Small ubiquitin-like modifiers (SUMOs) regulate virtually all nuclear processes. The fate of the target protein is determined by the architecture of the attached SUMO protein, which can be of polymeric nature. Here, we highlight the multifunctional aspects of dynamic signal transduction by SUMO polymers. The SUMO-targeted ubiquitin ligases (STUbLs) RING-finger protein 4 (RNF4) and RNF111 recognize SUMO polymers in a chain-architecture-dependent manner, leading to the formation of hybrid chains, which could enable proteasomal destruction of proteins. Recent publications have highlighted essential roles for SUMO chain disassembly by the mammalian SUMO proteases SENP6 and SENP7 and the yeast SUMO protease Ulp2. SENP6 is particularly important for centromere assembly. These recent findings demonstrate the diversity of SUMO polymer signal transduction for proteolytic and nonproteolytic purposes.

小的泛素样修饰剂 (SUMO) 几乎调节所有核过程。目标蛋白的命运由附着的 SUMO 蛋白的结构决定，它可以是聚合性质的。在这里，我们重点介绍了 SUMO 聚合物动态信号转导的多功能方面。SUMO 靶向泛素连接酶 (STUbLs) 环指蛋白 4 (RNF4) 和 RNF111 以依赖于链结构的方式识别 SUMO 聚合物，导致形成杂合链，从而能够破坏蛋白质的蛋白酶体。最近的出版物强调了哺乳动物 SUMO 蛋白酶 SENP6 和 SENP7 以及酵母 SUMO 蛋白酶 Ulp2 在 SUMO 链分解中的重要作用。SENP6 对于着丝粒组装尤为重要。