SENP2 regulated the stability of β-catenin through WWOX in hepatocellular carcinoma cell
详细信息    查看全文
  • 作者:Qing-Feng Jiang (1)
    Yu-Wei Tian (1)
    Quan Shen (1)
    Huan-Zhou Xue (1)
    Ke Li (1)
  • 关键词:SENP2 ; WWOX ; Hepatocellular carcinoma cell ; SUMOylation
  • 刊名:Tumor Biology
  • 出版年:2014
  • 出版时间:October 2014
  • 年:2014
  • 卷:35
  • 期:10
  • 页码:9677-9682
  • 全文大小:600 KB
  • 参考文献:1. Jemal A, Bray F, Center MM, Ferlay J, Ward E, Forman D. Global cancer statistics. CA Cancer J Clin. 2011;61:69-0. CrossRef
    2. Maluccio M, Covey A. Recent progress in understanding, diagnosing, and treating hepatocellular carcinoma. CA: Cancer J Clin. 2012;62:394-.
    3. Geiss-Friedlander R, Melchior F. Concepts in sumoylation: a decade on. Nat Rev Mol Cell Biol. 2007;8:947-6. CrossRef
    4. Wilkinson KA, Henley JM. Mechanisms, regulation and consequences of protein sumoylation. Biochem J. 2010;428:133-5. CrossRef
    5. Sarge KD, Park-Sarge OK. Sumo and its role in human diseases. Int Rev Cell Mol Biol. 2011;288:167-3. CrossRef
    6. Hwang KW, Won TJ, Kim H, Chun HJ, Chun T, Park Y. Characterization of the regulatory roles of the sumo. Diabetes Metab Res Rev. 2011;27:854-1. CrossRef
    7. Wei W, Yang P, Pang J, Zhang S, Wang Y, Wang MH, et al. A stress-dependent sumo4 sumoylation of its substrate proteins. Biochem Biophys Res Commun. 2008;375:454-. CrossRef
    8. Wang CY, Podolsky R, She JX. Genetic and functional evidence supporting sumo4 as a type 1 diabetes susceptibility gene. Ann N Y Acad Sci. 2006;1079:257-7. CrossRef
    9. Hannoun Z, Greenhough S, Jaffray E, Hay RT, Hay DC. Post-translational modification by sumo. Toxicology. 2010;278:288-3. CrossRef
    10. Bawa-Khalfe T, Yeh ET. Sumo losing balance: sumo proteases disrupt sumo homeostasis to facilitate cancer development and progression. Genes Cancer. 2010;1:748-2. CrossRef
    11. Yeh ET. Sumoylation and de-sumoylation: wrestling with life’s processes. J Biol Chem. 2009;284:8223-. CrossRef
    12. Kim JH, Baek SH. Emerging roles of desumoylating enzymes. Biochim Biophys Acta. 2009;1792:155-2. CrossRef
    13. Jiang M, Chiu SY, Hsu W. Sumo-specific protease 2 in mdm2-mediated regulation of p53. Cell Death Differ. 2011;18:1005-5. CrossRef
    14. Chiu SY, Asai N, Costantini F, Hsu W. Sumo-specific protease 2 is essential for modulating p53-mdm2 in development of trophoblast stem cell niches and lineages. PLoS Biol. 2008;6:e310. CrossRef
    15. Zhang XD, Goeres J, Zhang H, Yen TJ, Porter AC, Matunis MJ. Sumo ?/3 modification and binding regulate the association of cenp-e with kinetochores and progression through mitosis. Mol Cell. 2008;29:729-1. CrossRef
    16. Schweizer N, Ferras C, Kern DM, Logarinho E, Cheeseman IM, Maiato H. Spindle assembly checkpoint robustness requires tpr-mediated regulation of mad1/mad2 proteostasis. J Cell Biol. 2013;203:883-3. CrossRef
    17. Cubenas-Potts C, Goeres JD, Matunis MJ. Senp1 and Senp2 affect spatial and temporal control of sumoylation in mitosis. Mol Biol Cell. 2013;24:3483-5. CrossRef
    18. Lu H, Liu B, You S, Chen L, Dongmei Q, Gu M, Lu Y, Chen Y, Zhang F, Yu B: Senp2 regulates mef2a de-sumoylation in an activity dependent manner. Mol Biol Rep. 2012
    19. Kang X, Qi Y, Zuo Y, Wang Q, Zou Y, Schwartz RJ, et al. Sumo-specific protease 2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development. Mol Cell. 2010;38:191-01. <
  • 作者单位:Qing-Feng Jiang (1)
    Yu-Wei Tian (1)
    Quan Shen (1)
    Huan-Zhou Xue (1)
    Ke Li (1)

    1. Department of Hepatobiliary Surgery, Henan Provincial People’s Hospital, Zhengzhou, 450003, Henan, China
  • ISSN:1423-0380
文摘
SUMOylation and deSUMOylation are dynamic mechanisms regulating a spectrum of protein activities. The SUMO proteases (SENP) remove SUMO conjugate from proteins, and their expression is deregulated in cancers. SENP2 has been reported to play a critical role in the control of hepatocellular carcinoma (HCC) cell growth by modulating the stability of β-catenin. However, the underlying mechanism remains largely unknown. Here, we show that the WW domain-containing oxidoreductase (WWOX), a novel inhibitor of the Wnt/β-catenin pathway, is required for stabilization of β-catenin regulated by SENP2 in HCC cells. The transcriptional level of WWOX is tightly regulated by SENP2. Moreover, knockdown of WWOX by siRNA attuned SENP2-induced β-catenin degradation and decreased SENP2-mediated HCC cell proliferation arrest. Taken together, our data suggested that WWOX is a key downstream modulator of the SENP2 tumor suppressor function in HCC cell.

© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号

地址:北京市海淀区学院路29号 邮编:100083

电话:办公室:(+86 10)66554848;文献借阅、咨询服务、科技查新:66554700