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The Post-Translational Role of UFMylation in Physiology and Disease
Ubiquitin-fold modifier 1 (UFM1) is a newly identified ubiquitin-like protein that has been conserved during the evolution of multicellular organisms. In a similar manner to ubiquitin, UFM1 can become covalently linked to the lysine residue of a substrate via a dedicated enzymatic cascade. Although...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10648299/ https://www.ncbi.nlm.nih.gov/pubmed/37947621 http://dx.doi.org/10.3390/cells12212543 |
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author | Wang, Xingde Xu, Xingzhi Wang, Zhifeng |
author_facet | Wang, Xingde Xu, Xingzhi Wang, Zhifeng |
author_sort | Wang, Xingde |
collection | PubMed |
description | Ubiquitin-fold modifier 1 (UFM1) is a newly identified ubiquitin-like protein that has been conserved during the evolution of multicellular organisms. In a similar manner to ubiquitin, UFM1 can become covalently linked to the lysine residue of a substrate via a dedicated enzymatic cascade. Although a limited number of substrates have been identified so far, UFM1 modification (UFMylation) has been demonstrated to play a vital role in a variety of cellular activities, including mammalian development, ribosome biogenesis, the DNA damage response, endoplasmic reticulum stress responses, immune responses, and tumorigenesis. In this review, we summarize what is known about the UFM1 enzymatic cascade and its biological functions, and discuss its recently identified substrates. We also explore the pathological role of UFMylation in human disease and the corresponding potential therapeutic targets and strategies. |
format | Online Article Text |
id | pubmed-10648299 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-106482992023-10-29 The Post-Translational Role of UFMylation in Physiology and Disease Wang, Xingde Xu, Xingzhi Wang, Zhifeng Cells Review Ubiquitin-fold modifier 1 (UFM1) is a newly identified ubiquitin-like protein that has been conserved during the evolution of multicellular organisms. In a similar manner to ubiquitin, UFM1 can become covalently linked to the lysine residue of a substrate via a dedicated enzymatic cascade. Although a limited number of substrates have been identified so far, UFM1 modification (UFMylation) has been demonstrated to play a vital role in a variety of cellular activities, including mammalian development, ribosome biogenesis, the DNA damage response, endoplasmic reticulum stress responses, immune responses, and tumorigenesis. In this review, we summarize what is known about the UFM1 enzymatic cascade and its biological functions, and discuss its recently identified substrates. We also explore the pathological role of UFMylation in human disease and the corresponding potential therapeutic targets and strategies. MDPI 2023-10-29 /pmc/articles/PMC10648299/ /pubmed/37947621 http://dx.doi.org/10.3390/cells12212543 Text en © 2023 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 Wang, Xingde Xu, Xingzhi Wang, Zhifeng The Post-Translational Role of UFMylation in Physiology and Disease |
title | The Post-Translational Role of UFMylation in Physiology and Disease |
title_full | The Post-Translational Role of UFMylation in Physiology and Disease |
title_fullStr | The Post-Translational Role of UFMylation in Physiology and Disease |
title_full_unstemmed | The Post-Translational Role of UFMylation in Physiology and Disease |
title_short | The Post-Translational Role of UFMylation in Physiology and Disease |
title_sort | post-translational role of ufmylation in physiology and disease |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10648299/ https://www.ncbi.nlm.nih.gov/pubmed/37947621 http://dx.doi.org/10.3390/cells12212543 |
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