Both acute proteotoxic stresses that unfold proteins and expression of disease-causing
mutant proteins that expose aggregation-prone regions can promote protein aggregation …

Protein aggregates are formed in cells with profoundly perturbed proteostasis, where the
generation of misfolded proteins exceeds the cellular refolding and degradative capacity …

Stresses such as heat shock trigger the formation of protein aggregates and the induction of
a disaggregation system composed of molecular chaperones. Recent work reveals that …

The accumulation and prion‐like propagation of α‐synuclein and other amyloidogenic
proteins are associated with devastating neurodegenerative diseases. Metazoan heat shock …

The eukaryotic cell is morphologically and functionally organized as an interconnected
network of organelles that responds to stress and aging. Organelles communicate via …

The Hsp70 family of chaperones works with its co-chaperones, the nucleotide exchange
factors and J-domain proteins, to facilitate a multitude of cellular functions. Central players in …

Hsp104 is a hexameric AAA+ ATPase and protein disaggregase found in yeast, which
couples ATP hydrolysis to the dissolution of diverse polypeptides trapped in toxic …

Hsf1 is an ancient transcription factor that responds to protein folding stress by inducing the
heat-shock response (HSR) that restore perturbed proteostasis. Hsp70 chaperones …

Cellular proteostasis is maintained via the coordinated synthesis, maintenance, and
breakdown of proteins in the cytosol and organelles. While biogenesis of the mitochondrial …

The formation of insoluble inclusions in the cytosol and nucleus is associated with impaired
protein homeostasis and is a hallmark of several neurodegenerative diseases. Due to the …