Abstract
Ubiquitination, the prevalent posttranslational modification, plays a crucial role in regulating protein function, localization, and degradation within cellular environments. As an E3 ubiquitin ligase, TRIM65 has been shown in various studies to facilitate the ubiquitination of specific substrates, thereby controlling inflammation, innate immune responses, cell proliferation, apoptosis, and tumor progression. Given the multifaceted and significant role of TRIM65, this review compiles existing research on TRIM65 and lays the groundwork for future studies aimed at uncovering the mechanisms of TRIM65. Further understanding of TRIM65's interactions with its substrate proteins will offer valuable insights into the molecular underpinnings of certain diseases. Additionally, by identifying small molecules or inhibitors that target TRIM65, we may be able to develop novel drugs that modulate its activity. Such research could lead to more precise and effective treatments for conditions such as chronic inflammation, autoimmune diseases, and cancer. In summary, the study of TRIM65 not only enhances our understanding of fundamental cellular processes but also opens up new perspectives and avenues for the development of innovative therapies.