Structural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF168

E3 ubiquitin ligase RNF168 is important for the repair of DNA double-strand breaks and recognizes ubiquitylated targets through two Ub-dependent DSB recruitment modules UDM1 and UDM2. Here the authors combine crystallography, cell biology and biochemical experiments to reveal how UDM1 and UDM2 inter...

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Autores principales:	Tomio S. Takahashi, Yoshihiro Hirade, Aya Toma, Yusuke Sato, Atsushi Yamagata, Sakurako Goto-Ito, Akiko Tomita, Shinichiro Nakada, Shuya Fukai
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/844a6cbf8e1c4c36836921bf75e0a576
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spelling	oai:doaj.org-article:844a6cbf8e1c4c36836921bf75e0a5762021-12-02T17:31:15ZStructural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF16810.1038/s41467-017-02345-y2041-1723https://doaj.org/article/844a6cbf8e1c4c36836921bf75e0a5762018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02345-yhttps://doaj.org/toc/2041-1723E3 ubiquitin ligase RNF168 is important for the repair of DNA double-strand breaks and recognizes ubiquitylated targets through two Ub-dependent DSB recruitment modules UDM1 and UDM2. Here the authors combine crystallography, cell biology and biochemical experiments to reveal how UDM1 and UDM2 interact with polyubiquitin chains.Tomio S. TakahashiYoshihiro HiradeAya TomaYusuke SatoAtsushi YamagataSakurako Goto-ItoAkiko TomitaShinichiro NakadaShuya FukaiNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tomio S. Takahashi Yoshihiro Hirade Aya Toma Yusuke Sato Atsushi Yamagata Sakurako Goto-Ito Akiko Tomita Shinichiro Nakada Shuya Fukai Structural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF168
description	E3 ubiquitin ligase RNF168 is important for the repair of DNA double-strand breaks and recognizes ubiquitylated targets through two Ub-dependent DSB recruitment modules UDM1 and UDM2. Here the authors combine crystallography, cell biology and biochemical experiments to reveal how UDM1 and UDM2 interact with polyubiquitin chains.
format	article
author	Tomio S. Takahashi Yoshihiro Hirade Aya Toma Yusuke Sato Atsushi Yamagata Sakurako Goto-Ito Akiko Tomita Shinichiro Nakada Shuya Fukai
author_facet	Tomio S. Takahashi Yoshihiro Hirade Aya Toma Yusuke Sato Atsushi Yamagata Sakurako Goto-Ito Akiko Tomita Shinichiro Nakada Shuya Fukai
author_sort	Tomio S. Takahashi
title	Structural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF168
title_short	Structural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF168
title_full	Structural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF168
title_fullStr	Structural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF168
title_full_unstemmed	Structural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF168
title_sort	structural insights into two distinct binding modules for lys63-linked polyubiquitin chains in rnf168
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/844a6cbf8e1c4c36836921bf75e0a576
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Structural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF168

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