OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity

The mechanisms by which deubiquitinases modulate tumour progression are not fully understood. Here, the authors perform an RNAi screen and identify that the deubiquitinase OTUD5 suppresses cancer growth in a TRIM25 dependent manner, which in turn controls the expression of tumour suppressor protein,...

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Autores principales:	Fangzhou Li, Qianqian Sun, Kun Liu, Ling Zhang, Ning Lin, Kaiqiang You, Mingwei Liu, Ning Kon, Feng Tian, Zebin Mao, Tingting Li, Tanjun Tong, Jun Qin, Wei Gu, Dawei Li, Wenhui Zhao
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3f5c3332490c4893b498e60e24dbc29d
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spelling	oai:doaj.org-article:3f5c3332490c4893b498e60e24dbc29d2021-12-02T15:10:55ZOTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity10.1038/s41467-020-17926-72041-1723https://doaj.org/article/3f5c3332490c4893b498e60e24dbc29d2020-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17926-7https://doaj.org/toc/2041-1723The mechanisms by which deubiquitinases modulate tumour progression are not fully understood. Here, the authors perform an RNAi screen and identify that the deubiquitinase OTUD5 suppresses cancer growth in a TRIM25 dependent manner, which in turn controls the expression of tumour suppressor protein, PML.Fangzhou LiQianqian SunKun LiuLing ZhangNing LinKaiqiang YouMingwei LiuNing KonFeng TianZebin MaoTingting LiTanjun TongJun QinWei GuDawei LiWenhui ZhaoNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Fangzhou Li Qianqian Sun Kun Liu Ling Zhang Ning Lin Kaiqiang You Mingwei Liu Ning Kon Feng Tian Zebin Mao Tingting Li Tanjun Tong Jun Qin Wei Gu Dawei Li Wenhui Zhao OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity
description	The mechanisms by which deubiquitinases modulate tumour progression are not fully understood. Here, the authors perform an RNAi screen and identify that the deubiquitinase OTUD5 suppresses cancer growth in a TRIM25 dependent manner, which in turn controls the expression of tumour suppressor protein, PML.
format	article
author	Fangzhou Li Qianqian Sun Kun Liu Ling Zhang Ning Lin Kaiqiang You Mingwei Liu Ning Kon Feng Tian Zebin Mao Tingting Li Tanjun Tong Jun Qin Wei Gu Dawei Li Wenhui Zhao
author_facet	Fangzhou Li Qianqian Sun Kun Liu Ling Zhang Ning Lin Kaiqiang You Mingwei Liu Ning Kon Feng Tian Zebin Mao Tingting Li Tanjun Tong Jun Qin Wei Gu Dawei Li Wenhui Zhao
author_sort	Fangzhou Li
title	OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity
title_short	OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity
title_full	OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity
title_fullStr	OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity
title_full_unstemmed	OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity
title_sort	otud5 cooperates with trim25 in transcriptional regulation and tumor progression via deubiquitination activity
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/3f5c3332490c4893b498e60e24dbc29d
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OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity

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