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Molecular and Cellular Biology, March 2003, p. 1703-1716, Vol. 23, No. 5
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.5.1703-1716.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Biphasic Activation of Aurora-A Kinase during the Meiosis I- Meiosis II Transition in Xenopus Oocytes

Chunqi Ma,1 Cathy Cummings,1 and X. Johné Liu1,2,3*

Ottawa Health Research Institute, Ottawa Hospital Civic Campus,1 Department of Biochemistry, Microbiology and Immunology,2 Department of Obstetrics and Gynaecology, University of Ottawa, Ottawa, Ontario, Canada3

Received 4 September 2002/ Returned for modification 15 October 2002/ Accepted 9 December 2002

Xenopus Aurora-A (also known as Eg2) is a member of the Aurora family of mitotic serine/threonine kinases. In Xenopus oocytes, Aurora-A phosphorylates and activates a cytoplasmic mRNA polyadenylation factor (CPEB) and therefore plays a pivotal role in MOS translation. However, hyperphosphorylation and activation of Aurora-A appear to be dependent on maturation-promoting factor (MPF) activation. To resolve this apparent paradox, we generated a constitutively activated Aurora-A by engineering a myristylation signal at its N terminus. Injection of Myr-Aurora-A mRNA induced germinal vesicle breakdown (GVBD) with the concomitant activation of MOS, mitogen-activated protein kinase, and MPF. Myr-Aurora-A-injected oocytes, however, appeared to arrest in meiosis I with high MPF activity and highly condensed, metaphase-like chromosomes but no organized microtubule spindles. No degradation of CPEB or cyclin B2 was observed following GVBD in Myr-Aurora-A-injected oocytes. In the presence of progesterone, the endogenous Aurora-A became hyperphosphorylated and activated at the time of MPF activation. Following GVBD, Aurora-A was gradually dephosphorylated and inactivated before it was hyperphosphorylated and activated again. This biphasic pattern of Aurora-A activation mirrored that of MPF activation and hence may explain meiosis I arrest by the constitutively activated Myr-Aurora-A.

* Corresponding author. Mailing address: Ottawa Health Research Institute, 725 Parkdale Ave., Ottawa K1Y 4E9, Canada. Phone: (613) 798-5555, ext. 17752. Fax: (613) 761-5411. E-mail: jliu{at}ohri.ca.

Molecular and Cellular Biology, March 2003, p. 1703-1716, Vol. 23, No. 5
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.5.1703-1716.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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