Tag: Chaperones

ATF6 is an ER stress‑responsive transcription factor that enhances protein‑folding capacity and strengthens ER‑associated degradation. After trafficking to the Golgi and undergoing regulated proteolysis, ATF6 activates genes that restore ER proteostasis during unfolded protein accumulation.

ERAD is a central ER quality‑control pathway that recognises misfolded proteins, retrotranslocates them to the cytosol, ubiquitinates them and directs them to the proteasome. By preventing proteotoxic accumulation, ERAD preserves ER homeostasis and supports cellular proteostasis.

The proteostasis network is an integrated system of chaperones, degradation pathways and organelle‑specific quality‑control mechanisms that maintains protein folding, stability and function. By coordinating refolding, repair and degradation, cells prevent proteotoxic stress and preserve homeostasis.

The heat‑shock response (HSR) is a conserved cellular defence pathway that protects the proteome under stress. By activating HSF1 and inducing heat‑shock proteins, cells stabilise protein folding, prevent aggregation and restore proteostasis during proteotoxic conditions.

Protein quality control (PQC) is a cellular surveillance system that preserves proteome integrity by monitoring protein folding, repairing misfolded proteins and eliminating damaged or aggregated species. Through coordinated action of chaperones, the ubiquitin–proteasome system and autophagy, PQC protects cells from proteotoxic stress and maintains homeostasis.