Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 23, Issue 14, Pages 5018-5030Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.23.14.5018-5030.2003
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Funding
- NIGMS NIH HHS [GM 56800, R01 GM056800, R29 GM056800] Funding Source: Medline
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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.
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