biostudies-literatureUnknown46(1)Han TTThe proteasome, an evolutionarily conserved proteolytic complex comprising the 20S core particle and 19S regulatory particles, performs both shared and distinct functions across various tissues and organs. Spermatogenesis, a highly complex developmental process, relies on proteasome activity at multiple stages to regulate protein turnover. In this study, we selected the 20S subunit PSMA1 and 19S regulatory subunit PSMD2 to investigate the potential functions of the proteasome in spermatogenesis. Using <i>Psma1-EGFP</i> and <i>Psmd2-mCherry</i> knock-in mouse models, we confirmed the expression of both subunits in all spermatogenic cell types, with pronounced presence in early germ cell development. To further clarify their functional significance, we specifically knocked out <i>Psma1</i> aZoological research27-40https://www.ebi.ac.uk/biostudies/studies/S-EPMC11891003biostudies-literatureBoth 20S and 19S proteasome components are essential for meiosis in male mice.PMC11891003Li WMa YJZhou QXChen YHWang LYWei WLiu CJu ZYHan TTfalseBoth 20S and 19S proteasome components are essential for meiosis in male mice.The proteasome, an evolutionarily conserved proteolytic complex comprising the 20S core particle and 19S regulatory particles, performs both shared and distinct functions across various tissues and organs. Spermatogenesis, a highly complex developmental process, relies on proteasome activity at multiple stages to regulate protein turnover. In this study, we selected the 20S subunit PSMA1 and 19S regulatory subunit PSMD2 to investigate the potential functions of the proteasome in spermatogenesis. Using <i>Psma1-EGFP</i> and <i>Psmd2-mCherry</i> knock-in mouse models, we confirmed the expression of both subunits in all spermatogenic cell types, with pronounced presence in early germ cell development. To further clarify their functional significance, we specifically knocked out <i>Psma1</i> a2025-01-01T00:00:00Z2025 Jan2026-06-01T20:13:43.822Z2025-04-07T07:50:52.456ZS-EPMC118910033975701810.24272/j.issn.2095-8137.2024.281