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Mol. Cells 2013; 35(6): 514-518

Published online June 30, 2013

https://doi.org/10.1007/s10059-013-0029-6

© The Korean Society for Molecular and Cellular Biology

Cdc25B Phosphatase Participates in Maintaining Metaphase II Arrest in Mouse Oocytes

Hyoeun Kang, Seok Cheol Hwang, Yong Seok Park, and Jeong Su Oh

Department of Genetic Engineering, College of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon 440-746, Korea, 2These authors contributed equally to this work

Received: January 28, 2013; Revised: April 4, 2013; Accepted: April 5, 2013

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.

Keywords Cdc25B, meiosis, metaphase II (MII) arrest, MPF, oocyte

Article

Research Article

Mol. Cells 2013; 35(6): 514-518

Published online June 30, 2013 https://doi.org/10.1007/s10059-013-0029-6

Copyright © The Korean Society for Molecular and Cellular Biology.

Cdc25B Phosphatase Participates in Maintaining Metaphase II Arrest in Mouse Oocytes

Hyoeun Kang, Seok Cheol Hwang, Yong Seok Park, and Jeong Su Oh

Department of Genetic Engineering, College of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon 440-746, Korea, 2These authors contributed equally to this work

Received: January 28, 2013; Revised: April 4, 2013; Accepted: April 5, 2013

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.

Keywords: Cdc25B, meiosis, metaphase II (MII) arrest, MPF, oocyte

Mol. Cells
Jun 30, 2022 Vol.45 No.6, pp. 353~434
COVER PICTURE
ERα is modified by UFM1 and this modification (ufmylation) plays a crucial role in promoting the stability of ERα and breast cancer development. However, when ERα is deufmylated and then ubiquitinated, it disappears by proteasome-mediated degradation (Yoo et al., pp. 425-434).

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