The role of molecular chaperones and protein quality control Systems in disease

Abstract

Protein homeostasis, or proteostasis, is essential for cell health as it includes a network of chaperones and degradation mechanisms that control proper protein function. Major chaperones such as Hsp70, Hsp90, Hsp60, and GRP78, prevent protein aggregation, allow correct folding, and aid in the removal of damaged proteins. During stress, specialist systems like ER-associated degradation and unfolded protein responses help to maintain proteostasis across various cell compartments. This article studies how proteostasis failures are linked to neurodegenerative diseases such as Alzheimer's and Parkinson's, where chaperones lead to harmful protein buildup in neurons. Chaperones, on the other hand, increase cancer cell survival by stabilizing dangerous proteins. Thus, chaperones can be both harmful and beneficial, making them promising for therapeutic interventions.