Department of Cell and Chemical Biology, Leiden University Medical Center, Albinusdreef 2, 2333, ZA, Leiden, The Netherlands.
Department of Cell and Chemical Biology, Leiden University Medical Center, Albinusdreef 2, 2333, ZA, Leiden, The Netherlands.
Trends Biochem Sci. 2021 Feb;46(2):113-123. doi: 10.1016/j.tibs.2020.09.002. Epub 2020 Sep 29.
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.
小泛素样修饰物 (SUMO) 几乎调控所有核内进程。靶蛋白的命运取决于附着的 SUMO 蛋白的结构，它可以具有聚合性质。在这里，我们强调了 SUMO 聚合物动态信号转导的多功能性。SUMO 靶向泛素连接酶 (STUbL) RING 指蛋白 4 (RNF4) 和 RNF111 以依赖于链结构的方式识别 SUMO 聚合物，导致形成混合链，这可能使蛋白质被蛋白酶体破坏。最近的出版物强调了哺乳动物 SUMO 蛋白酶 SENP6 和 SENP7 和酵母 SUMO 蛋白酶 Ulp2 对 SUMO 链解体的重要作用。SENP6 对着丝粒组装尤为重要。这些最近的发现表明 SUMO 聚合物信号转导具有用于蛋白水解和非蛋白水解目的的多样性。
