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Nontraditional translation is the key to UFMylation and beyond

The Ubiquitin-fold modifier 1 (Ufm1) is a ubiquitin-like protein that can also be conjugated to protein substrates and subsequently alter their fates. Both UFMylation and de-UFMylation are mediated by Ufm1-specific proteases (UFSPs). In humans, it is widely believed that UFSP2 is the only active Ufm...

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Detalles Bibliográficos
Autores principales: Lin, Mengjia, Zheng, Xiaoyun, Jin, Jianping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9478918/
https://www.ncbi.nlm.nih.gov/pubmed/36037969
http://dx.doi.org/10.1016/j.jbc.2022.102431
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author Lin, Mengjia
Zheng, Xiaoyun
Jin, Jianping
author_facet Lin, Mengjia
Zheng, Xiaoyun
Jin, Jianping
author_sort Lin, Mengjia
collection PubMed
description The Ubiquitin-fold modifier 1 (Ufm1) is a ubiquitin-like protein that can also be conjugated to protein substrates and subsequently alter their fates. Both UFMylation and de-UFMylation are mediated by Ufm1-specific proteases (UFSPs). In humans, it is widely believed that UFSP2 is the only active Ufm1 protease involved in Ufm1 maturation and de-UFMylation, whereas UFSP1 is thought to be inactive. Here, Liang et al. provide strong evidence showing that human UFSP1 is also an active Ufm1 protease. These results solve an age-old mystery in the human Ufm1 conjugation system and could have a greater impact not only on Ufm1 biology but also on the translation of genes employing nontraditional start codons.
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spelling pubmed-94789182022-09-22 Nontraditional translation is the key to UFMylation and beyond Lin, Mengjia Zheng, Xiaoyun Jin, Jianping J Biol Chem Editors' Pick Highlight The Ubiquitin-fold modifier 1 (Ufm1) is a ubiquitin-like protein that can also be conjugated to protein substrates and subsequently alter their fates. Both UFMylation and de-UFMylation are mediated by Ufm1-specific proteases (UFSPs). In humans, it is widely believed that UFSP2 is the only active Ufm1 protease involved in Ufm1 maturation and de-UFMylation, whereas UFSP1 is thought to be inactive. Here, Liang et al. provide strong evidence showing that human UFSP1 is also an active Ufm1 protease. These results solve an age-old mystery in the human Ufm1 conjugation system and could have a greater impact not only on Ufm1 biology but also on the translation of genes employing nontraditional start codons. American Society for Biochemistry and Molecular Biology 2022-08-28 /pmc/articles/PMC9478918/ /pubmed/36037969 http://dx.doi.org/10.1016/j.jbc.2022.102431 Text en © 2022 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Editors' Pick Highlight
Lin, Mengjia
Zheng, Xiaoyun
Jin, Jianping
Nontraditional translation is the key to UFMylation and beyond
title Nontraditional translation is the key to UFMylation and beyond
title_full Nontraditional translation is the key to UFMylation and beyond
title_fullStr Nontraditional translation is the key to UFMylation and beyond
title_full_unstemmed Nontraditional translation is the key to UFMylation and beyond
title_short Nontraditional translation is the key to UFMylation and beyond
title_sort nontraditional translation is the key to ufmylation and beyond
topic Editors' Pick Highlight
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9478918/
https://www.ncbi.nlm.nih.gov/pubmed/36037969
http://dx.doi.org/10.1016/j.jbc.2022.102431
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AT zhengxiaoyun nontraditionaltranslationisthekeytoufmylationandbeyond
AT jinjianping nontraditionaltranslationisthekeytoufmylationandbeyond