Cargando…
Deubiquitinases in cell death and inflammation
Apoptosis, pyroptosis, and necroptosis are distinct forms of programmed cell death that eliminate infected, damaged, or obsolete cells. Many proteins that regulate or are a part of the cell death machinery undergo ubiquitination, a post-translational modification made by ubiquitin ligases that modul...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9162465/ https://www.ncbi.nlm.nih.gov/pubmed/35608338 http://dx.doi.org/10.1042/BCJ20210735 |
_version_ | 1784719710273667072 |
---|---|
author | Newton, Kim Gitlin, Alexander D. |
author_facet | Newton, Kim Gitlin, Alexander D. |
author_sort | Newton, Kim |
collection | PubMed |
description | Apoptosis, pyroptosis, and necroptosis are distinct forms of programmed cell death that eliminate infected, damaged, or obsolete cells. Many proteins that regulate or are a part of the cell death machinery undergo ubiquitination, a post-translational modification made by ubiquitin ligases that modulates protein abundance, localization, and/or activity. For example, some ubiquitin chains target proteins for degradation, while others function as scaffolds for the assembly of signaling complexes. Deubiquitinases (DUBs) are the proteases that counteract ubiquitin ligases by cleaving ubiquitin from their protein substrates. Here, we review the DUBs that have been found to suppress or promote apoptosis, pyroptosis, or necroptosis. |
format | Online Article Text |
id | pubmed-9162465 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-91624652022-06-07 Deubiquitinases in cell death and inflammation Newton, Kim Gitlin, Alexander D. Biochem J Signaling Apoptosis, pyroptosis, and necroptosis are distinct forms of programmed cell death that eliminate infected, damaged, or obsolete cells. Many proteins that regulate or are a part of the cell death machinery undergo ubiquitination, a post-translational modification made by ubiquitin ligases that modulates protein abundance, localization, and/or activity. For example, some ubiquitin chains target proteins for degradation, while others function as scaffolds for the assembly of signaling complexes. Deubiquitinases (DUBs) are the proteases that counteract ubiquitin ligases by cleaving ubiquitin from their protein substrates. Here, we review the DUBs that have been found to suppress or promote apoptosis, pyroptosis, or necroptosis. Portland Press Ltd. 2022-05-24 /pmc/articles/PMC9162465/ /pubmed/35608338 http://dx.doi.org/10.1042/BCJ20210735 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Signaling Newton, Kim Gitlin, Alexander D. Deubiquitinases in cell death and inflammation |
title | Deubiquitinases in cell death and inflammation |
title_full | Deubiquitinases in cell death and inflammation |
title_fullStr | Deubiquitinases in cell death and inflammation |
title_full_unstemmed | Deubiquitinases in cell death and inflammation |
title_short | Deubiquitinases in cell death and inflammation |
title_sort | deubiquitinases in cell death and inflammation |
topic | Signaling |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9162465/ https://www.ncbi.nlm.nih.gov/pubmed/35608338 http://dx.doi.org/10.1042/BCJ20210735 |
work_keys_str_mv | AT newtonkim deubiquitinasesincelldeathandinflammation AT gitlinalexanderd deubiquitinasesincelldeathandinflammation |