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Characterization of the mammalian family of DCN-type NEDD8 E3 ligases
Cullin-RING ligases (CRL) are ubiquitin E3 enzymes that bind substrates through variable substrate receptor proteins and are activated by attachment of the ubiquitin-like protein NEDD8 to the cullin subunit. DCNs are NEDD8 E3 ligases that promote neddylation. Mammalian cells express five DCN-like (D...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists Ltd
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4886823/ https://www.ncbi.nlm.nih.gov/pubmed/26906416 http://dx.doi.org/10.1242/jcs.181784 |
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author | Keuss, Matthew J. Thomas, Yann Mcarthur, Robin Wood, Nicola T. Knebel, Axel Kurz, Thimo |
author_facet | Keuss, Matthew J. Thomas, Yann Mcarthur, Robin Wood, Nicola T. Knebel, Axel Kurz, Thimo |
author_sort | Keuss, Matthew J. |
collection | PubMed |
description | Cullin-RING ligases (CRL) are ubiquitin E3 enzymes that bind substrates through variable substrate receptor proteins and are activated by attachment of the ubiquitin-like protein NEDD8 to the cullin subunit. DCNs are NEDD8 E3 ligases that promote neddylation. Mammalian cells express five DCN-like (DCNL) proteins but little is known about their specific functions or interaction partners. We found that DCNLs form stable stoichiometric complexes with CAND1 and cullins that can only be neddylated in the presence of a substrate adaptor. These CAND–cullin–DCNL complexes might represent ‘reserve’ CRLs that can be rapidly activated when needed. We further found that all DCNLs interact with most cullin subtypes, but that they are probably responsible for the neddylation of different subpopulations of any given cullin. This is consistent with the fact that the subcellular localization of DCNLs in tissue culture cells differs and that they show unique tissue-specific expression patterns in mice. Thus, the specificity between DCNL-type NEDD8 E3 enzymes and their cullin substrates is only apparent in well-defined physiological contexts and related to their subcellular distribution and restricted expression. |
format | Online Article Text |
id | pubmed-4886823 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The Company of Biologists Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-48868232016-07-14 Characterization of the mammalian family of DCN-type NEDD8 E3 ligases Keuss, Matthew J. Thomas, Yann Mcarthur, Robin Wood, Nicola T. Knebel, Axel Kurz, Thimo J Cell Sci Research Article Cullin-RING ligases (CRL) are ubiquitin E3 enzymes that bind substrates through variable substrate receptor proteins and are activated by attachment of the ubiquitin-like protein NEDD8 to the cullin subunit. DCNs are NEDD8 E3 ligases that promote neddylation. Mammalian cells express five DCN-like (DCNL) proteins but little is known about their specific functions or interaction partners. We found that DCNLs form stable stoichiometric complexes with CAND1 and cullins that can only be neddylated in the presence of a substrate adaptor. These CAND–cullin–DCNL complexes might represent ‘reserve’ CRLs that can be rapidly activated when needed. We further found that all DCNLs interact with most cullin subtypes, but that they are probably responsible for the neddylation of different subpopulations of any given cullin. This is consistent with the fact that the subcellular localization of DCNLs in tissue culture cells differs and that they show unique tissue-specific expression patterns in mice. Thus, the specificity between DCNL-type NEDD8 E3 enzymes and their cullin substrates is only apparent in well-defined physiological contexts and related to their subcellular distribution and restricted expression. The Company of Biologists Ltd 2016-04-01 /pmc/articles/PMC4886823/ /pubmed/26906416 http://dx.doi.org/10.1242/jcs.181784 Text en © 2016. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
spellingShingle | Research Article Keuss, Matthew J. Thomas, Yann Mcarthur, Robin Wood, Nicola T. Knebel, Axel Kurz, Thimo Characterization of the mammalian family of DCN-type NEDD8 E3 ligases |
title | Characterization of the mammalian family of DCN-type NEDD8 E3 ligases |
title_full | Characterization of the mammalian family of DCN-type NEDD8 E3 ligases |
title_fullStr | Characterization of the mammalian family of DCN-type NEDD8 E3 ligases |
title_full_unstemmed | Characterization of the mammalian family of DCN-type NEDD8 E3 ligases |
title_short | Characterization of the mammalian family of DCN-type NEDD8 E3 ligases |
title_sort | characterization of the mammalian family of dcn-type nedd8 e3 ligases |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4886823/ https://www.ncbi.nlm.nih.gov/pubmed/26906416 http://dx.doi.org/10.1242/jcs.181784 |
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