Non-proteolytic ubiquitylation counteracts the APC/C-inhibitory function of XErp1 |
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Authors: | Hörmanseder Eva Tischer Thomas Heubes Simone Stemmann Olaf Mayer Thomas U |
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Institution: | 1Department of Molecular Genetics, University of Konstanz, Universitätsstrasse 10, 78457 Konstanz, Germany;2Department of Genetics, University of Bayreuth, Universitätsstrasse 30, 95440 Bayreuth, Germany |
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Abstract: | Mature Xenopus oocytes are arrested in meiosis by the activity of XErp1/Emi2, an inhibitor of the ubiquitin-ligase anaphase-promoting complex/cyclosome (APC/C). On fertilization, XErp1 is degraded, resulting in APC/C activation and the consequent degradation of cell-cycle regulators and exit from meiosis. In this study, we show that a modest increase in the activity of the ubiquitin-conjugating enzyme UbcX overrides the meiotic arrest in an APC/C-dependent reaction. Intriguingly, XErp1 remains stable in these conditions. We found that UbcX causes the ubiquitylation of XErp1, followed by its dissociation from the APC/C. Our data support the idea that ubiquitylation regulates the APC/C-inhibitory activity of XErp1. |
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Keywords: | APC/C CSF XErp1/Emi2 UbcX/UbcH10 |
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