Cdc25B phosphatase participates in maintaining metaphase II arrest in mouse oocytes |
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Authors: | Hyoeun Kang Seok Cheol Hwang Yong Seok Park Jeong Su Oh |
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Affiliation: | 129. Department of Genetic Engineering, College of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon, 440-746, Korea
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Abstract: | Cdc25B is an essential regulator for meiotic resumption in mouse oocytes. However, the role of this phosphatase during the later stage of the meiotic cell cycle is not known. In this study, we investigated the role of Cdc25B during metaphase II (MII) arrest in mouse oocytes. Cdc25B was extensively phosphorylated during MII arrest with an increase in the phosphatase activity toward Cdk1. Downregulation of Cdc25B by antibody injection induced the formation of a pronucleus-like structure. Conversely, overexpression of Cdc25B inhibited Ca2+-mediated release from MII arrest. Moreover, Cdc25B was immediately dephosphorylated and hence inactivated during MII exit, suggesting that Cdk1 phosphorylation is required to exit from MII arrest. Interestingly, this inactivation occurred prior to cyclin B degradation. Taken together, our data demonstrate that MII arrest in mouse oocytes is tightly regulated not only by the proteolytic degradation of cyclin B but also by dynamic phosphorylation of Cdk1. |
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Keywords: | Cdc25B meiosis metaphase II (MII) arrest MPF oocyte |
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