Abstract
Ubiquitin specific protease 7 (USP7) is one of the deubiquitinating enzymes (DUB) that erases ubiquitin and protects substrate protein from degradation. Full activity of USP7 requires the C-terminal Ub-like domains fold back onto the catalytic domain, allowing the remodeling of the active site to a catalytically competent state by the C-terminal peptide. Until now, numerous proteins have been identified as substrates of USP7, which play a key role in cell cycle, DNA repair, chromatin remodeling, and epigenetic regulation. Aberrant activation or overexpression of USP7 may promote oncogenesis and viral disease, making it a target for therapeutic intervention. Currently, several synthetic small molecules have been identified as inhibitors of USP7, and applied in the treatment of diverse diseases. Hence, USP7 may be a promising therapeutic target for the treatment of cancer.
Highlights
Post-translational modification (PTM) is generally enzymatic modification of proteins following protein biosynthesis
Ubiquitin specific protease 7 (USP7) binds with Checkpoint with Forkhead and Ring domains (CHFR) in vivo and regulates its stability (Figure 6). These results indicate that USP7 may play a role in the cell cycle progression via the deubiquitination of CHFR (Oh et al, 2007)
This review illustrates our current knowledge of USP7, including its source and characterization, structure, binding partners and substrates in various biological processes
Summary
Post-translational modification (PTM) is generally enzymatic modification of proteins following protein biosynthesis. Rouge et al (2016) revealed how the C terminal 19 amino acids of the USP7 contribute to the enhancement of USP7 activity by stabilizing the ubiquitin binding conformation of the catalytic domain. Many proteins have been identified as potential substrates and binding partners of USP7, such as viral proteins, transcription factors, and epigenetic modulators (Figure 8), and most of these substrates play important roles in viral replication, immune response, tumor suppression, epigenetic control, and DNA repair.
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