Ufd1, the ubiquitin fusion degradation 1, is an essential component in the ubiquitin-proteasome pathway. It functions as a cofactor in the Cdc48-Ufd1-Npl4 complex, which is crucial for recognizing polyubiquitin-tagged proteins and facilitating their presentation to the 26S proteasome for degradation [1]. This complex is involved in eukaryotic cellular processes, such as the clearance of polyubiquitylated targets [2].

In zebrafish, allelic loss of ufd1 induces tumor cell apoptosis and impairs MYC-driven T-cell acute lymphoblastic leukemia (T-ALL) progression, suggesting Ufd1 contributes to MYC-mediated leukemia aggressiveness through suppression of the proapoptotic unfolded protein response [3]. In Enterovirus A71 (EVA71) infection, knockdown of Ufd1 significantly decreased the binding and entry of EVA71 to host cells, indicating its role in the viral entry process [4].

In conclusion, Ufd1 is vital in the ubiquitin-proteasome pathway, participating in crucial cellular processes. Its functions have been revealed through genetic models like zebrafish, highlighting its significance in leukemia and viral entry-related disease areas. Understanding Ufd1 can potentially provide new insights into the mechanisms of these diseases and offer new strategies for treatment.