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© The Rockefeller University Press, 0021-9525/2000//1377 $5.00
The Journal of Cell Biology, Volume 149, Number 7, , 2000 1377-1390

Original Article

Phosphorylation by Cdc28 Activates the Cdc20-Dependent Activity of the Anaphase-Promoting Complex



Adam D. Rudnera,b and Andrew W. Murraya,b

a Department of Physiology, University of California, San Francisco, California 94143-0444
b Department of Biochemistry, University of California, San Francisco, California 94143-0444
University of California, San Francisco, Department of Physiology, Box 0444, 513 Parnassus Avenue, San Francisco, CA 94143-0444.(415) 476-4929(415) 476-0364

amurray{at}cgl.ucsf.edu

Budding yeast initiates anaphase by activating the Cdc20-dependent anaphase-promoting complex (APC). The mitotic activity of Cdc28 (Cdk1) is required to activate this form of the APC, and mutants that are impaired in mitotic Cdc28 function have difficulty leaving mitosis. This defect can be explained by a defect in APC phosphorylation, which depends on mitotic Cdc28 activity in vivo and can be catalyzed by purified Cdc28 in vitro. Mutating putative Cdc28 phosphorylation sites in three components of the APC, Cdc16, Cdc23, and Cdc27, makes the APC resistant to phosphorylation both in vivo and in vitro. The nonphosphorylatable APC has normal activity in G1, but its mitotic, Cdc20-dependent activity is compromised. These results show that Cdc28 activates the APC in budding yeast to trigger anaphase. Previous reports have shown that the budding yeast Cdc5 homologue, Plk, can also phosphorylate and activate the APC in vitro. We show that, like cdc28 mutants, cdc5 mutants affect APC phosphorylation in vivo. However, although Cdc5 can phosphorylate Cdc16 and Cdc27 in vitro, this in vitro phosphorylation does not occur on in vivo sites of phosphorylation.

Key Words: mitosis • budding yeast • Cdc5 • Cks1 • Pds1

© 2000 The Rockefeller University Press

Abbreviations used in this paper: APC, anaphase-promoting complex; Cdk, cyclin-dependent kinase; HU, hydroxyurea; PP1, protein phosphatase 1; PP2A, protein phosphatase 2A.


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