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Molecular and Cellular Biology, July 2003, p. 5018-5030, Vol. 23, No. 14
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.14.5018-5030.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Mitotic Exit Regulation through Distinct Domains within the Protein Kinase Cdc15

Allison J. Bardin, Monica G. Boselli, and Angelika Amon^*

Center for Cancer Research, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Received 3 December 2002/ Returned for modification 21 January 2003/ Accepted 2 May 2003

The mitotic exit network (MEN), a Ras-like signaling cascade, promotes the release of the protein phosphatase Cdc14 from the nucleolus and is essential for cells to exit from mitosis in Saccharomyces cerevisiae. We have characterized the functional domains of one of the MEN components, the protein kinase Cdc15, and investigated the role of these domains in mitotic exit. We show that a region adjacent to Cdc15's kinase domain is required for self-association and for binding to spindle pole bodies and that this domain is essential for CDC15 function. Furthermore, we find that overexpression of CDC15 lacking the C-terminal 224 amino acids results in hyperactivation of MEN and premature release of Cdc14 from the nucleolus, suggesting that this domain within Cdc15 functions to inhibit MEN signaling. Our findings indicate that multiple modes of MEN regulation occur through the protein kinase Cdc15.

Present address: Ecole Normale Superieure, CNRS UMR 8542, 75230 Paris Cedex 05, France.

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