The recognition of ubiquitinated proteins by the proteasome
The ability of ubiquitin to form up to eight different polyubiquitin chain linkages generates complexity within the ubiquitin proteasome system, and accounts for the diverse roles of ubiquitination within the cell. Understanding how each type of ubiquitin linkage is correctly interpreted by ubiquiti...
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| Format: | Online |
| Language: | English |
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Springer International Publishing
2016
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4980412/ |
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pubmed-49804122016-08-19 The recognition of ubiquitinated proteins by the proteasome Grice, Guinevere L. Nathan, James A. Review The ability of ubiquitin to form up to eight different polyubiquitin chain linkages generates complexity within the ubiquitin proteasome system, and accounts for the diverse roles of ubiquitination within the cell. Understanding how each type of ubiquitin linkage is correctly interpreted by ubiquitin binding proteins provides important insights into the link between chain recognition and cellular fate. A major function of ubiquitination is to signal degradation of intracellular proteins by the 26S proteasome. Lysine-48 (K48) linked polyubiquitin chains are well established as the canonical signal for proteasomal degradation, but recent studies show a role for other ubiquitin linked chains in facilitating degradation by the 26S proteasome. Here, we review how different types of polyubiquitin linkage bind to ubiquitin receptors on the 26S proteasome, how they signal degradation and discuss the implications of ubiquitin chain linkage in regulating protein breakdown by the proteasome. Springer International Publishing 2016-05-02 2016 /pmc/articles/PMC4980412/ /pubmed/27137187 http://dx.doi.org/10.1007/s00018-016-2255-5 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Grice, Guinevere L. Nathan, James A. |
| spellingShingle |
Grice, Guinevere L. Nathan, James A. The recognition of ubiquitinated proteins by the proteasome |
| author_facet |
Grice, Guinevere L. Nathan, James A. |
| author_sort |
Grice, Guinevere L. |
| title |
The recognition of ubiquitinated proteins by the proteasome |
| title_short |
The recognition of ubiquitinated proteins by the proteasome |
| title_full |
The recognition of ubiquitinated proteins by the proteasome |
| title_fullStr |
The recognition of ubiquitinated proteins by the proteasome |
| title_full_unstemmed |
The recognition of ubiquitinated proteins by the proteasome |
| title_sort |
recognition of ubiquitinated proteins by the proteasome |
| description |
The ability of ubiquitin to form up to eight different polyubiquitin chain linkages generates complexity within the ubiquitin proteasome system, and accounts for the diverse roles of ubiquitination within the cell. Understanding how each type of ubiquitin linkage is correctly interpreted by ubiquitin binding proteins provides important insights into the link between chain recognition and cellular fate. A major function of ubiquitination is to signal degradation of intracellular proteins by the 26S proteasome. Lysine-48 (K48) linked polyubiquitin chains are well established as the canonical signal for proteasomal degradation, but recent studies show a role for other ubiquitin linked chains in facilitating degradation by the 26S proteasome. Here, we review how different types of polyubiquitin linkage bind to ubiquitin receptors on the 26S proteasome, how they signal degradation and discuss the implications of ubiquitin chain linkage in regulating protein breakdown by the proteasome. |
| publisher |
Springer International Publishing |
| publishDate |
2016 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4980412/ |
| _version_ |
1613625289913401344 |