Bidirectional substrate shuttling between the 26S proteasome and the Cdc48 ATPase promotes protein degradation

Folded proteins cannot be degraded directly by the 26S proteasome and, therefore, require prior unfolding by the Cdc48 ATPase. Li et  al. use purified yeast components to reconstitute Cdc48-dependent protein degradation by the proteasome. They show that substrates are shuttled between the two molecular machines before being degraded.

Source: Molecular Cell - February 23, 2024 Category: Cytology Authors: Hao Li, Zhejian Ji, Joao A. Paulo, Steven P. Gygi, Tom A. Rapoport Tags: Article Source Type: research