The Post-Translational Role of UFMylation in Physiology and Disease.
The Post-Translational Role of UFMylation in Physiology and Disease.
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泛素折叠修饰因子1（UFM1）是一种新发现的泛素样蛋白，在多细胞生物进化过程中一直保持着保守性。以类似于泛素的方式，UFM1可以通过专用的酶级联反应与底物的赖氨酸残基共价连接。尽管到目前为止已经确定了有限数量的底物，但UFM1修饰（UFMylation）已被证明在多种细胞活动中起重要作用，包括哺乳动物发育、核糖体生物合成、DNA损伤反应、内质网应激反应、免疫反应和肿瘤发生。在这篇综述中，我们总结了什么是已知的UFM 1酶级联及其生物学功能，并讨论了最近确定的底物。我们还探讨了UFMylation在人类疾病中的病理作用以及相应的潜在治疗靶点和策略。
Ubiquitin-fold modifier 1 (UFM1) is a newly identified ubiquitin-like protein that has been conserved during the evolution of multicellular organisms. In a similar manner to ubiquitin, UFM1 can become covalently linked to the lysine residue of a substrate via a dedicated enzymatic cascade. Although a limited number of substrates have been identified so far, UFM1 modification (UFMylation) has been demonstrated to play a vital role in a variety of cellular activities, including mammalian development, ribosome biogenesis, the DNA damage response, endoplasmic reticulum stress responses, immune responses, and tumorigenesis. In this review, we summarize what is known about the UFM1 enzymatic cascade and its biological functions, and discuss its recently identified substrates. We also explore the pathological role of UFMylation in human disease and the corresponding potential therapeutic targets and strategies.
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