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Current and future directions of USP7 interactome in cancer study.
- Source :
-
BBA - Reviews on Cancer . Nov2023, Vol. 1878 Issue 6, pN.PAG-N.PAG. 1p. - Publication Year :
- 2023
-
Abstract
- The ubiquitin-proteasome system (UPS) is an essential protein quality controller for regulating protein homeostasis and autophagy. Ubiquitination is a protein modification process that involves the binding of one or more ubiquitins to substrates through a series of enzymatic processes. These include ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). Conversely, deubiquitination is a reverse process that removes ubiquitin from substrates via deubiquitinating enzymes (DUBs). Dysregulation of ubiquitination-related enzymes can lead to various human diseases, including cancer, through the modulation of protein ubiquitination. The most structurally and functionally studied DUB is the ubiquitin-specific protease 7 (USP7). Both the TRAF and UBL domains of USP7 are known to bind to the [P/A/E]-X-X-S or K-X-X-X-K motif of substrates. USP7 has been shown to be involved in cancer pathogenesis by binding with numerous substrates. Recently, a novel substrate of USP7 was discovered through a systemic analysis of its binding motif. This review summarizes the currently discovered substrates and cellular functions of USP7 in cancer and suggests putative substrates of USP7 through a comprehensive systemic analysis. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 0304419X
- Volume :
- 1878
- Issue :
- 6
- Database :
- Academic Search Index
- Journal :
- BBA - Reviews on Cancer
- Publication Type :
- Academic Journal
- Accession number :
- 174014008
- Full Text :
- https://doi.org/10.1016/j.bbcan.2023.188992