among Animals and Their Molecular Evolution.Journal of molecular evolution · 2024Article
- Article
- Mitopherogenesis, a form of mitochondria-specific ectocytosis, regulates sperm mitochondrial quantity and fertility.Nature cell biology · 2023Article
- Hamster Sperm Possess Functional NaInternational journal of molecular sciences · 2023Article
- Fer and FerT: A New Regulatory Link between Sperm and Cancer Cells.International journal of molecular sciences · 2023Review
- Mouse sperm energy restriction and recovery (SER) revealed novel metabolic pathways.Frontiers in cell and developmental biology · 2023Article
- Mutation of S461, in the GOLGA3 phosphorylation site, does not affect mouse spermatogenesis.PeerJ · 2023Article
- PP1, PP2A and PP2B Interplay in the Regulation of Sperm Motility: Lessons from Protein Phosphatase Inhibitors.International journal of molecular sciences · 2022Review
- Mysteries and unsolved problems of mammalian fertilization and related topics.Biology of reproduction · 2022Review
- C2CD6 regulates targeting and organization of the CatSper calcium channel complex in sperm flagella.Development (Cambridge, England) · 2022Article
- Exploring the ovine sperm transcriptome by RNAseq techniques. I Effect of seasonal conditions on transcripts abundance.PloS one · 2022Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
Abstract
Sperm capacitation is required for fertilization. At the molecular level, this process is associated with fast activation of protein kinase A. Downstream of this event, capacitating conditions lead to an increase in tyrosine phosphorylation. The identity of the tyrosine kinase(s) mediating this process has not been conclusively demonstrated. Recent experiments using stallion and human sperm have suggested a role for PYK2 based on the use of small molecule inhibitors directed against this kinase. However, crucially, loss-of-function experiments have not been reported. Here, we used both pharmacological inhibitors and genetically modified mice models to investigate the identity of the tyrosine kinase(s) mediating the increase in tyrosine phosphorylation in mouse sperm. Similar to stallion and human, PF431396 blocks the capacitation-associated increase in tyrosine phosphorylation. Yet, sperm from Pyk2(-/-) mice displayed a normal increase in tyrosine phosphorylation, implying that PYK2 is not responsible for this phosphorylation process. Here, we show that PF431396 can also inhibit FER, a tyrosine kinase known to be present in sperm. Sperm from mice targeted with a kinase-inactivating mutation in Fer failed to undergo capacitation-associated increases in tyrosine phosphorylation. Although these mice are fertile, their sperm displayed a reduced ability to fertilize metaphase II-arrested eggs in vitro.
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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.