Gutierrez-Morton Emily, Wang Yanchang
Department of Biomedical Sciences, College of Medicine, Florida State University, 1115 West Call Street, Tallahassee, FL, 32306-4300, USA.
Cell Insight. 2024 Sep 10;3(6):100199. doi: 10.1016/j.cellin.2024.100199. eCollection 2024 Dec.
As a type of protein post-translational modification, SUMOylation is the process that attaches a small ubiquitin-like modifier (SUMO) to lysine residues of protein substrates. Not only do SUMO and ubiquitin exhibit structure similarity, but the enzymatic cascades for SUMOylation and ubiquitination are also similar. It is well established that protein ubiquitination triggers proteasomal degradation, but the function of SUMOylation remains poorly understood compared to ubiquitination. Recent studies reveal the role of SUMOylation in regulating protein localization, stability, and interaction networks. SUMO can be covalently attached to substrates either as an individual monomer (monoSUMOylation) or as a polymeric SUMO chain (polySUMOylation). Strikingly, mono- and polySUMOylation likely play distinct roles in protein subcellular localization and the assembly/disassembly of biomolecular condensates, which are membraneless cellular compartments with concentrated biomolecules. In this review, we summarize the recent advances in the understanding of the function and regulation of SUMOylation, which could reveal potential therapeutic targets in disease pathogenesis.
作为一种蛋白质翻译后修饰，小泛素样修饰（SUMO）化是将一个小泛素样修饰物（SUMO）连接到蛋白质底物赖氨酸残基上的过程。SUMO与泛素不仅结构相似，而且SUMO化和泛素化的酶促级联反应也相似。众所周知，蛋白质泛素化会触发蛋白酶体降解，但与泛素化相比，SUMO化的功能仍知之甚少。最近的研究揭示了SUMO化在调节蛋白质定位、稳定性和相互作用网络中的作用。SUMO可以作为单个单体（单SUMO化）或作为聚合SUMO链（多SUMO化）共价连接到底物上。引人注目的是，单SUMO化和多SUMO化可能在蛋白质亚细胞定位以及生物分子凝聚物的组装/解聚中发挥不同作用，生物分子凝聚物是富含生物分子的无膜细胞区室。在这篇综述中，我们总结了在理解SUMO化功能和调控方面的最新进展，这可能揭示疾病发病机制中的潜在治疗靶点。
