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Monoubiquitination in Homeostasis and Cancer
Monoubiquitination is a post-translational modification (PTM), through which a single ubiquitin molecule is covalently conjugated to a lysine residue of the target protein. Monoubiquitination regulates the activity, subcellular localization, protein–protein interactions, or endocytosis of the substr...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9180643/ https://www.ncbi.nlm.nih.gov/pubmed/35682605 http://dx.doi.org/10.3390/ijms23115925 |
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author | Chen, Yujie Zhou, Dandan Yao, Yinan Sun, Yutong Yao, Fan Ma, Li |
author_facet | Chen, Yujie Zhou, Dandan Yao, Yinan Sun, Yutong Yao, Fan Ma, Li |
author_sort | Chen, Yujie |
collection | PubMed |
description | Monoubiquitination is a post-translational modification (PTM), through which a single ubiquitin molecule is covalently conjugated to a lysine residue of the target protein. Monoubiquitination regulates the activity, subcellular localization, protein–protein interactions, or endocytosis of the substrate. In doing so, monoubiquitination is implicated in diverse cellular processes, including gene transcription, endocytosis, signal transduction, cell death, and DNA damage repair, which in turn regulate cell-cycle progression, survival, proliferation, and stress response. In this review, we summarize the functions of monoubiquitination and discuss how this PTM modulates homeostasis and cancer. |
format | Online Article Text |
id | pubmed-9180643 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-91806432022-06-10 Monoubiquitination in Homeostasis and Cancer Chen, Yujie Zhou, Dandan Yao, Yinan Sun, Yutong Yao, Fan Ma, Li Int J Mol Sci Review Monoubiquitination is a post-translational modification (PTM), through which a single ubiquitin molecule is covalently conjugated to a lysine residue of the target protein. Monoubiquitination regulates the activity, subcellular localization, protein–protein interactions, or endocytosis of the substrate. In doing so, monoubiquitination is implicated in diverse cellular processes, including gene transcription, endocytosis, signal transduction, cell death, and DNA damage repair, which in turn regulate cell-cycle progression, survival, proliferation, and stress response. In this review, we summarize the functions of monoubiquitination and discuss how this PTM modulates homeostasis and cancer. MDPI 2022-05-25 /pmc/articles/PMC9180643/ /pubmed/35682605 http://dx.doi.org/10.3390/ijms23115925 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Chen, Yujie Zhou, Dandan Yao, Yinan Sun, Yutong Yao, Fan Ma, Li Monoubiquitination in Homeostasis and Cancer |
title | Monoubiquitination in Homeostasis and Cancer |
title_full | Monoubiquitination in Homeostasis and Cancer |
title_fullStr | Monoubiquitination in Homeostasis and Cancer |
title_full_unstemmed | Monoubiquitination in Homeostasis and Cancer |
title_short | Monoubiquitination in Homeostasis and Cancer |
title_sort | monoubiquitination in homeostasis and cancer |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9180643/ https://www.ncbi.nlm.nih.gov/pubmed/35682605 http://dx.doi.org/10.3390/ijms23115925 |
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