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 protein-protein interactions involving Ub/UBLs and their cognate proteins.
journal_name
EMBO Repjournal_title
EMBO reportsauthors
Yagi H,Ishimoto K,Hiromoto T,Fujita H,Mizushima T,Uekusa Y,Yagi-Utsumi M,Kurimoto E,Noda M,Uchiyama S,Tokunaga F,Iwai K,Kato Kdoi
10.1038/embor.2012.24subject
Has Abstractpub_date
2012-05-01 00:00:00pages
462-8issue
5eissn
1469-221Xissn
1469-3178pii
embor201224journal_volume
13pub_type
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