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Structure and Function of HECT E3 Ubiquitin Ligases and their Role in Oxidative Stress
Ubiquitination is a modification after protein transcription that plays a vital role in maintaining the homeostasis of the cellular environment. The Homologous to E6AP C-terminus (HECT) family E3 ubiquitin ligases are a kind of E3 ubiquitin ligases with a C-terminal HECT domain that mediates the bin...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Sciendo
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7500122/ https://www.ncbi.nlm.nih.gov/pubmed/32983929 http://dx.doi.org/10.2478/jtim-2020-0012 |
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author | Qian, Hao Zhang, Ying Wu, Boquan Wu, Shaojun You, Shilong Zhang, Naijin Sun, Yingxian |
author_facet | Qian, Hao Zhang, Ying Wu, Boquan Wu, Shaojun You, Shilong Zhang, Naijin Sun, Yingxian |
author_sort | Qian, Hao |
collection | PubMed |
description | Ubiquitination is a modification after protein transcription that plays a vital role in maintaining the homeostasis of the cellular environment. The Homologous to E6AP C-terminus (HECT) family E3 ubiquitin ligases are a kind of E3 ubiquitin ligases with a C-terminal HECT domain that mediates the binding of ubiquitin to substrate proteins and a variable-length N-terminal extension. HECT-ubiquitinated ligases can be divided into three categories: NEDD4 superfamily, HERC superfamily, and other HECT superfamilies. HECT ubiquitin ligase plays an essential role in the development of many human diseases. In this review, we focus on the physiological and pathological processes involved in oxidative stress and the role of E3 ubiquitin ligase of the HECT family. |
format | Online Article Text |
id | pubmed-7500122 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Sciendo |
record_format | MEDLINE/PubMed |
spelling | pubmed-75001222020-09-25 Structure and Function of HECT E3 Ubiquitin Ligases and their Role in Oxidative Stress Qian, Hao Zhang, Ying Wu, Boquan Wu, Shaojun You, Shilong Zhang, Naijin Sun, Yingxian J Transl Int Med Review Article Ubiquitination is a modification after protein transcription that plays a vital role in maintaining the homeostasis of the cellular environment. The Homologous to E6AP C-terminus (HECT) family E3 ubiquitin ligases are a kind of E3 ubiquitin ligases with a C-terminal HECT domain that mediates the binding of ubiquitin to substrate proteins and a variable-length N-terminal extension. HECT-ubiquitinated ligases can be divided into three categories: NEDD4 superfamily, HERC superfamily, and other HECT superfamilies. HECT ubiquitin ligase plays an essential role in the development of many human diseases. In this review, we focus on the physiological and pathological processes involved in oxidative stress and the role of E3 ubiquitin ligase of the HECT family. Sciendo 2020-06-30 /pmc/articles/PMC7500122/ /pubmed/32983929 http://dx.doi.org/10.2478/jtim-2020-0012 Text en © 2020 Hao Qian et al., published by Sciendo http://creativecommons.org/licenses/by-nc-nd/4.0 This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. |
spellingShingle | Review Article Qian, Hao Zhang, Ying Wu, Boquan Wu, Shaojun You, Shilong Zhang, Naijin Sun, Yingxian Structure and Function of HECT E3 Ubiquitin Ligases and their Role in Oxidative Stress |
title | Structure and Function of HECT E3 Ubiquitin Ligases and their Role in Oxidative Stress |
title_full | Structure and Function of HECT E3 Ubiquitin Ligases and their Role in Oxidative Stress |
title_fullStr | Structure and Function of HECT E3 Ubiquitin Ligases and their Role in Oxidative Stress |
title_full_unstemmed | Structure and Function of HECT E3 Ubiquitin Ligases and their Role in Oxidative Stress |
title_short | Structure and Function of HECT E3 Ubiquitin Ligases and their Role in Oxidative Stress |
title_sort | structure and function of hect e3 ubiquitin ligases and their role in oxidative stress |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7500122/ https://www.ncbi.nlm.nih.gov/pubmed/32983929 http://dx.doi.org/10.2478/jtim-2020-0012 |
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