Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and activation

The XPF-ERCC1 heterodimer is an endonuclease involved in nucleotide excision (NER) and interstrand crosslink (ICL) repair in mammalian cells. Here, the authors provide insights into its regulation by revealing that TIP60 regulates XPF-ERCC1 complex assembly and activation.

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Autores principales:	Jiajia Wang, Hanqing He, Binbin Chen, Guixing Jiang, Liping Cao, Haiping Jiang, Guofei Zhang, Jianxiang Chen, Jun Huang, Bing Yang, Chun Zhou, Ting Liu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/34893e2e014a42498805fe529e103403
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spelling	oai:doaj.org-article:34893e2e014a42498805fe529e1034032021-12-02T15:39:19ZAcetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and activation10.1038/s41467-020-14564-x2041-1723https://doaj.org/article/34893e2e014a42498805fe529e1034032020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14564-xhttps://doaj.org/toc/2041-1723The XPF-ERCC1 heterodimer is an endonuclease involved in nucleotide excision (NER) and interstrand crosslink (ICL) repair in mammalian cells. Here, the authors provide insights into its regulation by revealing that TIP60 regulates XPF-ERCC1 complex assembly and activation.Jiajia WangHanqing HeBinbin ChenGuixing JiangLiping CaoHaiping JiangGuofei ZhangJianxiang ChenJun HuangBing YangChun ZhouTing LiuNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jiajia Wang Hanqing He Binbin Chen Guixing Jiang Liping Cao Haiping Jiang Guofei Zhang Jianxiang Chen Jun Huang Bing Yang Chun Zhou Ting Liu Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and activation
description	The XPF-ERCC1 heterodimer is an endonuclease involved in nucleotide excision (NER) and interstrand crosslink (ICL) repair in mammalian cells. Here, the authors provide insights into its regulation by revealing that TIP60 regulates XPF-ERCC1 complex assembly and activation.
format	article
author	Jiajia Wang Hanqing He Binbin Chen Guixing Jiang Liping Cao Haiping Jiang Guofei Zhang Jianxiang Chen Jun Huang Bing Yang Chun Zhou Ting Liu
author_facet	Jiajia Wang Hanqing He Binbin Chen Guixing Jiang Liping Cao Haiping Jiang Guofei Zhang Jianxiang Chen Jun Huang Bing Yang Chun Zhou Ting Liu
author_sort	Jiajia Wang
title	Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and activation
title_short	Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and activation
title_full	Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and activation
title_fullStr	Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and activation
title_full_unstemmed	Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and activation
title_sort	acetylation of xpf by tip60 facilitates xpf-ercc1 complex assembly and activation
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/34893e2e014a42498805fe529e103403
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_version_	1718385925156765696

Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and activation

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