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The Minimal Deneddylase Core of the COP9 Signalosome Excludes the Csn6 MPN(−) Domain
The COP9 signalosome (CSN) is a eukaryotic protein complex, which regulates a wide range of biological processes mainly through modulating the cullin ubiquitin E3 ligases in the ubiquitin-proteasome pathway. The CSN possesses a highly conserved deneddylase activity that centers at the JAMM motif of...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431379/ https://www.ncbi.nlm.nih.gov/pubmed/22956996 http://dx.doi.org/10.1371/journal.pone.0043980 |
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author | Pick, Elah Golan, Amnon Zimbler, Jacob Z. Guo, Liquan Sharaby, Yehonatan Tsuge, Tomohiko Hofmann, Kay Wei, Ning |
author_facet | Pick, Elah Golan, Amnon Zimbler, Jacob Z. Guo, Liquan Sharaby, Yehonatan Tsuge, Tomohiko Hofmann, Kay Wei, Ning |
author_sort | Pick, Elah |
collection | PubMed |
description | The COP9 signalosome (CSN) is a eukaryotic protein complex, which regulates a wide range of biological processes mainly through modulating the cullin ubiquitin E3 ligases in the ubiquitin-proteasome pathway. The CSN possesses a highly conserved deneddylase activity that centers at the JAMM motif of the Csn5 subunit but requires other subunits in a complex assembly. The classic CSN is composed of 8 subunits (Csn1–8), yet in several Ascomycota, the complex is smaller and lacks orthologs for a few CSN subunits, but nevertheless contains a conserved Csn5. This feature makes yeast a powerful model to determine the minimal assemblage required for deneddylation activity. Here we report, that Csi1, a diverged S. cerevisiae CSN subunit, displays significant homology with the carboxyl terminal domain of the canonical Csn6, but lacks the amino terminal MPN(-) domain. Through the comparative and experimental analyses of the budding yeast and the mammalian CSNs, we demonstrate that the MPN(−) domain of the canonical mouse Csn6 is not part of the CSN deneddylase core. We also show that the carboxyl domain of Csn6 has an indispensable role in maintaining the integrity of the CSN complex. The CSN complex assembled with the carboxyl fragment of Csn6, despite its lack of an MPN(−) domain, is fully active in deneddylation of cullins. We propose that the budding yeast Csi1 is a functional equivalent of the canonical Csn6, and thus the composition of the CSN across phyla is more conserved than hitherto appreciated. |
format | Online Article Text |
id | pubmed-3431379 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-34313792012-09-06 The Minimal Deneddylase Core of the COP9 Signalosome Excludes the Csn6 MPN(−) Domain Pick, Elah Golan, Amnon Zimbler, Jacob Z. Guo, Liquan Sharaby, Yehonatan Tsuge, Tomohiko Hofmann, Kay Wei, Ning PLoS One Research Article The COP9 signalosome (CSN) is a eukaryotic protein complex, which regulates a wide range of biological processes mainly through modulating the cullin ubiquitin E3 ligases in the ubiquitin-proteasome pathway. The CSN possesses a highly conserved deneddylase activity that centers at the JAMM motif of the Csn5 subunit but requires other subunits in a complex assembly. The classic CSN is composed of 8 subunits (Csn1–8), yet in several Ascomycota, the complex is smaller and lacks orthologs for a few CSN subunits, but nevertheless contains a conserved Csn5. This feature makes yeast a powerful model to determine the minimal assemblage required for deneddylation activity. Here we report, that Csi1, a diverged S. cerevisiae CSN subunit, displays significant homology with the carboxyl terminal domain of the canonical Csn6, but lacks the amino terminal MPN(-) domain. Through the comparative and experimental analyses of the budding yeast and the mammalian CSNs, we demonstrate that the MPN(−) domain of the canonical mouse Csn6 is not part of the CSN deneddylase core. We also show that the carboxyl domain of Csn6 has an indispensable role in maintaining the integrity of the CSN complex. The CSN complex assembled with the carboxyl fragment of Csn6, despite its lack of an MPN(−) domain, is fully active in deneddylation of cullins. We propose that the budding yeast Csi1 is a functional equivalent of the canonical Csn6, and thus the composition of the CSN across phyla is more conserved than hitherto appreciated. Public Library of Science 2012-08-30 /pmc/articles/PMC3431379/ /pubmed/22956996 http://dx.doi.org/10.1371/journal.pone.0043980 Text en © 2012 Pick et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Pick, Elah Golan, Amnon Zimbler, Jacob Z. Guo, Liquan Sharaby, Yehonatan Tsuge, Tomohiko Hofmann, Kay Wei, Ning The Minimal Deneddylase Core of the COP9 Signalosome Excludes the Csn6 MPN(−) Domain |
title | The Minimal Deneddylase Core of the COP9 Signalosome Excludes the Csn6 MPN(−) Domain |
title_full | The Minimal Deneddylase Core of the COP9 Signalosome Excludes the Csn6 MPN(−) Domain |
title_fullStr | The Minimal Deneddylase Core of the COP9 Signalosome Excludes the Csn6 MPN(−) Domain |
title_full_unstemmed | The Minimal Deneddylase Core of the COP9 Signalosome Excludes the Csn6 MPN(−) Domain |
title_short | The Minimal Deneddylase Core of the COP9 Signalosome Excludes the Csn6 MPN(−) Domain |
title_sort | minimal deneddylase core of the cop9 signalosome excludes the csn6 mpn(−) domain |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431379/ https://www.ncbi.nlm.nih.gov/pubmed/22956996 http://dx.doi.org/10.1371/journal.pone.0043980 |
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