Proteostasis Regulation: Chaperone Interactions and Post-Translational Modifications

This lecture delves into the intricate world of proteostasis regulation, focusing on the interactions between chaperones and post-translational modifications (PTMs). The instructor explores how Hsp70, a key chaperone, interacts with various proteins in the cell, shedding light on the crucial role of chaperones in maintaining protein homeostasis. Through advanced techniques like XL-MS, the lecture uncovers the complex network of biologically-important PTM-associated interactions, providing insights into protein folding, misfolding, and aggregation. The study of Hsp70's binding to PTMs and its impact on client interactions opens new avenues for understanding protein quality control mechanisms and their relevance in health and disease.