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The E3 ubiquitin ligase RNF 114 and TAB 1 degradation are required for maternal‐to‐zygotic transition
Author(s) -
Yang Ye,
Zhou Cheng,
Wang Ying,
Liu Weixiao,
Liu Chao,
Wang Liying,
Liu Yujiao,
Shang Yongliang,
Li Mingrui,
Zhou Shuai,
Wang Yuanting,
Zeng Wentao,
Zhou Jianli,
Huo Ran,
Li Wei
Publication year - 2017
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201642573
Subject(s) - china , stem cell biology , beijing , reproductive biology , library science , biology , reproductive technology , political science , genetics , law , embryo , computer science , embryogenesis
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 RNF 114‐mediated ubiquitination, including TAB 1. Furthermore, the degradation of TAB 1 in mouse early embryos is required for MZT , most likely because it activates the NF ‐κB pathway. Taken together, our study uncovers that RNF 114‐mediated ubiquitination and degradation of TAB 1 activate the NF ‐κB pathway during MZT , and thus directly link maternal clearance to early embryo development.