E3 ubiquitin ligase TRIM31: A potential therapeutic target
Nian-Hua Deng, Zhen Tian, Ying-Jiao Zou, Shou-Bo Quan
Abstract
Ubiquitination is a key mechanism for post-translational protein modification, affecting protein localization, metabolism, degradation and various cellular physiological processes. Dysregulation of ubiquitination is associated with the pathogenesis of various diseases, such as tumors and cardiovascular diseases, making it a primary area of interest in biochemical research and drug development endeavors. E3 ubiquitin ligases play a pivotal role in modulating the ubiquitination of substrate proteins through their unique recognition functions. TRIM31, a member of the TRIM family of E3 ubiquitin ligases, is aberrantly expressed in different pathophysiological conditions. The biological function of TRIM31 is associated with the occurrence and development of diverse diseases. TRIM31 has been demonstrated to inhibit inflammation by promoting ubiquitin-proteasome-mediated degradation of the sensing protein NLRP3 in the inflammasome. TRIM31 mediates ubiquitination of MAVS, inducing the formation of prion-like aggregates, and triggering innate antiviral immune responses. TRIM31 is also implicated in tumor pathophysiology through its ability to promote ubiquitination of the tumor suppressor protein p53. These findings indicate that TRIM31 is a potential therapeutic target, and subsequent in-depth research of TRIM31 is anticipated to provide information on its clinical application in therapy. • The E3 ligase TRIM31 is a potential therapeutic target for various diseases. • TRIM31 regulates inflammation and innate immunity through its E3 ligase activity. • The E3 ligase TRIM31 has a dual role as a tumor suppressor or oncogene in different tumors. • The challenges and prospective advances regarding TRIM31 as a therapeutic target are presented in this paper.