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[泛素-蛋白酶体系统与精子DNA修复:最新进展]

[Ubiquitin-proteasome system and sperm DNA repair: An update].

作者信息

Zhang Guo-Wei, Cai Hong-Cai, Shang Xue-Jun

机构信息

Department of Andrology, Jinling Hospital Affiliated to Southern Medical University / Nanjing General Hospital of Nanjing Military Region, Nanjing, Jiangsu 210002, China.

出版信息

Zhonghua Nan Ke Xue. 2016 Sep;22(9):834-837.

PMID:29071883
Abstract

The ubiquitin-proteasome system (UPS) is a proteasome system widely present in the human body, which is composed of ubiquitin (Ub), ubiquitin activating enzymes (E1), ubiquitin conjugating enzymes (E2), ubiquitin protein ligases (E3), 26S proteasome, and deubiquitinating enzymes (DUBs) and involved in cell cycle regulation, immune response, signal transduction, DNA repair as well as protein degradation. Sperm DNA is vulnerable to interference or damage in the progression of chromosome association and homologous recombination. Recent studies show that UPS participates in DNA repair in spermatogenesis by modulating DNA repair enzymes via ubiquitination, assisting in the identification of DNA damage sites, raising damage repair-related proteins, initiating the DNA repair pathway, maintaining chromosome stability, and ensuring the normal process of spermatogenesis.

摘要

泛素-蛋白酶体系统(UPS)是广泛存在于人体中的一种蛋白酶体系统,它由泛素(Ub)、泛素激活酶(E1)、泛素结合酶(E2)、泛素蛋白连接酶(E3)、26S蛋白酶体和去泛素化酶(DUBs)组成,参与细胞周期调控、免疫反应、信号转导、DNA修复以及蛋白质降解。精子DNA在染色体联会和同源重组过程中容易受到干扰或损伤。最近的研究表明,UPS通过泛素化调节DNA修复酶、协助识别DNA损伤位点、提高损伤修复相关蛋白、启动DNA修复途径、维持染色体稳定性以及确保精子发生的正常过程,参与精子发生过程中的DNA修复。

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引用本文的文献

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Structure and Function of HECT E3 Ubiquitin Ligases and their Role in Oxidative Stress.HECT E3泛素连接酶的结构与功能及其在氧化应激中的作用
J Transl Int Med. 2020 Jun 30;8(2):71-79. doi: 10.2478/jtim-2020-0012. eCollection 2020 Jun.
2
CSN6 promotes tumorigenesis of gastric cancer by ubiquitin-independent proteasomal degradation of p16.CSN6通过对p16进行非泛素依赖性蛋白酶体降解来促进胃癌的肿瘤发生。
Cancer Biol Med. 2019 Aug;16(3):514-529. doi: 10.20892/j.issn.2095-3941.2018.0410.
3
Deubiquitinating Enzymes and Bone Remodeling.
去泛素化酶与骨重塑
Stem Cells Int. 2018 Jul 8;2018:3712083. doi: 10.1155/2018/3712083. eCollection 2018.