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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...

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Detalles Bibliográficos
Autores principales: Wang, Xingde, Xu, Xingzhi, Wang, Zhifeng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
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.
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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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