Language
English
Publication Date
5-13-2025
Journal
Biology of Reproduction
DOI
10.1093/biolre/ioaf035
PMID
39982420
PMCID
PMC13017552
PubMedCentral® Posted Date
2-21-2025
PubMedCentral® Full Text Version
Post-print
Abstract
The conjugation of small ubiquitin-like modifiers (SUMO) to target proteins, known as SUMOylation, plays a crucial role in regulating protein homeostasis, activity, interaction with other proteins, and subcellular localization. Loss of SUMOylation in nongrowing oocytes by conditional deletion of the E2 SUMO conjugating enzyme, Ube2i, at the primordial follicle stage leads to female sterility due to complex changes in oocyte development, including altered folliculogenesis, defective meiotic progression, and premature loss of the ovarian reserve. In this study, proteomics was used to compare control and Ube2i conditional knockout ovaries during the first wave of folliculogenesis to identify key differences that may drive the premature follicle loss phenotype. Label-free mass spectrometry results showed that 238 proteins were significantly altered more than 2-fold (p < 0.05). Proteins upregulated in the Ube2i conditional knockout ovaries included those involved in mRNA splicing and WNT signaling, while those downregulated were related to metabolism, mitochondria, and the maternal effect proteins NLRP2 and NLRP9B. The majority of differentially expressed proteins showed no change by transcriptome analysis, indicating protein level regulation and revealing potential SUMOylation targets with necessary roles in oocyte and follicle development.
Keywords
Animals, Female, Oocytes, Sumoylation, Mice, Ovarian Follicle, Mice, Knockout, Ubiquitin-Conjugating Enzymes, Oogenesis, folliculogenesis, infertility, posttranslational protein modification, proteomics, ovary, SUMOylation
Published Open-Access
yes
Recommended Citation
Liao, Zian; Steenwinkel, Tessa E; Moscoso, Bruno; et al., "Disruption of Oocyte SUMOylation Impacts Critical Regulatory Processes During Folliculogenesis in Mice" (2025). Faculty, Staff and Students Publications. 6541.
https://digitalcommons.library.tmc.edu/baylor_docs/6541
Graphical Abstract