SUMO家族是一种类似于泛素的蛋白质修饰分子。它的蛋白质修饰机制与泛素化的机制相似：两者都涉及到修饰酶E1、结合酶E2和底物特异性连接酶E3。然而，多泛素化可能导致底物蛋白的降解，而多SUMO化只有在被泛素识别为信号因子后，才通过泛素体通路引起底物蛋白的降解。目前报告了SUMO家族的五个亚型，即SUMO1-5。作为一种可逆的动态修饰，细胞内的SUMO特异性蛋白酶（SENPs）主要调节SUMO化的反应逆向路径。SUMO化修饰系统影响细胞内蛋白的定位、激活和降解，并参与调控大部分核内和核外的分子反应。与SUMOylation途径相关的蛋白异常表达在肿瘤中常见，表明该途径与肿瘤的发生、转移和侵袭密切相关。本综述主要讨论与SUMOylation途径相关的蛋白质家族成员的构成，SUMOylation与其他蛋白质翻译后修饰之间的相互连接，以及基于这些途径开发的治疗药物。版权所有 © 2023. Elsevier Inc. 发表。

The SUMO family is a type of ubiquitin-like protein modification molecule. Its protein modification mechanism is similar to that of ubiquitination: both involve modifier-activating enzyme E1, conjugating enzyme E2 and substrate-specific ligase E3. However, polyubiquitination can lead to the degradation of substrate proteins, while poly-SUMOylation only leads to the degradation of substrate proteins through the proteasome pathway after being recognized by ubiquitin as a signal factor. There are currently five reported subtypes in the SUMO family, namely SUMO1-5. As a reversible dynamic modification, intracellular sentrin/SUMO-specific proteases (SENPs) mainly regulate the reverse reaction pathway of SUMOylation. The SUMOylation modification system affects the localization, activation and turnover of proteins in cells and participates in regulating most nuclear and extranuclear molecular reactions. Abnormal expression of proteins related to the SUMOylation pathway is commonly observed in tumors, indicating that this pathway is closely related to tumor occurrence, metastasis and invasion. This review mainly discusses the composition of members in the protein family related to SUMOylation pathways, mutual connections between SUMOylation and other post-translational modifications on proteins as well as therapeutic drugs developed based on these pathways.Copyright © 2023. Published by Elsevier Inc.