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SUMOylation modification-mediated cell death
SUMOylation dynamically conjugates SUMO molecules to the lysine residue of a substrate protein, which depends on the physiological state of the cell and the attached SUMO isoforms. A prominent role of SUMOylation in molecular pathways is to govern the cellular death process. Herein, we summarize the...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8277462/ https://www.ncbi.nlm.nih.gov/pubmed/34255975 http://dx.doi.org/10.1098/rsob.210050 |
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author | Sheng, Zenghua Zhu, Jing Deng, Ya-nan Gao, Shan Liang, Shufang |
author_facet | Sheng, Zenghua Zhu, Jing Deng, Ya-nan Gao, Shan Liang, Shufang |
author_sort | Sheng, Zenghua |
collection | PubMed |
description | SUMOylation dynamically conjugates SUMO molecules to the lysine residue of a substrate protein, which depends on the physiological state of the cell and the attached SUMO isoforms. A prominent role of SUMOylation in molecular pathways is to govern the cellular death process. Herein, we summarize the association between SUMOylation modification events and four types of cellular death processes: apoptosis, autophagy, senescence and pyroptosis. SUMOylation positively or negatively regulates a certain cellular death pattern depending on specific conditions including the attached SUMO isoforms, disease types, substrate proteins and cell context. Moreover, we also discuss the possible role of SUMOylation in ferroptosis and propose a potential role of the SUMOylated GPX4 in the regulation of ferroptosis. Mapping the exact SUMOylation network with cellular death contributes to develop novel SUMOylation-targeting disease therapeutic strategies. |
format | Online Article Text |
id | pubmed-8277462 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-82774622021-07-22 SUMOylation modification-mediated cell death Sheng, Zenghua Zhu, Jing Deng, Ya-nan Gao, Shan Liang, Shufang Open Biol Review SUMOylation dynamically conjugates SUMO molecules to the lysine residue of a substrate protein, which depends on the physiological state of the cell and the attached SUMO isoforms. A prominent role of SUMOylation in molecular pathways is to govern the cellular death process. Herein, we summarize the association between SUMOylation modification events and four types of cellular death processes: apoptosis, autophagy, senescence and pyroptosis. SUMOylation positively or negatively regulates a certain cellular death pattern depending on specific conditions including the attached SUMO isoforms, disease types, substrate proteins and cell context. Moreover, we also discuss the possible role of SUMOylation in ferroptosis and propose a potential role of the SUMOylated GPX4 in the regulation of ferroptosis. Mapping the exact SUMOylation network with cellular death contributes to develop novel SUMOylation-targeting disease therapeutic strategies. The Royal Society 2021-07-14 /pmc/articles/PMC8277462/ /pubmed/34255975 http://dx.doi.org/10.1098/rsob.210050 Text en © 2021 The Authors. https://creativecommons.org/licenses/by/4.0/Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Review Sheng, Zenghua Zhu, Jing Deng, Ya-nan Gao, Shan Liang, Shufang SUMOylation modification-mediated cell death |
title | SUMOylation modification-mediated cell death |
title_full | SUMOylation modification-mediated cell death |
title_fullStr | SUMOylation modification-mediated cell death |
title_full_unstemmed | SUMOylation modification-mediated cell death |
title_short | SUMOylation modification-mediated cell death |
title_sort | sumoylation modification-mediated cell death |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8277462/ https://www.ncbi.nlm.nih.gov/pubmed/34255975 http://dx.doi.org/10.1098/rsob.210050 |
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