Affiliation:
1. Department of General Surgery, The Second Affiliated Hospital of Nanjing Medical University, Nanjing 210011, China
Abstract
:
Ubiquitination, a crucial post-translational modification, plays a role in nearly all
physiological processes. Its functional execution depends on a series of catalytic reactions
involving numerous proteases. TRIM26, a protein belonging to the TRIM family, exhibits E3
ubiquitin ligase activity because of its RING structural domain, and is present in diverse cell
lineages. Over the last few decades, TRIM26 has been documented to engage in numerous
physiological and pathological processes as a controller, demonstrating a diverse array of
biological roles. Despite the growing research interest in TRIM26, there has been limited attention
given to examining the protein's structure and function in existing reviews. This review begins with
a concise overview of the composition and positioning of TRIM26 and then proceeds to examine
its roles in immune response, viral invasion, and inflammatory processes. Simultaneously, we
demonstrate the contribution of TRIM26 to the progression of various diseases, encompassing
numerous malignancies and neurologic conditions. Finally, we have investigated the potential
areas for future research on TRIM26.
Publisher
Bentham Science Publishers Ltd.