Regulation of cell functions by deubiquitinating enzymes

1)去泛素化酶USP18通过将非天然缺陷蛋白隔离到人类细胞中的攻击基因组中来保护细胞免受非天然缺陷蛋白的毒性。2）鉴定了与去泛素化酶USP36的核仁定位信号结合的小分子，并且显示其抑制人类细胞中的核仁定位以及USP36的功能。3)USP37中的泛素相互作用基序（UIM）显示通过结合泛素链并将其稳定定位在USP37催化核心附近，在增加USP37对泛素链的异肽酶活性中发挥作用。

1) Deubiquitinating enzyme USP18 was implicated in the protection of cells from the toxicity of non-native defective proteins by sequestering them to the aggresome in human cells.2) Small molecules that bind to the nucleolar localization signal of deubiquitinating enzyme USP36 were identified and were shown to inhibit the nucleolar localization as well as the function of USP36 in human cells. 3) The ubiquitin-interacting motifs (UIMs) in USP37 were shown to play a role in increasing the isopeptidase activity of USP37 toward ubiquitin chains by binding to the ubiquitin chains and stably positioning them in close proximity to the catalytic core of USP37.