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The HSP90 chaperone machinery
The HSP90 chaperone machinery
- Source :
- Nature Reviews Molecular Cell Biology. 18:345-360
- Publication Year :
- 2017
- Publisher :
- Springer Science and Business Media LLC, 2017.
-
Abstract
- The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis under both physiological and stress conditions in eukaryotic cells. As HSP90 has several hundred protein substrates (or 'clients'), it is involved in many cellular processes beyond protein folding, which include DNA repair, development, the immune response and neurodegenerative disease. A large number of co-chaperones interact with HSP90 and regulate the ATPase-associated conformational changes of the HSP90 dimer that occur during the processing of clients. Recent progress has allowed the interactions of clients with HSP90 and its co-chaperones to be defined. Owing to the importance of HSP90 in the regulation of many cellular proteins, it has become a promising drug target for the treatment of several diseases, which include cancer and diseases associated with protein misfolding.
- Subjects :
- Adenosine Triphosphatases
0301 basic medicine
Protein Folding
biology
DNA repair
Regulator
Cell Biology
Hsp90
Cell biology
03 medical and health sciences
030104 developmental biology
Immune system
Proteostasis
Chaperone (protein)
Heat shock protein
polycyclic compounds
biology.protein
Animals
Humans
Protein folding
HSP90 Heat-Shock Proteins
Molecular Biology
Molecular Chaperones
Protein Binding
Subjects
Details
- ISSN :
- 14710080 and 14710072
- Volume :
- 18
- Database :
- OpenAIRE
- Journal :
- Nature Reviews Molecular Cell Biology
- Accession number :
- edsair.doi.dedup.....a449af56edf55a6ae3366ef04104805c
- Full Text :
- https://doi.org/10.1038/nrm.2017.20