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

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-mediate...

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Detalles Bibliográficos
Autores principales: Cai, Jiali, Li, Mengying, Wang, Xiang, Li, Lei, Li, Qi, Hou, Zhaoyuan, Jia, Hao, Liu, Shiyuan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Genetics
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6967296/
https://www.ncbi.nlm.nih.gov/pubmed/31998374
http://dx.doi.org/10.3389/fgene.2019.01324
Descripción
Sumario: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.

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