ArticleCommunications biology2024
FBXO47 regulates centromere pairing as key component of centromeric SCF E3 ligase in mouse spermatocytes.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Testis-Enriched F-Box Protein FBXO39 Is Important for Spermiogenesis and Male Fertility in Mice.Andrology · 2026Article
- CRISPR/Cas9-mediated genome editing identifies six testis-expressed genes individually dispensable for overt male fecundity in mice.Journal of biomedical research · 2026Article
- Hsa-circ_0081481-miR 3960-FBXO24 regulatory axis in non-obstructive azoospermia identifies potential biomarkers of spermatogenic failure.Scientific reports · 2026Article
- ZCWPW1 organizes telomeric architecture to drive meiotic chromosome movements.bioRxiv : the preprint server for biology · 2026Article
- Loss of E3 ligase HvST1 function substantially increases distal crossover frequency.The New phytologist · 2026Article
- Mutation Severity ofHuman mutation · 2026Article
- Rewiring for movements in meiotic prophase: regulators, roles, and evolutionary pathways.Current opinion in genetics & development · 2025Review
- Genomic Landscape of Breast Cancer: Study Across Diverse Ethnic Groups.Diseases (Basel, Switzerland) · 2025Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Centromere pairing is crucial for synapsis in meiosis. This study delves into the Skp1-Cullin1-F-box protein (SCF) E3 ubiquitin ligase complex, specifically focusing on F-box protein 47 (FBXO47), in mouse meiosis. Here, we revealed that FBXO47 is localized at the centromere and it regulates centromere pairing cooperatively with SKP1 to ensure proper synapsis in pachynema. The absence of FBXO47 causes defective centromeres, resulting in incomplete centromere pairing, which leads to corruption of SC at centromeric ends and along chromosome axes, triggering premature dissociation of chromosomes and pachytene arrest. FBXO47 deficient pachytene spermatocytes exhibited drastically reduced SKP1 expression at centromeres and chromosomes. Additionally, FBXO47 stabilizes SKP1 by down-regulating its ubiquitination in HEK293T cells. In essence, we propose that FBXO47 collaborates with SKP1 to facilitate centromeric SCF formation in spermatocytes. In summary, we posit that the centromeric SCF E3 ligase complex regulates centromere pairing for pachynema progression in mice.
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