USP37 Promotes Lung Cancer Cell Migration by Stabilizing Snail Protein via Deubiquitination
USP37 Promotes Lung Cancer Cell Migration by Stabilizing Snail Protein via Deubiquitination
复制标题
USP37 通过去泛素化稳定 Snail 蛋白，促进肺癌细胞迁移
DOI：
10.3389/fgene.2019.01324
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发表时间：
2020-01-10
影响因子：
3.7
通讯作者：
Liu, Shiyuan
中科院分区：
文献类型：
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作者：
Cai, Jiali;Li, Mengying;Liu, Shiyuan
Snail是一种重要的上皮-间质转化（EMT）转录因子，并促进转移。然而，Snail蛋白是不稳定的，并且通过泛素化介导的蛋白酶体途径被快速降解。去泛素化酶通过调节泛素化介导的水解过程来防止Snail降解。我们的研究表明去泛素化酶（DUB）家族成员USP 37可以使Snail去泛素化并阻止Snail的降解。USP 37与Snail共定位于细胞核中。在生物学上，USP 37的上调表达促进肺癌细胞迁移，而Snail的缺失消除了USP 37的作用。这些数据表明，USP 37是蜗牛特异性去泛素化酶，也表明转移的潜在治疗靶点。
Snail is a prominent epithelial-mesenchymal transition (EMT) transcription factor and promotes metastasis. However, Snail protein is unstable and is quickly degraded through ubiquitination-mediated proteasome pathway. Deubiquitinases prevent Snail degradation by regulating the ubiquitination-mediated hydrolysis process. Our studies demonstrate that a deubiquitinating enzyme (DUB) family member, USP37, can deubiquitinate Snail and prevent degradation of Snail. USP37 is co-localized with Snail in the nucleus. Biologically, upregulated expression of USP37 promotes lung cancer cell migration, while depletion of Snail abolishes the effect of USP37. These data demonstrate that USP37 is a Snail-specific deubiquitinase and also indicate a potential therapeutic target for metastasis.