Ube2g1, an ubiquitin-conjugating enzyme, is a key factor in ubiquitination, which is closely related to the post-translation modification of proteins and plays vital roles in many biological processes and immune defense pathways [2]. It is involved in the regulation of various cellular functions, and its activity is crucial for the proper functioning of the ubiquitin-proteasome system.

In the context of osteoarthritis, circRNA-UBE2G1, which may be related to the Ube2g1 gene, was found to be significantly increased in OA tissues. Inhibition of circRNA-UBE2G1 reduced the effects of LPS on C28/I2 cells viability and apoptosis, suggesting it may facilitate OA progression via the miR-373/HIF-1a axis [1].

In large yellow croaker, the ubiquitin-binding enzyme E2G1 (LcUbe2g1) was activated by the infection of Pseudomonas plecoglossicida, and it interacted with NEDD8 to co-regulate the ubiquitination process, indicating its importance in the immune response against this infection [2].

In multiple myeloma, UBE2G1 cooperates with UBE2D3 to promote the K48-linked polyubiquitination of CRL4CRBN neomorphic substrates. Blockade of UBE2G1 diminishes the ubiquitination and degradation of these substrates, conferring drug resistance to lenalidomide and pomalidomide [3].

In summary, Ube2g1 is essential for ubiquitination-related processes. Its dysregulation is associated with diseases such as osteoarthritis, infectious diseases in fish, and multiple myeloma. Studies on Ube2g1 contribute to understanding the mechanisms of these diseases and may offer potential therapeutic targets [1,2,3].