Protein Disaggregation by Hsp70 Chaperone System

This lecture by the instructor covers the role of the Hsp70 chaperone system in controlling protein disaggregation and refolding. It discusses how Hsp70, Hsp40, and Hsp104 chaperones work together to modify aggregates, bind to aggregates, and activate disaggregation, ultimately leading to protein refolding. The lecture also explores the significance of aggregate modification for protein disaggregation and the different modes of Ssa1 recruitment to aggregates driven by Sis1 and Ydj1. Additionally, it delves into the interaction between Sis1 and Hsp70's EEVD-motif in aggregate remodeling. Various experiments and models are presented to illustrate the mechanisms and outcomes of protein disaggregation by the Hsp70 chaperone system.