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Phosphorylation of Xenopus p31(comet) potentiates mitotic checkpoint exit

p31(comet) plays an important role in spindle assembly checkpoint (SAC) silencing. However, how p31(comet)'s activity is regulated remains unclear. Here we show that the timing of M-phase exit in Xenopus egg extracts (XEEs) depends upon SAC activity, even under conditions that are permissive fo...

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Detalles Bibliográficos
Autores principales: Mo, Min, Arnaoutov, Alexei, Dasso, Mary
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4825729/
https://www.ncbi.nlm.nih.gov/pubmed/25892037
http://dx.doi.org/10.1080/15384101.2015.1033590
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author Mo, Min
Arnaoutov, Alexei
Dasso, Mary
author_facet Mo, Min
Arnaoutov, Alexei
Dasso, Mary
author_sort Mo, Min
collection PubMed
description p31(comet) plays an important role in spindle assembly checkpoint (SAC) silencing. However, how p31(comet)'s activity is regulated remains unclear. Here we show that the timing of M-phase exit in Xenopus egg extracts (XEEs) depends upon SAC activity, even under conditions that are permissive for spindle assembly. p31(comet) antagonizes the SAC, promoting XEE progression into anaphase after spindles are fully formed. We further show that mitotic p31(comet) phosphorylation by Inhibitor of nuclear factor κ-B kinase-β (IKK-β) enhances this role in SAC silencing. Together, our findings implicate IKK-β in the control of anaphase timing in XEE through p31(comet) activation and SAC downregulation.
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spelling pubmed-48257292016-04-27 Phosphorylation of Xenopus p31(comet) potentiates mitotic checkpoint exit Mo, Min Arnaoutov, Alexei Dasso, Mary Cell Cycle Report p31(comet) plays an important role in spindle assembly checkpoint (SAC) silencing. However, how p31(comet)'s activity is regulated remains unclear. Here we show that the timing of M-phase exit in Xenopus egg extracts (XEEs) depends upon SAC activity, even under conditions that are permissive for spindle assembly. p31(comet) antagonizes the SAC, promoting XEE progression into anaphase after spindles are fully formed. We further show that mitotic p31(comet) phosphorylation by Inhibitor of nuclear factor κ-B kinase-β (IKK-β) enhances this role in SAC silencing. Together, our findings implicate IKK-β in the control of anaphase timing in XEE through p31(comet) activation and SAC downregulation. Taylor & Francis 2015-04-18 /pmc/articles/PMC4825729/ /pubmed/25892037 http://dx.doi.org/10.1080/15384101.2015.1033590 Text en This article is not subject to US copyright law http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
spellingShingle Report
Mo, Min
Arnaoutov, Alexei
Dasso, Mary
Phosphorylation of Xenopus p31(comet) potentiates mitotic checkpoint exit
title Phosphorylation of Xenopus p31(comet) potentiates mitotic checkpoint exit
title_full Phosphorylation of Xenopus p31(comet) potentiates mitotic checkpoint exit
title_fullStr Phosphorylation of Xenopus p31(comet) potentiates mitotic checkpoint exit
title_full_unstemmed Phosphorylation of Xenopus p31(comet) potentiates mitotic checkpoint exit
title_short Phosphorylation of Xenopus p31(comet) potentiates mitotic checkpoint exit
title_sort phosphorylation of xenopus p31(comet) potentiates mitotic checkpoint exit
topic Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4825729/
https://www.ncbi.nlm.nih.gov/pubmed/25892037
http://dx.doi.org/10.1080/15384101.2015.1033590
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