The E3 ubiquitin ligase RNF114 and TAB1 degradation are required for maternal‐to‐zygotic transition |
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| Authors: | Liying Wang Yujiao Liu Yongliang Shang Mingrui Li Shuai Zhou Yuanting Wang Wentao Zeng Jianli Zhou Ran Huo Wei Li |
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| Institution: | 1. State Key Laboratory of Stem Cell and Reproductive Biology, Institute of Zoology, the Chinese Academy of Science, Beijing, China;2. State Key Laboratory of Reproductive Medicine, Department of Histology and Embryology, Nanjing Medical University, Nanjing, China;3. Animal Core Facility, Nanjing Medical University, Nanjing, China |
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| Abstract: | The functional role of the ubiquitin‐proteasome pathway during maternal‐to‐zygotic transition (MZT) remains to be elucidated. Here we show that the E3 ubiquitin ligase, Rnf114, is highly expressed in mouse oocytes and that knockdown of Rnf114 inhibits development beyond the two‐cell stage. To study the underlying mechanism, we identify its candidate substrates using a 9,000‐protein microarray and validate them using an in vitro ubiquitination system. We show that five substrates could be degraded by RNF114‐mediated ubiquitination, including TAB1. Furthermore, the degradation of TAB1 in mouse early embryos is required for MZT, most likely because it activates the NF‐κB pathway. Taken together, our study uncovers that RNF114‐mediated ubiquitination and degradation of TAB1 activate the NF‐κB pathway during MZT, and thus directly link maternal clearance to early embryo development. |
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| Keywords: | maternal‐to‐zygotic transition NF‐κ B pathway RNF114 TAB1 two‐cell‐stage arrest |
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