Function and regulation of ubiquitin-like SUMO system in heart
The small ubiquitin-related modifier (SUMOylation) system is a conserved, reversible, post-translational protein modification pathway covalently attached to the lysine residues of proteins in eukaryotic cells, and SUMOylation is catalyzed by SUMO-specific activating enzyme (E1), binding enzyme (E2)...
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Frontiers Media S.A.
2023-11-01
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Online Access: | https://www.frontiersin.org/articles/10.3389/fcell.2023.1294717/full |
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author | Ying Wang Ying Wang Zhihao Liu Zhihao Liu Xiyun Bian Xiyun Bian Chenxu Zhao Xin Zhang Xiaozhi Liu Xiaozhi Liu Nan Wang |
author_facet | Ying Wang Ying Wang Zhihao Liu Zhihao Liu Xiyun Bian Xiyun Bian Chenxu Zhao Xin Zhang Xiaozhi Liu Xiaozhi Liu Nan Wang |
author_sort | Ying Wang |
collection | DOAJ |
description | The small ubiquitin-related modifier (SUMOylation) system is a conserved, reversible, post-translational protein modification pathway covalently attached to the lysine residues of proteins in eukaryotic cells, and SUMOylation is catalyzed by SUMO-specific activating enzyme (E1), binding enzyme (E2) and ligase (E3). Sentrin-specific proteases (SENPs) can cleave the isopeptide bond of a SUMO conjugate and catalyze the deSUMOylation reaction. SUMOylation can regulate the activity of proteins in many important cellular processes, including transcriptional regulation, cell cycle progression, signal transduction, DNA damage repair and protein stability. Biological experiments in vivo and in vitro have confirmed the key role of the SUMO conjugation/deconjugation system in energy metabolism, Ca2+ cycle homeostasis and protein quality control in cardiomyocytes. In this review, we summarized the research progress of the SUMO conjugation/deconjugation system and SUMOylation-mediated cardiac actions based on related studies published in recent years, and highlighted the further research areas to clarify the role of the SUMO system in the heart by using emerging technologies. |
first_indexed | 2024-03-11T10:13:25Z |
format | Article |
id | doaj.art-099308daabc0405f9f6ab94df52035e2 |
institution | Directory Open Access Journal |
issn | 2296-634X |
language | English |
last_indexed | 2024-03-11T10:13:25Z |
publishDate | 2023-11-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Cell and Developmental Biology |
spelling | doaj.art-099308daabc0405f9f6ab94df52035e22023-11-16T12:39:28ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2023-11-011110.3389/fcell.2023.12947171294717Function and regulation of ubiquitin-like SUMO system in heartYing Wang0Ying Wang1Zhihao Liu2Zhihao Liu3Xiyun Bian4Xiyun Bian5Chenxu Zhao6Xin Zhang7Xiaozhi Liu8Xiaozhi Liu9Nan Wang10College of Biotechnology, Tianjin University of Science and Technology, Tianjin, ChinaCentral Laboratory, The Fifth Central Hospital of Tianjin, Tianjin, ChinaFirst Teaching Hospital of Tianjin University of Traditional Chinese Medicine, National Clinical Research Center for Chinese Medicine Acupuncture and Moxibustion, Tianjin, ChinaState Key Laboratory of Modern Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin, ChinaCentral Laboratory, The Fifth Central Hospital of Tianjin, Tianjin, ChinaTianjin Key Laboratory of Epigenetics for Organ Development in Preterm Infants, The Fifth Central Hospital of Tianjin, Tianjin, ChinaCollege of Biotechnology, Tianjin University of Science and Technology, Tianjin, ChinaCollege of Biotechnology, Tianjin University of Science and Technology, Tianjin, ChinaCentral Laboratory, The Fifth Central Hospital of Tianjin, Tianjin, ChinaTianjin Key Laboratory of Epigenetics for Organ Development in Preterm Infants, The Fifth Central Hospital of Tianjin, Tianjin, ChinaCollege of Biotechnology, Tianjin University of Science and Technology, Tianjin, ChinaThe small ubiquitin-related modifier (SUMOylation) system is a conserved, reversible, post-translational protein modification pathway covalently attached to the lysine residues of proteins in eukaryotic cells, and SUMOylation is catalyzed by SUMO-specific activating enzyme (E1), binding enzyme (E2) and ligase (E3). Sentrin-specific proteases (SENPs) can cleave the isopeptide bond of a SUMO conjugate and catalyze the deSUMOylation reaction. SUMOylation can regulate the activity of proteins in many important cellular processes, including transcriptional regulation, cell cycle progression, signal transduction, DNA damage repair and protein stability. Biological experiments in vivo and in vitro have confirmed the key role of the SUMO conjugation/deconjugation system in energy metabolism, Ca2+ cycle homeostasis and protein quality control in cardiomyocytes. In this review, we summarized the research progress of the SUMO conjugation/deconjugation system and SUMOylation-mediated cardiac actions based on related studies published in recent years, and highlighted the further research areas to clarify the role of the SUMO system in the heart by using emerging technologies.https://www.frontiersin.org/articles/10.3389/fcell.2023.1294717/fullSUMOheartprotein quality controlCa2+ cyclecardiac metabolism |
spellingShingle | Ying Wang Ying Wang Zhihao Liu Zhihao Liu Xiyun Bian Xiyun Bian Chenxu Zhao Xin Zhang Xiaozhi Liu Xiaozhi Liu Nan Wang Function and regulation of ubiquitin-like SUMO system in heart Frontiers in Cell and Developmental Biology SUMO heart protein quality control Ca2+ cycle cardiac metabolism |
title | Function and regulation of ubiquitin-like SUMO system in heart |
title_full | Function and regulation of ubiquitin-like SUMO system in heart |
title_fullStr | Function and regulation of ubiquitin-like SUMO system in heart |
title_full_unstemmed | Function and regulation of ubiquitin-like SUMO system in heart |
title_short | Function and regulation of ubiquitin-like SUMO system in heart |
title_sort | function and regulation of ubiquitin like sumo system in heart |
topic | SUMO heart protein quality control Ca2+ cycle cardiac metabolism |
url | https://www.frontiersin.org/articles/10.3389/fcell.2023.1294717/full |
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