10779/crick.11558262.v1
Michael Lim
Michael
Lim
Joseph A Newman
Joseph A
Newman
Hannah L Williams
Hannah L
Williams
Laura Masino
Laura
Masino
Hazel Aitkenhead
Hazel
Aitkenhead
Angeline E Gravard
Angeline E
Gravard
Opher Gileadi
Opher
Gileadi
Jesper Q Svejstrup
Jesper Q
Svejstrup
A ubiquitin-binding domain that binds a structural fold distinct from that of ubiquitin.
The Francis Crick Institute
2020
CUE domain
KAP1
SMARCAD1
TIF1β
TRIM28
UBA domain
ubiquitin
ubiquitin-binding domain
Svejstrup FC001166
SB
PRT-ack
PC-ack
CS-ack
06 Biological Sciences
08 Information and Computing Sciences
03 Chemical Sciences
Biophysics
2020-01-09 11:44:16
Journal contribution
https://crick.figshare.com/articles/journal_contribution/A_ubiquitin-binding_domain_that_binds_a_structural_fold_distinct_from_that_of_ubiquitin_/11558262
Ubiquitylation, the posttranslational linkage of ubiquitin moieties to lysines in target proteins, helps regulate a myriad of biological processes. Ubiquitin, and sometimes ubiquitin-homology domains, are recognized by ubiquitin-binding domains, including CUE domains. CUE domains are thus generally thought to function by mediating interactions with ubiquitylated proteins. The chromatin remodeler, SMARCAD1, interacts with KAP1, a transcriptional corepressor. The SMARCAD1-KAP1 interaction is direct and involves the first SMARCAD1 CUE domain (CUE1) and the RBCC domain of KAP1. Here, we present a structural model of the KAP1 RBCC-SMARCAD1 CUE1 complex based on X-ray crystallography. Remarkably, CUE1, a canonical CUE domain, recognizes a cluster of exposed hydrophobic and surrounding charged/amphipathic residues on KAP1, which are presented in the context of a coiled-coil domain, not in a structure resembling ubiquitin. Together, these data suggest that CUE domains may have a wider function than simply recognizing ubiquitin and the ubiquitin-fold.