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Regulation of E3 ubiquitin ligases by homotypic and heterotypic assembly
Protein ubiquitylation is essential for the maintenance of cellular homeostasis. E3 ubiquitin ligases are key components of the enzymatic machinery catalyzing the attachment of ubiquitin to substrate proteins. Consequently, enzymatic dysfunction has been associated with medical conditions including...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
F1000 Research Limited
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7005916/ https://www.ncbi.nlm.nih.gov/pubmed/32076548 http://dx.doi.org/10.12688/f1000research.21253.1 |
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author | Balaji, Vishnu Hoppe, Thorsten |
author_facet | Balaji, Vishnu Hoppe, Thorsten |
author_sort | Balaji, Vishnu |
collection | PubMed |
description | Protein ubiquitylation is essential for the maintenance of cellular homeostasis. E3 ubiquitin ligases are key components of the enzymatic machinery catalyzing the attachment of ubiquitin to substrate proteins. Consequently, enzymatic dysfunction has been associated with medical conditions including cancer, diabetes, and cardiovascular and neurodegenerative disorders. To safeguard substrate selection and ubiquitylation, the activity of E3 ligases is tightly regulated by post-translational modifications including phosphorylation, sumoylation, and ubiquitylation, as well as binding of alternative adaptor molecules and cofactors. Recent structural studies identified homotypic and heterotypic interactions between E3 ligases, adding another layer of control for rapid adaptation to changing environmental and physiological conditions. Here, we discuss the regulation of E3 ligase activity by combinatorial oligomerization and summarize examples of associated ubiquitylation pathways and mechanisms. |
format | Online Article Text |
id | pubmed-7005916 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | F1000 Research Limited |
record_format | MEDLINE/PubMed |
spelling | pubmed-70059162020-02-18 Regulation of E3 ubiquitin ligases by homotypic and heterotypic assembly Balaji, Vishnu Hoppe, Thorsten F1000Res Review Protein ubiquitylation is essential for the maintenance of cellular homeostasis. E3 ubiquitin ligases are key components of the enzymatic machinery catalyzing the attachment of ubiquitin to substrate proteins. Consequently, enzymatic dysfunction has been associated with medical conditions including cancer, diabetes, and cardiovascular and neurodegenerative disorders. To safeguard substrate selection and ubiquitylation, the activity of E3 ligases is tightly regulated by post-translational modifications including phosphorylation, sumoylation, and ubiquitylation, as well as binding of alternative adaptor molecules and cofactors. Recent structural studies identified homotypic and heterotypic interactions between E3 ligases, adding another layer of control for rapid adaptation to changing environmental and physiological conditions. Here, we discuss the regulation of E3 ligase activity by combinatorial oligomerization and summarize examples of associated ubiquitylation pathways and mechanisms. F1000 Research Limited 2020-02-06 /pmc/articles/PMC7005916/ /pubmed/32076548 http://dx.doi.org/10.12688/f1000research.21253.1 Text en Copyright: © 2020 Balaji V and Hoppe T http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Balaji, Vishnu Hoppe, Thorsten Regulation of E3 ubiquitin ligases by homotypic and heterotypic assembly |
title | Regulation of E3 ubiquitin ligases by homotypic and heterotypic assembly |
title_full | Regulation of E3 ubiquitin ligases by homotypic and heterotypic assembly |
title_fullStr | Regulation of E3 ubiquitin ligases by homotypic and heterotypic assembly |
title_full_unstemmed | Regulation of E3 ubiquitin ligases by homotypic and heterotypic assembly |
title_short | Regulation of E3 ubiquitin ligases by homotypic and heterotypic assembly |
title_sort | regulation of e3 ubiquitin ligases by homotypic and heterotypic assembly |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7005916/ https://www.ncbi.nlm.nih.gov/pubmed/32076548 http://dx.doi.org/10.12688/f1000research.21253.1 |
work_keys_str_mv | AT balajivishnu regulationofe3ubiquitinligasesbyhomotypicandheterotypicassembly AT hoppethorsten regulationofe3ubiquitinligasesbyhomotypicandheterotypicassembly |