Small-molecule inhibitors targeting small ubiquitin-like modifier pathway for the treatment of cancers and other diseases

Dexiang Hua; Xiaoxing Wu

doi:10.1016/j.ejmech.2022.114227

Small-molecule inhibitors targeting small ubiquitin-like modifier pathway for the treatment of cancers and other diseases

Eur J Med Chem. 2022 Apr 5:233:114227. doi: 10.1016/j.ejmech.2022.114227. Epub 2022 Feb 28.

Authors

Dexiang Hua¹, Xiaoxing Wu²

Affiliations

¹ State Key Laboratory of Natural Medicines and Department of Medicinal Chemistry, School of Pharmacy, China Pharmaceutical University, Nanjing, 211198, China.
² State Key Laboratory of Natural Medicines and Department of Medicinal Chemistry, School of Pharmacy, China Pharmaceutical University, Nanjing, 211198, China. Electronic address: wu_xiaoxing@cpu.edu.cn.

PMID: 35247754
DOI: 10.1016/j.ejmech.2022.114227

Abstract

SUMOylation is a key post-translational modification that involves the covalent attachment of small ubiquitin-like modifier (SUMO) to the lysine residues of target proteins. The well-balanced SUMOylation is essential for normal cellular behaviors, while disturbance of SUMOylation is associated with various cancers and other diseases. Herein, we summarize the structures and biological functions of proteins involved in the SUMOylation process, their dysregulation in human diseases, and the discovery of small-molecular inhibitors targeting this pathway. In addition, we highlight the emerging trends in this field.

Keywords: Cancer; Inhibitor; Post-translational modification; SENP; SUMO.

Publication types

Review

MeSH terms

Humans
Neoplasms* / drug therapy
Neoplasms* / metabolism
Protein Processing, Post-Translational
Small Ubiquitin-Related Modifier Proteins* / genetics
Small Ubiquitin-Related Modifier Proteins* / metabolism
Sumoylation
Ubiquitin / metabolism

Substances

Small Ubiquitin-Related Modifier Proteins
Ubiquitin