Methylation-regulated decommissioning of multimeric PP2A complexes

Protein phosphatase 2A (PP2A) forms different holoenzymes but little is known about the disassembly of these important signalling complexes. Here the authors present the crystal structure of PP2A bound to TOR signaling pathway regulator (TIPRL) and give insights into the methylation-dependent disass...

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Autores principales:	Cheng-Guo Wu, Aiping Zheng, Li Jiang, Michael Rowse, Vitali Stanevich, Hui Chen, Yitong Li, Kenneth A. Satyshur, Benjamin Johnson, Ting-Jia Gu, Zuojia Liu, Yongna Xing
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/94a35d46f87a45ba809c7ceade92ca57
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spelling	oai:doaj.org-article:94a35d46f87a45ba809c7ceade92ca572021-12-02T17:06:19ZMethylation-regulated decommissioning of multimeric PP2A complexes10.1038/s41467-017-02405-32041-1723https://doaj.org/article/94a35d46f87a45ba809c7ceade92ca572017-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02405-3https://doaj.org/toc/2041-1723Protein phosphatase 2A (PP2A) forms different holoenzymes but little is known about the disassembly of these important signalling complexes. Here the authors present the crystal structure of PP2A bound to TOR signaling pathway regulator (TIPRL) and give insights into the methylation-dependent disassembly of PP2A holenzymes.Cheng-Guo WuAiping ZhengLi JiangMichael RowseVitali StanevichHui ChenYitong LiKenneth A. SatyshurBenjamin JohnsonTing-Jia GuZuojia LiuYongna XingNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Cheng-Guo Wu Aiping Zheng Li Jiang Michael Rowse Vitali Stanevich Hui Chen Yitong Li Kenneth A. Satyshur Benjamin Johnson Ting-Jia Gu Zuojia Liu Yongna Xing Methylation-regulated decommissioning of multimeric PP2A complexes
description	Protein phosphatase 2A (PP2A) forms different holoenzymes but little is known about the disassembly of these important signalling complexes. Here the authors present the crystal structure of PP2A bound to TOR signaling pathway regulator (TIPRL) and give insights into the methylation-dependent disassembly of PP2A holenzymes.
format	article
author	Cheng-Guo Wu Aiping Zheng Li Jiang Michael Rowse Vitali Stanevich Hui Chen Yitong Li Kenneth A. Satyshur Benjamin Johnson Ting-Jia Gu Zuojia Liu Yongna Xing
author_facet	Cheng-Guo Wu Aiping Zheng Li Jiang Michael Rowse Vitali Stanevich Hui Chen Yitong Li Kenneth A. Satyshur Benjamin Johnson Ting-Jia Gu Zuojia Liu Yongna Xing
author_sort	Cheng-Guo Wu
title	Methylation-regulated decommissioning of multimeric PP2A complexes
title_short	Methylation-regulated decommissioning of multimeric PP2A complexes
title_full	Methylation-regulated decommissioning of multimeric PP2A complexes
title_fullStr	Methylation-regulated decommissioning of multimeric PP2A complexes
title_full_unstemmed	Methylation-regulated decommissioning of multimeric PP2A complexes
title_sort	methylation-regulated decommissioning of multimeric pp2a complexes
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/94a35d46f87a45ba809c7ceade92ca57
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Methylation-regulated decommissioning of multimeric PP2A complexes

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