GEOapplication/xmlftp://ftp.ncbi.nlm.nih.gov/geo/series/GSE293nnn/GSE293047/primaryOK200TranscriptomicsMus musculusExpression profiling by high throughput sequencinghttps://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE293047GEOGSEfalse20S proteasomes are required for ELVAs-mediated protein degradation during oocyte-to-embryo transition and agingThe degradation of maternal factors is essential for oocyte-to-embryo transition (OET). While extensive research has focused on maternal mRNA degradation, the mechanisms underlying maternal protein degradation remain poorly understood. ELVAs, the oocyte-specific membraneless structure which comprises proteasomes, endolysosomes and autophagosomes, are required for protein degradation in maturing oocytes and zygotes. In this study, we embloyed oocyte-specific Psma7 knockout, targeting the α4 subunit of 20S proteasome, to investigate the physiological function of proteasomes in ELVAs-mediated protein degradation. PSMA7-deficiency destabilizes 20S proteasome components and disrupts ELVAs assembly and spatial organization, resulting in the accumulation of ubiquitinated proteins in both oocytes and zygotes. Consequently, maternal PSMA7-deletion results in female infertility, manifested by impaired oocyte maturation and developmental arrest at the 1- to 2-cell stage. Furthermore, in oocytes from both aged mice and women, reduced proteasome abundance and aberrations in ELVAs distribution and activity were found, providing a mechanistic explanation for the diminished developmental competence aged oocytes. Taken together, our findings elucidate the critical function of proteasome-regulated proteostasis in oocyte quality control during OET and reproductive aging in females.2026/04/27GSE293047GSM8874510GSM8874511GSM8874500GSM8874505GSM8874506GSM8874507GSM8874508GSM8874512GSM8874501GSM8874502GSM8874513GSM8874514GSM8874503GSM8874515GSM8874504GSM887450924247293047Mus musculus