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USP37 Promotes Lung Cancer Cell Migration by Stabilizing Snail Protein via Deubiquitination

Jiali Cai1, Mengying Li2, Xiang Wang1

  • 1Department of Radiology, Changzheng Hospital, Second Military Medical University, Shanghai, China.

Frontiers in Genetics
|January 31, 2020
PubMed

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.

Keywords:
SnailUSP37cell migrationdeubiquitinationlung cancer

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