Proteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN

Ubiquitin-specific protease 14 (USP14) is a proteasome-associated deubiquitinating enzyme with known roles in physiology and disease. Here the authors show that fatty acid synthase (FASN) is a substrate of USP14, and that by stabilizing FASN, it plays a role in hepatosteatosis.

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Autores principales:	Bin Liu, Shangwen Jiang, Min Li, Xuelian Xiong, Mingrui Zhu, Duanzhuo Li, Lei Zhao, Lili Qian, Linhui Zhai, Jing Li, Han Lu, Shengnan Sun, Jiandie Lin, Yan Lu, Xiaoying Li, Minjia Tan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3581473922f6403895adb5219d0ee52b
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spelling	oai:doaj.org-article:3581473922f6403895adb5219d0ee52b2021-12-02T17:31:44ZProteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN10.1038/s41467-018-07185-y2041-1723https://doaj.org/article/3581473922f6403895adb5219d0ee52b2018-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07185-yhttps://doaj.org/toc/2041-1723Ubiquitin-specific protease 14 (USP14) is a proteasome-associated deubiquitinating enzyme with known roles in physiology and disease. Here the authors show that fatty acid synthase (FASN) is a substrate of USP14, and that by stabilizing FASN, it plays a role in hepatosteatosis.Bin LiuShangwen JiangMin LiXuelian XiongMingrui ZhuDuanzhuo LiLei ZhaoLili QianLinhui ZhaiJing LiHan LuShengnan SunJiandie LinYan LuXiaoying LiMinjia TanNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Bin Liu Shangwen Jiang Min Li Xuelian Xiong Mingrui Zhu Duanzhuo Li Lei Zhao Lili Qian Linhui Zhai Jing Li Han Lu Shengnan Sun Jiandie Lin Yan Lu Xiaoying Li Minjia Tan Proteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN
description	Ubiquitin-specific protease 14 (USP14) is a proteasome-associated deubiquitinating enzyme with known roles in physiology and disease. Here the authors show that fatty acid synthase (FASN) is a substrate of USP14, and that by stabilizing FASN, it plays a role in hepatosteatosis.
format	article
author	Bin Liu Shangwen Jiang Min Li Xuelian Xiong Mingrui Zhu Duanzhuo Li Lei Zhao Lili Qian Linhui Zhai Jing Li Han Lu Shengnan Sun Jiandie Lin Yan Lu Xiaoying Li Minjia Tan
author_facet	Bin Liu Shangwen Jiang Min Li Xuelian Xiong Mingrui Zhu Duanzhuo Li Lei Zhao Lili Qian Linhui Zhai Jing Li Han Lu Shengnan Sun Jiandie Lin Yan Lu Xiaoying Li Minjia Tan
author_sort	Bin Liu
title	Proteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN
title_short	Proteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN
title_full	Proteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN
title_fullStr	Proteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN
title_full_unstemmed	Proteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN
title_sort	proteome-wide analysis of usp14 substrates revealed its role in hepatosteatosis via stabilization of fasn
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/3581473922f6403895adb5219d0ee52b
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Proteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN

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