Protein folding and quality control are essential for maintaining proteostasis, the balance of the proteome in cells. Newly synthesized proteins must fold into their correct three-dimensional structures to function properly. In the crowded cellular environment, misfolding and aggregation can occur, leading to toxic effects. To prevent this, cells use molecular chaperones and other mechanisms to assist in folding and to remove misfolded or aggregated proteins. The proteostasis network, which includes chaperones, the ubiquitin-proteasome system, and autophagy, ensures that proteins remain functional and properly folded. However, this network declines with age, contributing to neurodegenerative diseases and other conditions associated with protein aggregation. Molecular chaperones, such as Hsp70, Hsp90, and chaperonins, play critical roles in protein folding and quality control. They assist in the folding of newly synthesized proteins, prevent misfolding, and help in the degradation of misfolded proteins. The chaperone system is highly conserved across species and is essential for maintaining proteostasis. The ribosome also plays a role in protein folding, as the nascent polypeptide chain is folded as it is synthesized. The ribosome exit channel provides a confined environment that influences the folding process. The proteostasis network is crucial for cellular and organismal health. Disruptions in this network can lead to the accumulation of misfolded proteins and the development of diseases. Understanding the mechanisms of the proteostasis network is important for developing therapeutic strategies to treat diseases associated with protein misfolding. Research has shown that modulating the proteostasis network, such as by enhancing chaperone activity or improving protein degradation, can be beneficial in treating diseases like cancer and neurodegenerative disorders. The proteostasis network is a promising target for drug development, as it plays a key role in maintaining protein homeostasis and preventing the accumulation of toxic protein aggregates.Protein folding and quality control are essential for maintaining proteostasis, the balance of the proteome in cells. Newly synthesized proteins must fold into their correct three-dimensional structures to function properly. In the crowded cellular environment, misfolding and aggregation can occur, leading to toxic effects. To prevent this, cells use molecular chaperones and other mechanisms to assist in folding and to remove misfolded or aggregated proteins. The proteostasis network, which includes chaperones, the ubiquitin-proteasome system, and autophagy, ensures that proteins remain functional and properly folded. However, this network declines with age, contributing to neurodegenerative diseases and other conditions associated with protein aggregation. Molecular chaperones, such as Hsp70, Hsp90, and chaperonins, play critical roles in protein folding and quality control. They assist in the folding of newly synthesized proteins, prevent misfolding, and help in the degradation of misfolded proteins. The chaperone system is highly conserved across species and is essential for maintaining proteostasis. The ribosome also plays a role in protein folding, as the nascent polypeptide chain is folded as it is synthesized. The ribosome exit channel provides a confined environment that influences the folding process. The proteostasis network is crucial for cellular and organismal health. Disruptions in this network can lead to the accumulation of misfolded proteins and the development of diseases. Understanding the mechanisms of the proteostasis network is important for developing therapeutic strategies to treat diseases associated with protein misfolding. Research has shown that modulating the proteostasis network, such as by enhancing chaperone activity or improving protein degradation, can be beneficial in treating diseases like cancer and neurodegenerative disorders. The proteostasis network is a promising target for drug development, as it plays a key role in maintaining protein homeostasis and preventing the accumulation of toxic protein aggregates.