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Vol. 15, Issue 12, 5623-5634, December 2004
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TrCP-dependent Destruction of the APC Inhibitor Emi1
Department of Pathology, Stanford University School of Medicine, Palo Alto, CA 94305
Submitted July 16, 2004;
Revised September 1, 2004;
Accepted September 29, 2004
Monitoring Editor: Tim Stearns
Progression through mitosis requires activation of cyclin B/Cdk1 and its downstream targets, including Polo-like kinase and the anaphase-promoting complex (APC), the ubiquitin ligase directing degradation of cyclins A and B. Recent evidence shows that APC activation requires destruction of the APC inhibitor Emi1. In prophase, phosphorylation of Emi1 generates a D-pS-G-X-X-pS degron to recruit the SCF
TrCP ubiquitin ligase, causing Emi1 destruction and allowing progression beyond prometaphase, but the kinases directing this phosphorylation remain undefined. We show here that the polo-like kinase Plk1 is strictly required for Emi1 destruction and that overexpression of Plk1 is sufficient to trigger Emi1 destruction. Plk1 stimulates Emi1 phosphorylation, TrCP binding, and ubiquitination in vitro and cyclin B/Cdk1 enhances these effects. Plk1 binds to Emi1 in mitosis and the two proteins colocalize on the mitotic spindle poles, suggesting that Plk1 may spatially control Emi1 destruction. These data support the hypothesis that Plk1 activates the APC by directing the SCF-dependent destruction of Emi1 in prophase.
Abbreviations used: APC, anaphase promoting complex; MPF, mitosis promoting factor; Plk1, Polo-like kinase 1; Plx1, Xenopus polo-like kinase 1; PBD, Polo Box domain.
* Corresponding author. E-mail address: pjackson{at}stanford.edu.
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