USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization

Histone chaperone ASF1A is often dysregulated in cancers, however the regulation of its abundance is unclear. Here, the authors show that USP52 promotes ASF1A stability through deubiquitination while impairment of this stability reduces breast tumorigenesis and confers sensitivity to DNA damage.

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Autores principales:	Shangda Yang, Ling Liu, Cheng Cao, Nan Song, Yuejiao Wang, Shuai Ma, Qi Zhang, Na Yu, Xiang Ding, Fuquan Yang, Shanshan Tian, Kai Zhang, Tao Sun, Jie Yang, Zhi Yao, Shaoyuan Wu, Lei Shi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/19657680f5d0410bbe493e8461cbd273
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

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spelling	oai:doaj.org-article:19657680f5d0410bbe493e8461cbd2732021-12-02T17:31:15ZUSP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization10.1038/s41467-018-03588-z2041-1723https://doaj.org/article/19657680f5d0410bbe493e8461cbd2732018-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03588-zhttps://doaj.org/toc/2041-1723Histone chaperone ASF1A is often dysregulated in cancers, however the regulation of its abundance is unclear. Here, the authors show that USP52 promotes ASF1A stability through deubiquitination while impairment of this stability reduces breast tumorigenesis and confers sensitivity to DNA damage.Shangda YangLing LiuCheng CaoNan SongYuejiao WangShuai MaQi ZhangNa YuXiang DingFuquan YangShanshan TianKai ZhangTao SunJie YangZhi YaoShaoyuan WuLei ShiNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-17 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Shangda Yang Ling Liu Cheng Cao Nan Song Yuejiao Wang Shuai Ma Qi Zhang Na Yu Xiang Ding Fuquan Yang Shanshan Tian Kai Zhang Tao Sun Jie Yang Zhi Yao Shaoyuan Wu Lei Shi USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization
description	Histone chaperone ASF1A is often dysregulated in cancers, however the regulation of its abundance is unclear. Here, the authors show that USP52 promotes ASF1A stability through deubiquitination while impairment of this stability reduces breast tumorigenesis and confers sensitivity to DNA damage.
format	article
author	Shangda Yang Ling Liu Cheng Cao Nan Song Yuejiao Wang Shuai Ma Qi Zhang Na Yu Xiang Ding Fuquan Yang Shanshan Tian Kai Zhang Tao Sun Jie Yang Zhi Yao Shaoyuan Wu Lei Shi
author_facet	Shangda Yang Ling Liu Cheng Cao Nan Song Yuejiao Wang Shuai Ma Qi Zhang Na Yu Xiang Ding Fuquan Yang Shanshan Tian Kai Zhang Tao Sun Jie Yang Zhi Yao Shaoyuan Wu Lei Shi
author_sort	Shangda Yang
title	USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization
title_short	USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization
title_full	USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization
title_fullStr	USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization
title_full_unstemmed	USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization
title_sort	usp52 acts as a deubiquitinase and promotes histone chaperone asf1a stabilization
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/19657680f5d0410bbe493e8461cbd273
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USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization

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