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Updated: Aug 9, 2025
In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
Published on: November 2, 2017
Post-ovulatory aging is associated with altered patterns for small ubiquitin-like modifier (SUMO) proteins and
Weber Beringui Feitosa1, Patricia L Morris1,2
1Center for Biomedical Research, Population Council, New York, New York, USA.
Abstract:
Mammalian oocytes are ovulated arrested at metaphase of the second meiotic division. If they are not fertilized within a short period, the oocyte undergoes several progressive morphological, structural, and molecular changes during a process called oocyte aging. Herein, we focused on those functional events associated with proper cytoskeleton organization and those that correlate with spindle displacement and chromosome misalignment or scatter. Post-translational modifications by Small Ubiquitin-like Modifier (SUMO) proteins are involved in spindle organization and here we demonstrate that the SUMO pathway is involved in spindle morphology changes and chromosome movements during oocyte aging. SUMO-2/3 as well as the SUMO-specific proteases SENP-2 localization are affected by postovulatory aging in vitro. Consistent with these findings, UBC9 decreases during oocyte aging while differential ubiquitination patterns also correlate with in vitro oocyte aging. These results are consistent with postovulatory aging-related alterations in the posttranslational modifications of the spindle apparatus by SUMO and its SENP proteases. These findings are suggestive that such age-related changes in SUMOylation and the deSUMOylation of key target proteins in the spindle apparatus and kinetochore may be involved with spindle and chromosome alignment defects during mammalian oocyte postovulatory aging. Such findings may have implications for ART-related human oocyte aging in vitro regarding the activities of the SUMO pathway and fertilization success.
Insights
Oocyte aging affects the SUMOylation pathway, impacting spindle organization and chromosome alignment. These changes in Small Ubiquitin-like Modifier (SUMO) modifications may explain age-related defects in mammalian oocytes.
Area of Science:
- Reproductive Biology
- Cell Biology
- Molecular Biology
Background:
- Mammalian oocytes ovulate arrested at metaphase II, susceptible to aging if unfertilized.
- Oocyte aging involves morphological, structural, and molecular changes impacting function.
- Cytoskeleton organization, spindle, and chromosome alignment are critical for oocyte quality.
Purpose of the Study:
- To investigate the role of the SUMOylation pathway in mammalian oocyte aging.
- To examine changes in spindle morphology and chromosome alignment during oocyte aging.
- To determine the impact of post-translational SUMO modifications on oocyte aging and potential ART implications.
Main Methods:
- In vitro culture of mammalian oocytes to induce postovulatory aging.
- Analysis of SUMO-2/3 and SENP-2 protease localization during aging.
- Quantification of UBC9 levels and assessment of ubiquitination patterns.
- Evaluation of spindle organization and chromosome alignment.
Main Results:
- SUMO-2/3 and SENP-2 localization were altered during in vitro oocyte aging.
- UBC9 levels decreased, and differential ubiquitination patterns correlated with aging.
- Age-related changes in SUMOylation and deSUMOylation of spindle/kinetochore proteins were observed.
Conclusions:
- The SUMOylation pathway is implicated in regulating spindle morphology and chromosome movement during oocyte aging.
- Altered SUMOylation/deSUMOylation of key proteins may contribute to spindle and chromosome alignment defects.
- Findings suggest potential implications for the SUMO pathway in human oocyte aging within assisted reproductive technologies (ART).
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