The post-translational modification, SUMOylation, and cancer (Review)

被引:289
|
作者
Han, Zhi-Jian [1 ]
Feng, Yan-Hu [1 ]
Gu, Bao-Hong [2 ]
Li, Yu-Min [2 ]
Chen, Hao [2 ]
机构
[1] Lanzhou Univ, Hosp 2, Key Lab Digest Syst Tumors Gansu Prov, Lanzhou 730030, Gansu, Peoples R China
[2] Lanzhou Univ, Dept Gen Surg, Hosp 2, 82 Cui Ying Men St, Lanzhou 730030, Gansu, Peoples R China
基金
中国国家自然科学基金;
关键词
SUMO pathway; cancer; post-translational modification; SUMO protease; Ubc9; SUMO E3 LIGASE; EPITHELIAL-MESENCHYMAL TRANSITION; HEAT-SHOCK-PROTEIN; NUCLEAR-PORE COMPLEX; WIDE RNAI SCREEN; PROSTATE-CANCER; HEPATOCELLULAR-CARCINOMA; TRANSCRIPTIONAL ACTIVITY; CELL-PROLIFERATION; DNA-DAMAGE;
D O I
10.3892/ijo.2018.4280
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
SUMOylation is a reversible post-translational modification which has emerged as a crucial molecular regulatory mechanism, involved in the regulation of DNA damage repair, immune responses, carcinogenesis, cell cycle progression and apoptosis. Four SUMO isoforms have been identified, which are SUMO1, SUMO2/3 and SUMO4. The small ubiquitin-like modifier (SUMO) pathway is conserved in all eukaryotes and plays pivotal roles in the regulation of gene expression, cellular signaling and the maintenance of genomic integrity. The SUMO catalytic cycle includes maturation, activation, conjugation, ligation and de-modification. The dysregulation of the SUMO system is associated with a number of diseases, particularly cancer. SUMOylation is widely involved in carcinogenesis, DNA damage response, cancer cell proliferation, metastasis and apoptosis. SUMO can be used as a potential therapeutic target for cancer. In this review, we briefly outline the basic concepts of the SUMO system and summarize the involvement of SUMO proteins in cancer cells in order to better understand the role of SUMO in human disease.
引用
收藏
页码:1081 / 1094
页数:14
相关论文
共 50 条
  • [21] Post-translational modification of KRAS: potential targets for cancer therapy
    Wang, Wei-hua
    Yuan, Tao
    Qian, Mei-jia
    Yan, Fang-jie
    Yang, Liu
    He, Qiao-jun
    Yang, Bo
    Lu, Jin-jian
    Zhu, Hong
    ACTA PHARMACOLOGICA SINICA, 2021, 42 (08) : 1201 - 1211
  • [22] Post-Translational Modification of ZEB Family Members in Cancer Progression
    Park, Mi Kyung
    Lee, Ho
    Lee, Chang Hoon
    INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2022, 23 (23)
  • [23] Deciphering post-translational modification "codes"
    Fuchs, Stephen
    Rothbart, Scott
    Krajewski, Krzysztof
    Strahl, Brian
    PROTEIN SCIENCE, 2012, 21 : 118 - 118
  • [24] Regulation of Neurofibromin by Post-Translational Modification
    Kaleem, Afshan
    Ahmad, Ishtiaq
    Shakoori, Abdul Rauf
    Nasir-Ud-Din
    PAKISTAN JOURNAL OF ZOOLOGY, 2008, 40 (06) : 417 - 422
  • [25] Protein Post-translational Modification in Prokaryotes
    Tan Yong-Cong
    Wang Qi-Jun
    Zhao Guo-Ping
    Yao Yu-Feng
    PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS, 2011, 38 (03) : 197 - 203
  • [26] POST-TRANSLATIONAL COVALENT MODIFICATION OF PROTEINS
    UY, R
    WOLD, F
    SCIENCE, 1977, 198 (4320) : 890 - 896
  • [27] Post-translational modification of PML proteins
    Foertsch, C.
    Distel, L.
    Grabenbauer, G.
    Sauer, R.
    STRAHLENTHERAPIE UND ONKOLOGIE, 2007, 183 : 52 - 52
  • [28] Shining a light on post-translational modification
    Richards, Nigel G. J.
    HFSP JOURNAL, 2008, 2 (02): : 57 - 60
  • [29] AMPylation is a new post-translational modiFICation
    Melanie L Yarbrough
    Kim Orth
    Nature Chemical Biology, 2009, 5 : 378 - 379
  • [30] Post-translational Modification in Microviridin Biosynthesis
    Philmus, Benjamin
    Christiansen, Guntram
    Yoshida, Wesley Y.
    Hemscheidt, Thomas K.
    CHEMBIOCHEM, 2008, 9 (18) : 3066 - 3073