Molecular chaperones in protein folding and proteostasis

@article{Hartl2011MolecularCI,
  title={Molecular chaperones in protein folding and proteostasis},
  author={F. Ulrich Hartl and Andreas Bracher and Manajit Hayer‐Hartl},
  journal={Nature},
  year={2011},
  volume={475},
  pages={324-332}
}
Most proteins must fold into defined three-dimensional structures to gain functional activity. But in the cellular environment, newly synthesized proteins are at great risk of aberrant folding and aggregation, potentially forming toxic species. To avoid these dangers, cells invest in a complex network of molecular chaperones, which use ingenious mechanisms to prevent aggregation and promote efficient folding. Because protein molecules are highly dynamic, constant chaperone surveillance is… 
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This review focuses on recent advances in understanding the mechanisms of chaperone action in promoting and regulating protein folding and on the pathological consequences of protein misfolding and aggregation.
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The importance of molecular chaperones in neurodegenerative diseases is focused on, advances in understanding their protective mechanisms are discussed, and they are considered exciting therapeutic targets.
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Proteostasis, the controlled balance of protein synthesis, folding, assembly, trafficking and degradation, is a paramount necessity for cell homeostasis and the fate of an Hsp70 substrate is dictated by the combination of partners (cochaperones and other chaperones that interact with HSp70 in a given cell context.
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This work reports some extracellular proteins that are reported to interfere with two qualitatively different aspects of protein aggregation formation of highly structured b-sheet rich amyloid fibrils and/or generation of amorphous protein aggregates.
Protein Folding in the Cell
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Current status of protein folding in the cell is discussed with special reference to chaperone pathways in  de novo  folding, chaperones acting downstream of the ribosome, proteostasis network and protestasis network as drug target.
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