Ube3c, an E3 ubiquitin ligase, plays crucial roles in multiple biological processes. It is involved in pathways such as autophagy, endoplasmic reticulum-associated degradation (ERAD), antiviral innate immune response, and Wnt/β-catenin signaling. Its function in ubiquitination of target proteins is vital for regulating protein stability and activity, thus influencing cell growth, proliferation, and viral infection responses [1-5, 8-10].

In autophagy, Ube3c was identified as a new E3 ligase of ATG4B. It assembles K33-branched ubiquitin chains on ATG4B at Lys119, inhibiting autophagy flux without causing ATG4B degradation [1]. In ERAD, Ube3c facilitates the degradation of misfolded CFTR and ABCB1, even in the absence of RNF5/185 [2]. In antiviral response, Ube3c restricts EV-A71 replication by promoting K33/K48-linked ubiquitination degradation of the viral 2C protein [3]. In cancer, Ube3c promotes breast and gastric cancer progression by activating the Wnt/β-catenin signaling pathway [4,5].

In conclusion, Ube3c is essential for regulating autophagy, ERAD, antiviral response, and cancer cell behaviors through its ubiquitination-related functions. Studies on Ube3c, especially those using gene-knockout models in relevant disease areas like cancer and viral infection, have provided insights into its role in these biological processes, potentially guiding new therapeutic strategies.