Sumoylation is an essential post-translational modification that is catalysed by a small number of modifying enzymes but regulates thousands of target proteins in a dynamic manner. Small ubiquitin-like modifiers (SUMOs) can be attached to target proteins as one or more monomers or in the form of polymers of different types. Non-covalent readers recognize SUMO-modified proteins via SUMO interaction motifs. SUMO simultaneously modifies groups of functionally related proteins to regulate predominantly nuclear processes, including gene expression, the DNA damage response, RNA processing, cell cycle progression and proteostasis. Recent progress has increased our understanding of the cellular and pathophysiological roles of SUMO modifications, extending their functions to the regulation of immunity, pluripotency and nuclear body assembly in response to oxidative stress, which partly occurs through the recently characterized mechanism of liquid–liquid phase separation. Such progress in understanding the roles and regulation of sumoylation opens new avenues for the targeting of SUMO to treat disease, and indeed the first drug blocking sumoylation is currently under investigation in clinical trials as a possible anticancer agent.

Sumoylation 是一种重要的翻译后修饰，由少量修饰酶催化，但以动态方式调节数千种靶蛋白。小的泛素样修饰剂 (SUMO) 可以作为一种或多种单体或以不同类型的聚合物的形式附着到目标蛋白质上。非共价阅读器通过 SUMO 相互作用基序识别 SUMO 修饰的蛋白质。SUMO 同时修饰功能相关的蛋白质组以调节主要的核过程，包括基因表达、DNA 损伤反应、RNA 加工、细胞周期进程和蛋白质稳态。最近的进展增加了我们对 SUMO 修饰的细胞和病理生理作用的理解，将它们的功能扩展到免疫调节，响应氧化应激的多能性和核体组装，这部分是通过最近表征的液-液相分离机制发生的。在理解苏木化的作用和调控方面取得的这些进展为靶向 SUMO 治疗疾病开辟了新途径，事实上，第一个阻断苏木化的药物目前正在临床试验中作为一种可能的抗癌剂进行研究。