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A non‐canonical UBA–UBL interaction forms the linear‐ubiquitin‐chain assembly complex
Author(s) -
Yagi Hirokazu,
Ishimoto Kazuhiro,
Hiromoto Takeshi,
Fujita Hiroaki,
Mizushima Tsunehiro,
Uekusa Yoshinori,
YagiUtsumi Maho,
Kurimoto Eiji,
Noda Masanori,
Uchiyama Susumu,
Tokunaga Fuminori,
Iwai Kazuhiro,
Kato Koichi
Publication year - 2012
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2012.24
Subject(s) - ubiquitin , ubiquitin ligase , ubiquitin protein ligases , computational biology , protein–protein interaction , chemistry , domain (mathematical analysis) , plasma protein binding , biochemistry , microbiology and biotechnology , biology , mathematics , mathematical analysis , gene
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 protein–protein interactions involving Ub/UBLs and their cognate proteins.