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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2022
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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. |
format | Online Article Text |
id | pubmed-9478918 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT linmengjia nontraditionaltranslationisthekeytoufmylationandbeyond AT zhengxiaoyun nontraditionaltranslationisthekeytoufmylationandbeyond AT jinjianping nontraditionaltranslationisthekeytoufmylationandbeyond |