RESUMO
Autophagy is a common cellular metabolic process, which is characterized by the formation of double membrane structures named autophagosomes to degrade intracellular components or invading foreign substances to maintain cellular homeostasis. Autophagy is crucial for maintaining cell homeostasis. The dysfunction of autophagy is closely related to the occurrence and development of various diseases, including tumors, neurodegenerative diseases, viral infection, immune diseases and so on. Autophagy may be a potential therapeutic target for these diseases. Therefore, the investigation of autophagy regulation is a hot issue in life science and medical research. The TRIM (tripartite motif-containing proteins) family is a set of proteins with E3 ubiquitin ligase activity and usually contains three conserved domains, a RING zinc finger structure, a B-box structure and a coiled helix domain. Many TRIM family members have been found to play important roles in autophagy regulation, the mechanism of which include modulating autophagy-related signaling pathways, regulating autophagy core molecules and acting as autophagy receptors, etc. TRIMs participate in many biological pathways through regulating autophagy, such as immunity, virus infection and tumors. This review covers the role of TRIM proteins in regulating autophagy, the molecular mechanism and the corresponding biological effects.