Abstract
Ubiquitin conjugating enzyme E2 is an important component of the post-translational protein ubiquitination pathway, which mediates the transfer of activated ubiquitin to substrate proteins. UBE2L3, also called UBcH7, is one of many E2 ubiquitin conjugating enzymes that participate in the ubiquitination of many substrate proteins and regulate many signaling pathways, such as the NF-κB, GSK3β/p65, and DSB repair pathways. Studies on UBE2L3 have found that it has an abnormal expression in many diseases, mainly immune diseases, tumors and Parkinson’s disease. It can also promote the occurrence and development of these diseases. Resultantly, UBE2L3 may become an important target for some diseases. Herein, we review the structure of UBE2L3, and its mechanism in diseases, as well as diseases related to UBE2L3 and discuss the related challenges.
Highlights
Ubiquitination is an important posttranslational modification that regulates many cellular processes, including protein turnover and the stress response, the cell cycle, organelle synthesis, and the intracellular homeostasis maintenance [1]
We review the structure of UBE2L3 and its mechanism in diseases, as well as diseases associated with UBE2L3, and discuss the related challenges
UBE2L3 is an E2 conjugating enzyme that exists widely in eukaryotes. It plays a critical role in the ubiquitin–proteasome system (UPS)
Summary
Ubiquitination is an important posttranslational modification that regulates many cellular processes, including protein turnover and the stress response, the cell cycle, organelle synthesis, and the intracellular homeostasis maintenance [1]. The E3 ubiquitin ligase enzyme promotes the ubiquitin transfer from E2 to the substrate lysine to complete the ubiquitination process [6] (Figure 1). Ubiquitin has eight ubiquitination sites in which seven lysine residues(K6、K11、K27、K29、K33、 K48、K63) are used as receptor sites for the polyubiquitin chain formation enabling the attachment to different substrates to complete the ubiquitination process [19–21]. Due to the complexity of ubiquitination, different Ub lysine linkages can form homotypic (linked by a single residue), heterotypic, or branched chains [22, 23]. The catalytic crack in this UBE2L3 structure contains a histidine (His119) similar to the acid residue in the a3-a4 ring (D117 in UBE2D1), which is directed into the lysine of the substrate protein [24, 28, 29]. Complex), which belongs to the RBR E3 enzyme, binds to UBE2L3 to form a specific linear ubiquitin chain linked by MET1 in vitro. A large number of reports have indicated that UBE2L3 is involved in the occurrence and
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