Publikation: Non-proteolytic ubiquitylation counteracts the APC/C-inhibitory function of XErp1
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2011
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SP Mechanisms of Genome Haploidization -Regulatory Mechanisms of Meiosis in Vertebrate Oocytes-
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EMBO reports. 2011, 12(5), pp. 436-443. ISSN 1469-221X. eISSN 1469-3178. Available under: doi: 10.1038/embor.2011.32
Zusammenfassung
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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HÖRMANSEDER, Eva Beate, Thomas TISCHER, Simone HEUBES, Olaf STEMMANN, Thomas U. MAYER, 2011. Non-proteolytic ubiquitylation counteracts the APC/C-inhibitory function of XErp1. In: EMBO reports. 2011, 12(5), pp. 436-443. ISSN 1469-221X. eISSN 1469-3178. Available under: doi: 10.1038/embor.2011.32BibTex
@article{Hormanseder2011-05Nonpr-13685,
year={2011},
doi={10.1038/embor.2011.32},
title={Non-proteolytic ubiquitylation counteracts the APC/C-inhibitory function of XErp1},
number={5},
volume={12},
issn={1469-221X},
journal={EMBO reports},
pages={436--443},
author={Hörmanseder, Eva Beate and Tischer, Thomas and Heubes, Simone and Stemmann, Olaf and Mayer, Thomas U.}
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<dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
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