Role of Molecular Chaperone Network in Understanding In Vitro Proteotoxicity

Proteins are vital biological macromolecules that regulate various indispensible pathways and processes for cellular homeostasis. Misfolded and aggregated species of proteins target the protein homeostasis of the cell and are widely implicated in several neurological and metabolic disorders. Accumulation of such proteotoxic species instigates cellular dysfunction resulting in toxicity. The cellular response to proteotoxicity is regulated by a network of various proteins such as molecular chaperones, transport, and clearance machineries and the stress signaling pathways that regulates stability and functionality of the cell. Here, we discuss the mechanisms of molecular chaperones and degradation pathways that regulate the formation and accumulation of proteotoxic species in vitro and also emphasize on protein aggregation disorders involved in the progression of various diseases and mitigation of proteotoxicity.