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iASPP–PP1 complex is required for cytokinetic abscission by controlling CEP55 dephosphorylation

Cytokinesis is the last step of cell division and is concluded by the abscission of the intercellular bridge that connects two daughter cells. The tight regulation of cytokinesis completion is essential because cytokinesis failure is associated with various human diseases. Here, we report that iASPP...

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Autores principales: Gao, Kun, Zhang, Yuanyuan, Shi, Qing, Zhang, Jianong, Zhang, Liang, Sun, Huiru, Jiao, Dongyue, Zhao, Xiayin, Tao, Hongru, Wei, Youheng, Wang, Yuqi, Saiyin, Hexige, Zhao, Shi-Min, Li, Yao, Zhang, Pingzhao, Wang, Chenji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5943338/
https://www.ncbi.nlm.nih.gov/pubmed/29743530
http://dx.doi.org/10.1038/s41419-018-0561-6
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author Gao, Kun
Zhang, Yuanyuan
Shi, Qing
Zhang, Jianong
Zhang, Liang
Sun, Huiru
Jiao, Dongyue
Zhao, Xiayin
Tao, Hongru
Wei, Youheng
Wang, Yuqi
Saiyin, Hexige
Zhao, Shi-Min
Li, Yao
Zhang, Pingzhao
Wang, Chenji
author_facet Gao, Kun
Zhang, Yuanyuan
Shi, Qing
Zhang, Jianong
Zhang, Liang
Sun, Huiru
Jiao, Dongyue
Zhao, Xiayin
Tao, Hongru
Wei, Youheng
Wang, Yuqi
Saiyin, Hexige
Zhao, Shi-Min
Li, Yao
Zhang, Pingzhao
Wang, Chenji
author_sort Gao, Kun
collection PubMed
description Cytokinesis is the last step of cell division and is concluded by the abscission of the intercellular bridge that connects two daughter cells. The tight regulation of cytokinesis completion is essential because cytokinesis failure is associated with various human diseases. Here, we report that iASPP, a member of the apoptosis-stimulating proteins of p53 (ASPP) family, is required for proper cell division. iASPP depletion results in abnormal midbody structure and failed cytokinesis. We used protein affinity purification methods to identify the functional partners of iASPP. We found that iASPP associates with centrosomal protein of 55 kDa (CEP55), an important cytokinetic abscission regulator. Mechanically, iASPP acts as a PP1-targeting subunit to facilitate the interaction between PP1 and CEP55 and to remove PLK1-mediated Ser436 phosphorylation in CEP55 during late mitosis. The latter step is critical for the timely recruitment of CEP55 to the midbody. The present observations revealed a previously unrecognized function of iASPP in cytokinesis. This function, in turn, likely contributes to the roles of iASPP in tumor development and genetic diseases.
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spelling pubmed-59433382018-05-10 iASPP–PP1 complex is required for cytokinetic abscission by controlling CEP55 dephosphorylation Gao, Kun Zhang, Yuanyuan Shi, Qing Zhang, Jianong Zhang, Liang Sun, Huiru Jiao, Dongyue Zhao, Xiayin Tao, Hongru Wei, Youheng Wang, Yuqi Saiyin, Hexige Zhao, Shi-Min Li, Yao Zhang, Pingzhao Wang, Chenji Cell Death Dis Article Cytokinesis is the last step of cell division and is concluded by the abscission of the intercellular bridge that connects two daughter cells. The tight regulation of cytokinesis completion is essential because cytokinesis failure is associated with various human diseases. Here, we report that iASPP, a member of the apoptosis-stimulating proteins of p53 (ASPP) family, is required for proper cell division. iASPP depletion results in abnormal midbody structure and failed cytokinesis. We used protein affinity purification methods to identify the functional partners of iASPP. We found that iASPP associates with centrosomal protein of 55 kDa (CEP55), an important cytokinetic abscission regulator. Mechanically, iASPP acts as a PP1-targeting subunit to facilitate the interaction between PP1 and CEP55 and to remove PLK1-mediated Ser436 phosphorylation in CEP55 during late mitosis. The latter step is critical for the timely recruitment of CEP55 to the midbody. The present observations revealed a previously unrecognized function of iASPP in cytokinesis. This function, in turn, likely contributes to the roles of iASPP in tumor development and genetic diseases. Nature Publishing Group UK 2018-05-09 /pmc/articles/PMC5943338/ /pubmed/29743530 http://dx.doi.org/10.1038/s41419-018-0561-6 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Gao, Kun
Zhang, Yuanyuan
Shi, Qing
Zhang, Jianong
Zhang, Liang
Sun, Huiru
Jiao, Dongyue
Zhao, Xiayin
Tao, Hongru
Wei, Youheng
Wang, Yuqi
Saiyin, Hexige
Zhao, Shi-Min
Li, Yao
Zhang, Pingzhao
Wang, Chenji
iASPP–PP1 complex is required for cytokinetic abscission by controlling CEP55 dephosphorylation
title iASPP–PP1 complex is required for cytokinetic abscission by controlling CEP55 dephosphorylation
title_full iASPP–PP1 complex is required for cytokinetic abscission by controlling CEP55 dephosphorylation
title_fullStr iASPP–PP1 complex is required for cytokinetic abscission by controlling CEP55 dephosphorylation
title_full_unstemmed iASPP–PP1 complex is required for cytokinetic abscission by controlling CEP55 dephosphorylation
title_short iASPP–PP1 complex is required for cytokinetic abscission by controlling CEP55 dephosphorylation
title_sort iaspp–pp1 complex is required for cytokinetic abscission by controlling cep55 dephosphorylation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5943338/
https://www.ncbi.nlm.nih.gov/pubmed/29743530
http://dx.doi.org/10.1038/s41419-018-0561-6
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