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Science 332 (6028): 462-465

Copyright © 2011 by the American Association for the Advancement of Science

Protein Tyrosine Kinase Wee1B Is Essential for Metaphase II Exit in Mouse Oocytes

Jeong Su Oh, Andrej Susor, Marco Conti*

Abstract: Waves of cyclin synthesis and degradation regulate the activity of Cdc2 protein kinase during the cell cycle. Cdc2 inactivation by Wee1B-mediated phosphorylation is necessary for arrest of the oocyte at G2-prophase, but it is unclear whether this regulation functions later during the metaphase-to-anaphase transition. We show that reactivation of a Wee1B pathway triggers the decrease in Cdc2 activity during egg activation. When Wee1B is down-regulated, oocytes fail to form a pronucleus in response to Ca2+ signals. Calcium-calmodulin–dependent kinase II (CaMKII) activates Wee1B, and CaMKII-driven exit from metaphase II is inhibited by Wee1B down-regulation, demonstrating that exit from metaphase requires not only a proteolytic degradation of cyclin B but also the inhibitory phosphorylation of Cdc2 by Wee1B.

Center for Reproductive Sciences and The Eli and Edythe Broad Center of Regeneration Medicine and Stem Cell Research, Department of Obstetrics, Gynecology and Reproductive Sciences, University of California, San Francisco, CA 94143–0556, USA.

* To whom correspondence should be addressed. E-mail: contim{at}obgyn.ucsf.edu


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