上海交通大学学报（医学版）

上海交通大学学报(医学版) ›› 2021, Vol. 41 ›› Issue (1): 89-94.doi: 10.3969/j.issn.1674-8115.2021.01.016

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蛋白质SUMO化修饰的蛋白质组学研究述评

熊强强1(), 屠俊2, 李郡如2,3, 程金科2, 左建宏1(), 陈亚兰2()   

  1. 1.南华大学衡阳医学院转化医学研究室，衡阳 421001
    2.上海交通大学基础医学院生物化学与分子细胞生物学系，上海市肿瘤微环境与炎症重点实验室，上海 200025
    3.上海交通大学医学院2016级临床医学八年制，上海 200025
  • 出版日期:2021-01-28 发布日期:2021-02-22
  • 通讯作者: 左建宏,陈亚兰 E-mail:1216268842@qq.com;632138414@qq.com;chenyl@shsmu.edu.cn
  • 作者简介:熊强强（1993—），男，硕士生；电子信箱：1216268842@qq.com。
  • 基金资助:
    国家自然科学基金(81700701);上海交通大学医学院高水平地方高校创新团队(SSMU-ZDCX20180802);湖南省科学技术厅重点项目(2017SK2082);湖南省卫生健康委员会重点项目(20201909)

Review of proteomic study of protein SUMOylation

Qiang-qiang XIONG1(), Jun TU2, Jun-ru LI2,3, Jin-ke CHENG2, Jian-hong ZUO1(), Ya-lan CHEN2()   

  1. 1.Research Lab of Translational Medicine, Hengyang Medical School, University of South China, Hengyang 421001, China
    2.Shanghai Key Laboratory for Tumor Microenvironment and Inflammation; Department of Biochemistry and Molecular Biology, Shanghai Jiao Tong University College of Basic Medical Sciences, Shanghai 200025, China
    3.Eight-year Specialty of Grade 2016 Clinical Medicine, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China
  • Online:2021-01-28 Published:2021-02-22
  • Contact: Jian-hong ZUO,Ya-lan CHEN E-mail:1216268842@qq.com;632138414@qq.com;chenyl@shsmu.edu.cn
  • Supported by:
    Funding Information] National Natural Science Foundation of China(81700701);Innovative Research Team of High-Level Local University in Shanghai(SSMU-ZDCX20180802);Key Program of China Hunan Provincial Science & Technology Department(2017SK2082);Key Program of Health Commission of Hunan Province(20201909)

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摘要：

小分子泛素相关修饰物（small ubiquitin-related modifier，SUMO）化修饰在真核细胞中广泛存在，参与了多种信号转导和代谢途径。规模化鉴定SUMO化修饰蛋白质有助于从整体角度揭示SUMO化修饰的功能和作用机制。目前，有关SUMO化修饰位点的鉴定难度较大，如何规模化研究蛋白质的SUMO化修饰尚未有定论。基于此，该文系统分析了哺乳动物细胞中开展SUMO化修饰蛋白质组学的研究工作，并在总结其研究方法和成果的基础上，对SUMO的突变模式和富集方式进行详细分析，进而归纳出针对细胞和组织样品进行SUMO化修饰位点系统化鉴定的理想方法。

关键词: 小分子泛素相关修饰物, 小类泛素化修饰, 蛋白质组学, 质谱

Abstract:

Small ubiquitin-related modifier (SUMO) exists widely in all eukaryotic cells, which is involved in many signal transduction and metabolism pathways. Systematic identification of SUMOylated proteins is helpful to reveal the function and mechanism of SUMOylation from an overall perspective. At present, it is difficult to identify the SUMOylation sites, and how to study the SUMOylated proteins on a large scale has not been determined. This paper systematically analyzes the proteomic studies of protein SUMOylation in mammalian cells. On the basis of summarizing the research methods and achievements, the mutation mode and enrichment mode of SUMO are analyzed in detail, and then the ideal methods for systematic identification of SUMOylation sites in cells and tissues are concluded.

Key words: small ubiquitin-related modifier (SUMO), SUMOylation, proteomics, mass spectrometry

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