Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression

Abstract EG5 (KIF11) is a member of the kinesin-like protein family involved in centrosome separation and bipolar spindle formation. When a cell enters mitosis, CDK1 phosphorylates EG5 at Thr926 and promotes EG5 localization on the mitotic spindle which drives bipolar spindle formation. EG5 provides...

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Autores principales:	Yang Liu, Zhong Zhang, Hui Liang, Xuyang Zhao, Ling Liang, Guangxi Wang, Jingyi Yang, Yan Jin, Michael A. McNutt, Yuxin Yin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/015bb20e9498412f995e66a46eb0fed6
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spelling	oai:doaj.org-article:015bb20e9498412f995e66a46eb0fed62021-12-02T15:05:27ZProtein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression10.1038/s41598-017-01915-w2045-2322https://doaj.org/article/015bb20e9498412f995e66a46eb0fed62017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01915-whttps://doaj.org/toc/2045-2322Abstract EG5 (KIF11) is a member of the kinesin-like protein family involved in centrosome separation and bipolar spindle formation. When a cell enters mitosis, CDK1 phosphorylates EG5 at Thr926 and promotes EG5 localization on the mitotic spindle which drives bipolar spindle formation. EG5 provides power for spindle movement and thus controls the dynamics of spindle assembly. However, little is known about EG5 regulation or how EG5 detaches from the spindle upon mitotic exit. In this study we identify EG5 as a novel substrate of PP2A phosphatase, and we show that the PP2A/B55α complex plays an important role in mitotic exit by a mechanism involving EG5. The PP2A/B55α complex physically associates with the EG5 C-terminal tail domain and dephosphorylates EG5 at Thr926 that enables mitotic exit. Conversely PP2A knockdown cells show a high level of phospho-EG5 in late metaphase, which is associated with a delay in mitotic exit. These phenotypic features are similar to those induced by EG5/T926D transfection that mimics phosphorylated EG5 status. Our results argue that PP2A controls mitotic exit through EG5 dephosphorylation. Lack of PP2A leads to abnormal EG5 activation, resulting in delay of mitotic exit.Yang LiuZhong ZhangHui LiangXuyang ZhaoLing LiangGuangxi WangJingyi YangYan JinMichael A. McNuttYuxin YinNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yang Liu Zhong Zhang Hui Liang Xuyang Zhao Ling Liang Guangxi Wang Jingyi Yang Yan Jin Michael A. McNutt Yuxin Yin Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression
description	Abstract EG5 (KIF11) is a member of the kinesin-like protein family involved in centrosome separation and bipolar spindle formation. When a cell enters mitosis, CDK1 phosphorylates EG5 at Thr926 and promotes EG5 localization on the mitotic spindle which drives bipolar spindle formation. EG5 provides power for spindle movement and thus controls the dynamics of spindle assembly. However, little is known about EG5 regulation or how EG5 detaches from the spindle upon mitotic exit. In this study we identify EG5 as a novel substrate of PP2A phosphatase, and we show that the PP2A/B55α complex plays an important role in mitotic exit by a mechanism involving EG5. The PP2A/B55α complex physically associates with the EG5 C-terminal tail domain and dephosphorylates EG5 at Thr926 that enables mitotic exit. Conversely PP2A knockdown cells show a high level of phospho-EG5 in late metaphase, which is associated with a delay in mitotic exit. These phenotypic features are similar to those induced by EG5/T926D transfection that mimics phosphorylated EG5 status. Our results argue that PP2A controls mitotic exit through EG5 dephosphorylation. Lack of PP2A leads to abnormal EG5 activation, resulting in delay of mitotic exit.
format	article
author	Yang Liu Zhong Zhang Hui Liang Xuyang Zhao Ling Liang Guangxi Wang Jingyi Yang Yan Jin Michael A. McNutt Yuxin Yin
author_facet	Yang Liu Zhong Zhang Hui Liang Xuyang Zhao Ling Liang Guangxi Wang Jingyi Yang Yan Jin Michael A. McNutt Yuxin Yin
author_sort	Yang Liu
title	Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression
title_short	Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression
title_full	Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression
title_fullStr	Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression
title_full_unstemmed	Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression
title_sort	protein phosphatase 2a (pp2a) regulates eg5 to control mitotic progression
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/015bb20e9498412f995e66a46eb0fed6
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Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression

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