USP7’s deubiquitination of ubiquitinated substrates
Embargo Date
2027-10-21
OA Version
Citation
Abstract
Ubiquitination is the biological mechanism by which proteins are marked for degradation by attaching ubiquitin molecules. This process is a crucial post-translational modification that governs the stability and operational effectiveness of numerous proteins (Popovic, Vucic, & Dikic, 2014). It is tightly regulated and can be reversed by enzymes known as deubiquitinases (Dai et al., 2020). One such deubiquitinase is USP7; USP7 significantly influences the levels of various proteins, such as tumor suppressors, transcription factors, epigenetic modulators, DNA repair proteins, and immune response-regulators. Cancer, among other diseases, can arise due to dysregulation of the deubiquitinase enzyme, USP7 (G. Saha, S. Roy, M. Basu, & M. K. Ghosh, 2023). Thus, USP7 emerges as a compelling candidate for targeted therapeutic interventions, offering promising avenues in the pursuit of effective cancer treatments. This study seeks to look at USP7’s capability to identify and deubiquitinate three cancer relevant proteins: p53, MDM2, and DNMT1. In order to do so, select sequences of these proteins will be synthesized, ubiquitinated at a pre-determined site, and the ability of USP7 ability to remove the ubiquitin will be quantified.
Description
2024
License
Attribution 4.0 International