P53: Stability from the Ubiquitin-Proteasome System and Specific 26S Proteasome Inhibitors

Author(s)

do Patrocinio, Andressa Barban ; Rodrigues, Vanderlei ; Magalhaes, Lizandra Guidi

• Document type: Journal article
• Source: ACS OMEGA; v. 7, n. 5, p. 8-pg., 2022-01-27.

Abstract

Protein p53 is degraded by the 26S proteasome, a protein complex that breaks down cellular proteins. Degradation begins with activation of the protein ubiquitin (Ub) by the ubiquitin-activating E1 enzymes, ubiquitin-conjugating E2 enzymes, and ubiquitin E3 ligases, linking Ub or the polyubiquitin chain to p53 and marking it for degradation by the 26S proteasome. E3 ubiquitin ligases participate in this process and regulate p53 stabi l i t y . There are compounds that inhibit the 26S proteasome and interfere at the p53 level, and some of these inhibitors are used to treat cancer and other diseases and can stabilize tumor suppressor proteins through the p53 pathway. This review discusses how the ubiquitin-proteasome system, p53, and these compounds are related. (AU)

• FAPESP's process: 16/06769-2 - Molecular studies of deubiquitinating enzymes and its involvement in TGFb signaling pathway in the development of the reproductive system of Schistosoma mansoni
• Grantee: Vanderlei Rodrigues
• Support Opportunities: Regular Research Grants