HSP70 and HSP90 in neurodegenerative diseases.

• This review outlines chaperone machinery of HSP70 and HSP90. • Roles of HSP70 and HSP90 and their co-chaperons are summarized in various neurodegenerative diseases. • Pharmacological inhibition of HSP90 as a potential treatment of neurodegenerative disorders is discussed. Molecular chaperones have a role to stabilize proteins or assist them in reaching their native fold. Heat shock proteins (HSPs) are a family of molecular chaperons that protect proteins from cellular stress during the assembly of protein complexes and also prevent the proteins from aggregation and disassembly. The immediate increase of HSPs is crucial for cellular adaptation to environmental changes and protection of other proteins from denaturation, thereby maintaining the cellular homeostasis and increasing the longevity of an organism. HSP70 and HSP90 are the most studied HSPs in this very large HSP family. Notably, HSP90 also stabilizes the disease-related proteins in neurodegenerative disorders. Therefore, small molecules that inhibit the HSP90 but also increase the HSP70 has been tested as potential drugs for neurodegenerative disorders. [ABSTRACT FROM AUTHOR]