A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex

Hirokazu Yagi; Kazuhiro Ishimoto; Takeshi Hiromoto; Hiroaki Fujita; Tsunehiro Mizushima; Yoshinori Uekusa; Maho Yagi-Utsumi; Eiji Kurimoto; Masanori Noda; Susumu Uchiyama; Fuminori Tokunaga; Kazuhiro Iwai; Koichi Kato

doi:10.1038/embor.2012.24

A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex

Hirokazu Yagi, Kazuhiro Ishimoto, Takeshi Hiromoto, Hiroaki Fujita, Tsunehiro Mizushima, Yoshinori Uekusa, Maho Yagi-Utsumi, Eiji Kurimoto, Masanori Noda, Susumu Uchiyama, Fuminori Tokunaga, Kazuhiro Iwai, Koichi Kato

研究成果: Article › 査読

44 被引用数 (Scopus)

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HOIL-1L and its binding partner HOIP are essential components of the E3-ligase complex that generates linear ubiquitin (Ub) chains, which are critical regulators of NF-κB activation. Using crystallographic and mutational approaches, we characterize the unexpected structural basis for the specific interaction between the Ub-like domain (UBL) of HOIL-1L and the Ub-associated domain (UBA) of HOIP. Our data indicate the functional significance of this non-canonical mode of UBA-UBL interaction in E3 complex formation and subsequent NF-κB activation. This study highlights the versatility and specificity of proteing-protein interactions involving Ub/UBLs and their cognate proteins.

本文言語	English
ページ（範囲）	462-468
ページ数	7
ジャーナル	EMBO Reports
巻	13
号	5
DOI	https://doi.org/10.1038/embor.2012.24
出版ステータス	Published - 2012 5月 1
外部発表	はい

ASJC Scopus subject areas

生化学
分子生物学
遺伝学

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10.1038/embor.2012.24

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abstract = "HOIL-1L and its binding partner HOIP are essential components of the E3-ligase complex that generates linear ubiquitin (Ub) chains, which are critical regulators of NF-κB activation. Using crystallographic and mutational approaches, we characterize the unexpected structural basis for the specific interaction between the Ub-like domain (UBL) of HOIL-1L and the Ub-associated domain (UBA) of HOIP. Our data indicate the functional significance of this non-canonical mode of UBA-UBL interaction in E3 complex formation and subsequent NF-κB activation. This study highlights the versatility and specificity of proteing-protein interactions involving Ub/UBLs and their cognate proteins.",

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AU - Ishimoto, Kazuhiro

AU - Hiromoto, Takeshi

AU - Fujita, Hiroaki

AU - Mizushima, Tsunehiro

AU - Uekusa, Yoshinori

AU - Yagi-Utsumi, Maho

AU - Kurimoto, Eiji

AU - Noda, Masanori

AU - Uchiyama, Susumu

AU - Tokunaga, Fuminori

AU - Iwai, Kazuhiro

AU - Kato, Koichi

PY - 2012/5/1

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N2 - HOIL-1L and its binding partner HOIP are essential components of the E3-ligase complex that generates linear ubiquitin (Ub) chains, which are critical regulators of NF-κB activation. Using crystallographic and mutational approaches, we characterize the unexpected structural basis for the specific interaction between the Ub-like domain (UBL) of HOIL-1L and the Ub-associated domain (UBA) of HOIP. Our data indicate the functional significance of this non-canonical mode of UBA-UBL interaction in E3 complex formation and subsequent NF-κB activation. This study highlights the versatility and specificity of proteing-protein interactions involving Ub/UBLs and their cognate proteins.

AB - HOIL-1L and its binding partner HOIP are essential components of the E3-ligase complex that generates linear ubiquitin (Ub) chains, which are critical regulators of NF-κB activation. Using crystallographic and mutational approaches, we characterize the unexpected structural basis for the specific interaction between the Ub-like domain (UBL) of HOIL-1L and the Ub-associated domain (UBA) of HOIP. Our data indicate the functional significance of this non-canonical mode of UBA-UBL interaction in E3 complex formation and subsequent NF-κB activation. This study highlights the versatility and specificity of proteing-protein interactions involving Ub/UBLs and their cognate proteins.

KW - HOIL-1L

KW - HOIP

KW - NF-kB activation

KW - UBA-UBL interaction

KW - linear-ubiquitin-chain assembly complex

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A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex

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