Allosteric regulation of the 20S proteasome by the Catalytic Core Regulators (CCRs) family.

ABSTRACT: Controlled degradation of proteins is necessary for ensuring their abundance and sustaining a healthy and accurately functioning proteome. One of the degradation routes involves the uncapped 20S proteasome, which cleaves proteins with a partially unfolded region, including those that are damaged or contain intrinsically disordered regions. This degradation route is tightly controlled by a recently discovered family of proteins named Catalytic Core Regulators (CCRs). Here, we show that CCRs function through an allosteric mechanism, coupling the physical binding of the PSMB4 β-subunit with attenuation of the complex's three proteolytic activities. In addition, by dissecting the structural properties that are required for CCR-like function, we could recapitulate this activity using a designed

SUBMITTER: Deshmukh FK 

PROVIDER: S-EPMC10229617 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature