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Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes
Author(s) -
Zhang Yang,
Zhang Zhe,
Xu XiaoYan,
Li XueSong,
Yu Meng,
Yu AiMing,
Zong ZhiHong,
Yu BingZhi
Publication year - 2008
Publication title -
developmental dynamics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.634
H-Index - 141
eISSN - 1097-0177
pISSN - 1058-8388
DOI - 10.1002/dvdy.21799
Subject(s) - germinal vesicle , biology , meiosis , phosphorylation , oocyte , microbiology and biotechnology , cytoplasm , protein kinase a , kinase , embryo , biochemistry , gene
Protein kinase A (PKA) play a critical role in maintaining the meiotic arrest. However, the steps downstream of PKA remain largely unknown. In this study, we investigated the regulation of meiotic resumption by PKA/Cdc25B pathway in mouse oocytes. Injection of mRNA coding for Cdc25b ‐S321A had a more potent maturation‐inducing ability than Cdc25b ‐WT. When co‐injected with PKA inhibitor, Cdc25B‐WT had similar activities with Cdc25B‐S321A. Meanwhile, the phosphorylation of Cdc25B‐S321 was detected in germinal vesicle (GV) oocytes by Western blotting with a phospho‐Ser321‐specific antibody and the band disappeared when oocytes reenter into the meiotic cell cycle. Furthermore, Cdc25B‐WT translocated to the nucleus shortly before GV breakdown (GVBD), whereas phosphorylated Cdc25B‐S321 expressed exclusively in the cytoplasm and the signal could not be detected in GVBD oocytes. Taken together, these data indicate that Cdc25B‐Serine321 is the potential PKA target and Cdc25B subcellular localization determines its function during the process of maintaining GV arrest in mouse oocytes. Developmental Dynamics 237:3777–3786, 2008. © 2008 Wiley‐Liss, Inc.