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RESEARCH PAPER
1 Chemical Biology, Independent Research Group, and 2 Department of Cell Biology, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany; 3 Department of Biochemistry, University of Leicester, Leicester LE1 7RH, UK
Metaphase-to-anaphase transition is a fundamental step in cell cycle progression where duplicated sister-chromatids segregate to the future daughter cells. The anaphase-promoting complex/cyclosome (APC/C) is a highly regulated ubiquitin-ligase that triggers anaphase onset and mitotic exit by targeting securin and mitotic cyclins for destruction. It was previously shown that the Xenopus polo-like kinase Plx1 is essential to activate APC/C upon release from cytostatic factor (CSF) arrest in Xenopus egg extract. Although the mechanism by which Plx1 regulates APC/C activation remained unclear, the existence of a putative APC/C inhibitor was postulated whose activity would be neutralized by Plx1 upon CSF release. Here we identify XErp1, a novel Plx1-regulated inhibitor of APC/C activity, and we demonstrate that XErp1 is required to prevent anaphase onset in CSF-arrested Xenopus egg extract. Inactivation of XErp1 leads to premature APC/C activation. Conversely, addition of excess XErp1 to Xenopus egg extract prevents APC/C activation. Plx1 phosphorylates XErp1 in vitro at a site that targets XErp1 for degradation upon CSF release. Thus, our data lead to a model of APC/C activation in Xenopus egg extract in which Plx1 targets the APC/C inhibitor XErp1 for degradation.
[Keywords: Cell cycle; anaphase-promoting complex/cyclosome; Xenopus; polo-like kinase; cytostatic factor; mitotic exit]
Received August 9, 2004; revised version accepted December 16, 2004.
4 Present address: Nestlé Research Center, Vers-chez-les-Blanc, PO Box 44, CH-1000 Lausanne 26, Switzerland.
E-MAIL mayer{at}biochem.mpg.de; FAX 49-89-8578-3138.
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