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

被引:47
作者
Cai, Jiali [1 ]
Li, Mengying [2 ]
Wang, Xiang [1 ]
Li, Lei [3 ]
Li, Qi [2 ]
Hou, Zhaoyuan [2 ,3 ,4 ]
Jia, Hao [2 ,4 ]
Liu, Shiyuan [1 ]
机构
[1] Second Mil Med Univ, Changzheng Hosp, Dept Radiol, Shanghai, Peoples R China
[2] Shanghai Jiao Tong Univ, Shanghai Tongren Hosp, Fac Basic Med, Hongqiao Inst Med,Sch Med, Shanghai, Peoples R China
[3] Lanling Peoples Hosp, Dept Thorac Surg, Linyi, Shandong, Peoples R China
[4] Shanghai Jiao Tong Univ, Dept Biochem & Mol Cellular Biol, Shanghai Key Lab Tumor Microenvironm & Inflammat, Sch Med, Shanghai, Peoples R China
基金
美国国家科学基金会;
关键词
deubiquitination; USP37; Snail; cell migration; lung cancer; EPITHELIAL-MESENCHYMAL TRANSITION; E-CADHERIN; UBIQUITIN; METASTASIS; CARCINOMA; EMT; PHOSPHORYLATION; SPECIFICITY; EXPRESSION; REPRESSION;
D O I
10.3389/fgene.2019.01324
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
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.
引用
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页数:9
相关论文
共 44 条
[1]  
Cercelaru L, 2017, ROM J MORPHOL EMBRYO, V58, P761
[2]   Twist and Snail/Slug Expression in Oropharyngeal Squamous Cell Carcinoma in Correlation With Lymph Node Metastasis [J].
Cho, Yoon Ah ;
Kim, Eun Kyung ;
Cho, Byoung Chul ;
Koh, Yoon Woo ;
Yoon, Sun Och .
ANTICANCER RESEARCH, 2019, 39 (11) :6307-6316
[3]   The deubiquitylase USP37 links REST to the control of p27 stability and cell proliferation (vol 32, pg 1691, 2012) [J].
Das, C. M. ;
Taylor, P. ;
Gireud, M. ;
Singh, A. ;
Lee, D. ;
Fuller, G. ;
Ji, L. ;
Fangusaro, J. ;
Rajaram, V. ;
Goldman, S. ;
Eberhart, C. ;
Gopalakrishnan, V. .
ONCOGENE, 2016, 35 (47) :6153-6154
[4]   Regulation of the protein stability of EMT transcription factors [J].
Diaz, V. M. ;
Vinas-Castells, R. ;
Garcia de Herreros, A. .
CELL ADHESION & MIGRATION, 2014, 8 (04) :418-428
[5]   F-box proteins: Keeping the epithelial-to-mesenchymal transition (EMT) in check [J].
Diaz, Victor M. ;
de Herreros, Antonio Garcia .
SEMINARS IN CANCER BIOLOGY, 2016, 36 :71-79
[6]   Loss of FBP1 by Snail-Mediated Repression Provides Metabolic Advantages in Basal-like Breast Cancer [J].
Dong, Chenfang ;
Yuan, Tingting ;
Wu, Yadi ;
Wang, Yifan ;
Fan, Teresa W. M. ;
Miriyala, Sumitra ;
Lin, Yiwei ;
Yao, Jun ;
Shi, Jian ;
Kang, Tiebang ;
Lorkiewicz, Pawel ;
St Clair, Daret ;
Hung, Mien-Chie ;
Evers, B. Mark ;
Zhou, Binhua P. .
CANCER CELL, 2013, 23 (03) :316-331
[7]   The SUMO guards for SNAIL [J].
Ye, Xin ;
Weinberg, Robert A. .
ONCOTARGET, 2017, 8 (58) :97701-97702
[8]   USP37 deubiquitinates Cdt1 and contributes to regulate DNA replication [J].
Hernandez-Perez, Santiago ;
Cabrera, Elisa ;
Amoedo, Hugo ;
Rodriguez-Acebes, Sara ;
Koundrioukoff, Stephane ;
Debatisse, Michelle ;
Mendez, Juan ;
Freire, Raimundo .
MOLECULAR ONCOLOGY, 2016, 10 (08) :1196-1206
[9]   UBIQUITIN, PROTEASOMES, AND THE REGULATION OF INTRACELLULAR PROTEIN-DEGRADATION [J].
HOCHSTRASSER, M .
CURRENT OPINION IN CELL BIOLOGY, 1995, 7 (02) :215-223
[10]   Deubiquitinase USP37 Is Activated by CDK2 to Antagonize APCCDH1 and Promote S Phase Entry [J].
Huang, XiaoDong ;
Summers, Matthew K. ;
Pham, Victoria ;
Lill, Jennie R. ;
Liu, Jinfeng ;
Lee, Gwanghee ;
Kirkpatrick, Donald S. ;
Jackson, Peter K. ;
Fang, Guowei ;
Dixit, Vishva M. .
MOLECULAR CELL, 2011, 42 (04) :511-523