泛素折叠修饰因子1作用的研究进展

泛素折叠修饰因子1(Ufm1)是最近发现的一种类泛素蛋白,其三级结构与泛素十分类似,但其氨基酸序列与泛素只有16%的相似性。Ufm1及其修饰系统广泛、稳定地存在于多细胞生物中。Ufm1结合到靶蛋白需要通过一系列的酶级联反应,首先Ufm1被Uab5激活,然后转移给Ufc1及Ufl1,最后Ufm1与靶蛋白结合,并对其进行加工、修饰。Ufm1及其修饰系统参与了内质网应激及其诱导的凋亡,同时也参与了细胞周期、细胞存活、脂肪酸β氧化等生物过程的调控,为进一步研究Ufm1的功能提供了新的方向。

Research Advance in the Effect of Ubiquitin Fold Modifier 1

Ufm1 has recently been identified as a novel ubiquitin-like protein,displaying a similar tertiary structure,although only sharing 16％ sequence identity with ubiquition.Ufm1 and its protein-conjugating system extensively and stably exist in multicellutar organism.Ufm1 conjugates with target protein（s） through an enzymatic cascade analogous to ubiquitylation,consisting of activating,conjugating and ligating enzymes.Recently researchs identified that Ufm1 and its protein-conjugating system participated in endoplasmic reticulum（ER） stress and ER stress-induced apoptosis,and involved in the regulation of cell cycle,cell survival,β-oxidation of fatty acids,which all provide a new direction to further explore the function of Ufm1.