Proteomic Profiling Reveals the Molecular Control of Oocyte Maturation

Meiotic maturation is an intricate and precisely regulated process orchestrated by various pathways and numerous proteins. However, little is known about the proteome landscape during oocytes maturation. Here, we obtained the temporal proteomic profiles of mouse oocytes during in vivo maturation. We successfully quantified 4694 proteins from 4500 oocytes in three key stages (germinal vesicle, germinal vesicle breakdown, and metaphase II). In particular, we discovered the novel proteomic features during oocyte maturation, such as the active Skp1–Cullin–Fbox pathway and an increase in mRNA decay–related proteins. Using functional approaches, we further identified the key factors controlling the histone acetylation state in oocytes and the vital proteins modulating meiotic cell cycle. Taken together, our data serve as a broad resource on the dynamics occurring in oocyte proteome and provide important knowledge to better understand the molecular mechanisms during germ cell development. [Display omitted] •In vivo quantitative and comparative analysis performed for mouse oocytes.•CEP57L1 plays important roles for assembly of meiotic apparatus.•SIN3A modulates histone deacetylation during oocyte maturation.•mRNA metabolism is active in MII oocytes.•Fbxo28 participates in substrates degradation in oocytes. Using TMT-based LC-MS/MS, we systematically performed a quantitative proteomic analysis of GV, GVBD, and MII oocytes. We successfully quantified 4694 proteins from 4500 oocytes in three key stages. By combining bioinformatics analysis with functional approaches, our results showed the protein kinetics and molecular mechanisms during meiotic maturation.