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

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 Rep

journal_title

EMBO reports

authors

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 K

doi

10.1038/embor.2012.24

subject

Has Abstract

pub_date

2012-05-01 00:00:00

pages

462-8

issue

5

eissn

1469-221X

issn

1469-3178

pii

embor201224

journal_volume

13

pub_type

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