PT  - JOURNAL ARTICLE
AU  - Yanfang Yang
AU  - Zijing Xia
AU  - Xixi Wang
AU  - Xinyu Zhao
AU  - Zenghua Sheng
AU  - Yang Ye
AU  - Gu He
AU  - Liangxue Zhou
AU  - Hongxia Zhu
AU  - Ningzhi Xu
AU  - Shufang Liang
TI  - Small molecular inhibitors targeting protein SUMOylation as novel anticancer compounds
AID  - 10.1124/mol.118.112300
DP  - 2018 Jan 01
TA  - Molecular Pharmacology
PG  - mol.118.112300
4099  - http://molpharm.aspetjournals.org/content/early/2018/05/21/mol.118.112300.short
4100  - http://molpharm.aspetjournals.org/content/early/2018/05/21/mol.118.112300.full
AB  - SUMOylation, one of post-translational modifications, is covalently modified on lysine residues of a target protein through an enzymatic cascade reaction similar to protein ubiquitination. Along with identification of many SUMOylated proteins, protein SUMOylation has been proven to regulate multiple biological activities including transcription, cell cycle, DNA repair and innate immunity. The dysregulation of protein SUMOylation and deSUMOylation modification is linked with carcinogenesis and tumor progression. The SUMOylation-associated enzymes are usually elevated in various cancers, which function as cancer biomarkers to relate to poor outcomes for patients. Considering the significance of protein SUMOylation in regulating diverse biological functions in cancer progression, numerous small-molecule inhibitors targeting protein SUMOylation pathway are developed as potentially clinical anti-cancer therapeutics. Here, we systematically summarized the latest progresses of associations of SUMO enzymes with cancers and small-molecular inhibitors against human cancers by targeting SUMOylation enzymes. We also compared the pros and cons of several special anticancer inhibitors targeting SUMO pathway. As more efforts are invested in this field, small-molecule inhibitors targeting the SUMOylation modification pathway are promising to develop into novel anticancer drugs.