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SUMO2 modification of Aurora B and its impact on follicular development and atresia in the mouse ovary.


ABSTRACT: In the mammalian ovary, >99% follicles fail to ovulate due to apoptosis in granulosa cells. Aurora B, a core subunit enzyme of the chromosomal passenger complex, exerts a crucial role in microtubule‑kinetochore attachment, and has been reported to be modified by small ubiquitin‑related modifier (SUMO) proteins. However, the details of how Aurora B and its SUMOylation impact on follicular development have yet to be fully elucidated. The aim of the present study was to explore the roles, and possible molecular mechanism, of Aurora B and its SUMOylation in the granulosa cells of the mouse follicle. It was revealed that the protein level of Aurora B increased with follicular development and the growth of the granulosa cells. Aurora B impacted follicular development and atresia through mediating the p38 mitogen‑activated protein kinase and FasL/Fas pathways, and caused the downregulation of cyclin‑dependent kinase 4, proliferating cell nuclear antigen, Bcl‑2, and upregulation of caspases‑3 and ‑8 to modulate the viability of the granulosa cells. In addition, Aurora B undergoes modification by SUMO2, but not by SUMO1, in vivo and in vitro, and Lys‑207 is a major modification site. SUMOylation modulates follicular development through an increase in Aurora B localization in the nucleus, and by stabilizing the protein level of Aurora B and keeping the viability of the granulosa cells. Taken together, Aurora B and its SUMOylation are important for follicular development and atresia in the ovaries of mice.

SUBMITTER: Cao J 

PROVIDER: S-EPMC5881745 | BioStudies | 2018-01-01

SECONDARY ACCESSION(S): NM_011496.2

REPOSITORIES: biostudies

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