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Protein ubiquitination is one type of post-translational modification that can alter many properties of the protein-stability, activity, subcellular location, binding affinity for other proteins, etc. It has been involved in almost all life activities, including immune response regulation, DNA damage repair, cell cycle regulation, cell proliferation, apoptosis, and protein degradation. Moreover, it is associated with many kinds of disease, such as neurodegenerative diseases, various tumors, immune diseases, and metabolic diseases. Recent reports revealed that protein ubiquitination plays a key role in the breast cancer (BC) immune evasion. "Immune evasion" refers to the ability of tumor cells/pathogens to evade recognition and attack by the immune system through different mechanisms; it includes three interconnected processes: "immune editing," "antigenic variation," and "immunosuppressive molecules expression." These three points lead to the difficulty for the body to clear the transformed cells/pathogens promptly. Here, we summarize the mechanisms of protein ubiquitination in breast cancer immune evasion and explore new strategies targeting protein ubiquitination to combat BC.
Wu et al. (Mon,) studied this question.