Lecture
This lecture explores the molecular chaperone action of small heat shock proteins (sHsps) in proteostasis, focusing on their interaction with misfolded proteins, amyloid fibrils, and clients like CLIC1. The lecture delves into the complex and dynamic Hsp chaperone network, the mechanism of sHsps binding to mature amyloid fibrils, and their role in inhibiting fibril-associated cytotoxicity. Through single-molecule fluorescence techniques, the lecture investigates the stoichiometry and subunit architecture of sHsp-client protein complexes, providing insights into the chaperone activity of sHsps. The findings suggest that sHsps stabilize amyloid fibrils, prevent fragmentation, and mitigate fibril-associated cytotoxicity, shedding light on the potential therapeutic implications of sHsps in protein misfolding diseases.