RNF20 Regulates Oocyte Meiotic Spindle Assembly by Recruiting TPM3 to Centromeres and Spindle Poles

Previously a ring finger protein 20 (RNF20) is found to be essential for meiotic recombination and mediates H2B ubiquitination during spermatogenesis. However, its role in meiotic division is still unknown. Here, it is shown that RNF20 is localized at both centromeres and spindle poles, and it is re...

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Published inAdvanced science Vol. 11; no. 13; pp. e2306986 - n/a
Main Authors Wang, Liying, Liu, Chao, Li, Li, Wei, Huafang, Wei, Wei, Zhou, Qiuxing, Chen, Yinghong, Meng, Tie‐Gang, Jiao, Renjie, Wang, Zhen‐Bo, Sun, Qing‐Yuan, Li, Wei
Format Journal Article
LanguageEnglish
Published Germany John Wiley & Sons, Inc 01.04.2024
John Wiley and Sons Inc
Wiley
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Summary:Previously a ring finger protein 20 (RNF20) is found to be essential for meiotic recombination and mediates H2B ubiquitination during spermatogenesis. However, its role in meiotic division is still unknown. Here, it is shown that RNF20 is localized at both centromeres and spindle poles, and it is required for oocyte acentrosomal spindle organization and female fertility. RNF20‐depleted oocytes exhibit severely abnormal spindle and chromosome misalignment caused by defective bipolar organization. Notably, it is found that the function of RNF20 in spindle assembly is not dependent on its E3 ligase activity. Instead, RNF20 regulates spindle assembly by recruiting tropomyosin3 (TPM3) to both centromeres and spindle poles with its coiled‐coil motif. The RNF20‐TPM3 interaction is essential for acentrosomal meiotic spindle assembly. Together, the studies uncover a novel function for RNF20 in mediating TPM3 recruitment to both centromeres and spindle poles during oocyte spindle assembly. It is shown that RNF20 is a key regulator for acentrosomal spindle assembly and first meiosis completion in oocytes. It is found that the RNF20‐TPM3 interaction is essential for acentrosomal meiotic spindle assembly. RNF20 regulates spindle assembly by recruiting TPM3 to centromeres and spindle poles, which is independent on its E3 ligase activity.
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ISSN:2198-3844
2198-3844
DOI:10.1002/advs.202306986