Exposing different mechanisms of post translational modifications of OTUB1
Embargo Date
2026-03-01
OA Version
Citation
Abstract
Ubiquitination is an essential cellular process that is involved with protein degradation and migration in a cell. OTUB1 is an important deubiquitinase and implicated in many different cancer, immune response, and homeostasis pathways. OTUB1 specifically cleaves K48 poly-ubiquitin chains on target proteins. In this study, I aimed to find how different post-translational modifications of OTUB1 could influence its deubiquitinase activity in the presence and absence of UbCh5B, an OTUB1 activator. I found that phosphorylation of specific amino acid residues of OTUB1 could increase its ability to cleave K48 linked di-ubiquitin. OTUB1 decreases its K48 cleavage ability when the N-terminal helix is partially removed from the protein. These results could elucidate potential post-translational modifications for OTUB1 for future oncogenic therapies.