A Ubiquitin-binding domain that binds a structural fold distinct from that of Ubiquitin
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...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Elsevier
2019
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| _version_ | 1797058576199450624 |
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| author | Lim, M Newman, J Williams, H Masino, L Aitkenhead, H Gravard, A Gileadi, O Svejstrup, J |
| author_facet | Lim, M Newman, J Williams, H Masino, L Aitkenhead, H Gravard, A Gileadi, O Svejstrup, J |
| author_sort | Lim, M |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T19:52:15Z |
| format | Journal article |
| id | oxford-uuid:245828bb-1421-45a7-ad70-8f9c80230945 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:52:15Z |
| publishDate | 2019 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:245828bb-1421-45a7-ad70-8f9c802309452022-03-26T11:49:35ZA Ubiquitin-binding domain that binds a structural fold distinct from that of UbiquitinJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:245828bb-1421-45a7-ad70-8f9c80230945EnglishSymplectic Elements at OxfordElsevier2019Lim, MNewman, JWilliams, HMasino, LAitkenhead, HGravard, AGileadi, OSvejstrup, JUbiquitylation, 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. |
| spellingShingle | Lim, M Newman, J Williams, H Masino, L Aitkenhead, H Gravard, A Gileadi, O Svejstrup, J A Ubiquitin-binding domain that binds a structural fold distinct from that of Ubiquitin |
| title | A Ubiquitin-binding domain that binds a structural fold distinct from that of Ubiquitin |
| title_full | A Ubiquitin-binding domain that binds a structural fold distinct from that of Ubiquitin |
| title_fullStr | A Ubiquitin-binding domain that binds a structural fold distinct from that of Ubiquitin |
| title_full_unstemmed | A Ubiquitin-binding domain that binds a structural fold distinct from that of Ubiquitin |
| title_short | A Ubiquitin-binding domain that binds a structural fold distinct from that of Ubiquitin |
| title_sort | ubiquitin binding domain that binds a structural fold distinct from that of ubiquitin |
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