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Published 20 January 2004. doi:10.1083/jcb.200309035
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 164, Number 2, 233-241
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Article

 Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells

Catherine Lindon and Jonathon Pines

Wellcome Trust/Cancer Research UK Gurdon Institute and Department of Zoology, University of Cambridge, Cambridge CB2 1QR, England, UK

Address correspondence to Jonathon Pines, Wellcome Trust/Cancer Research UK Gurdon Institute, Tennis Court Rd., Cambridge CB2 1QR, England, UK. Tel.: (44) 1223-334-093. Fax: (44) 1223-334-089. email: j.pines{at}welc.cam.ac.uk or Catherine Lindon, Wellcome Trust/Cancer Research UK Gurdon Institute, Tennis Court Rd., Cambridge CB2 1QR, England, UK. Tel.: (44) 1223-334-093. Fax: (44) 1223-334-089. c.lindon{at}welc.cam.ac.uk

We have found that key mitotic regulators show distinct patterns of degradation during exit from mitosis in human cells. Using a live-cell assay for proteolysis, we show that two of these regulators, polo-like kinase 1 (Plk1) and Aurora A, are degraded at different times after the anaphase-promoting complex/cyclosome (APC/C) switches from binding Cdc20 to Cdh1. Therefore, events in addition to the switch from Cdc20 to Cdh1 control the proteolysis of APC/CCdh1 substrates in vivo. We have identified a putative destruction box in Plk1 that is required for degradation of Plk1 in anaphase, and have examined the effect of nondegradable Plk1 on mitotic exit. Our results show that Plk1 proteolysis contributes to the inactivation of Plk1 in anaphase, and that this is required for the proper control of mitotic exit and cytokinesis. Our experiments reveal a role for APC/C-mediated proteolysis in exit from mitosis in human cells.

Key Words: Aurora; cytokinesis; mitosis; APC/C; Cdh1

The online version of this article includes supplemental material.

Abbreviations used in this paper: APC/C, anaphase-promoting complex/cyclosome; D-box, destruction box; DIC, differential interference contrast; FP, fluorescent protein; Plk1, polo-like kinase 1.


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