Research Paper on Protein Degradation Mechanisms that Activate 26S Proteasomes

Description

Title: Protein Degradation Mechanisms that Activate 26S Proteasomes

Abstract: Despite the widespread belief that the only regulated step in the ubiquitin proteasome pathway is ubiquitination, recent research has revealed a number of significant mechanisms that control 26S proteasome activity. The majority of proteasomes in cells are inactive, but when they bind a substrate that has been ubiquitinated, they become active via a two-step mechanism that first requires the ubiquitin chain to associate with Usp14 and then a loosely folded protein domain to interact with the ATPases. The UBL domain of Usp14 signals the first stage of proteasome activation, and many other proteins (such as Rad23 and Parkin) also contribute to this process. When muscles atrophy, the unique activator ZFAND5 stimulates proteolysis by binding to ubiquitin conjugates and the proteasome. The phosphorylation of subunits also controls the proteasome’s activity. Rpn6 phosphorylation is stimulated within minutes by substances that increase cAMP and activate PKA, which also speeds up the selective degradation of short-lived proteins. Similarly, in target tissues, hormones, fasting, and exercise, which increase cAMP, activate proteasomes and proteolysis. In addition to stimulating 26S activities, substances that increase cGMP and activate PKG also modify different subunit(s) and promote the breakdown of long-lived cell proteins. The selective degradation of proteins that are prone to aggregation and lead to neurodegenerative diseases is improved by both kinases. Thus, the physiological significance of these novel mechanisms controlling proteolysis is obvious, as is their therapeutic potential.

Keywords: ubiquitin–proteasome system; Usp14; Rad23; UBL-domain-containing proteins; ZFAND5; PKA; PKG

Paper Quality: SCOPUS / Web of Science Level Research Paper

Subject: Biomolecules

Writer Experience: 20+ Years

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