Abstract 2410 The constitutive Hsp70 proteins, Ssa1 and Ssa2, are critical for limiting the aggregation of the poly-A binding protein

Molecular chaperones play a pivotal role in maintaining proteostasis under normal conditions by regulating the heat shock response (HSR), refolding misfolded proteins, and disassembling aggregates. Under transient stress, such as heat shock, certain proteins and RNAs assemble into membrane-less, protective organelles called stress granules (SGs), while a heat shock response (HSR) is activated to upregulate the expression of chaperones. Once stress subsides, the upregulated chaperone network efficiently disassembles SGs.