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文章简介组蛋白去甲基化酶在多种生命过程中发挥重要作用,这些作用以往被认为是依赖于其组蛋白去甲基化酶活性的。但其组蛋白去甲基化酶非依赖的活性却知之甚少。科研人员在研究中惊奇地发现,LSD2(一个广为人知的组蛋白H3K4me1/me2去甲基化酶)具备E3泛素连接酶活性。LSD2能够直接泛素化N-乙酰氨基葡萄糖转移酶(OGT),促使其发生降解。LSD2通过其E3泛素连接酶活性(而不是组蛋白去甲基化酶活性)抑制肺癌细胞系A549的细胞生长。去除LSD2能够稳定OGT并促进293细胞的克隆形成。LSD2利用其组蛋白去甲基化酶和E3泛素连
INTRODUCTION Histone demethylase plays an important role in a variety of life processes that were previously thought to be dependent on histone demethylase activity. However, its histone demethylase-independent activity is poorly understood. Researchers were surprised to find in the study that LSD2, a well-known histone H3K4me1 / me2 demethylase, possesses E3 ubiquitin ligase activity. LSD2 can directly ubiquitinate N-acetylglucosaminyltransferase (OGT), to promote its degradation. LSD2 inhibits the cell growth of lung cancer cell line A549 through its E3 ubiquitin ligase activity, but not its histone demethylase activity. Removal of LSD2 stabilizes OGT and promotes clonal formation of 293 cells. LSD2 utilizes its histone demethylase and E3 ubiquitin