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Heat Shock Proteins and Inflammasomes
Open AccessReview

Hsp90 and Its Co-Chaperones in Neurodegenerative Diseases

1
Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Street, 02-093 Warsaw, Poland
2
Mossakowski Medical Research Centre, Polish Academy of Sciences, 5 Pawińskiego Street, 02-106 Warsaw, Poland
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(20), 4976; https://doi.org/10.3390/ijms20204976
Received: 19 September 2019 / Revised: 3 October 2019 / Accepted: 4 October 2019 / Published: 9 October 2019
Proper folding is crucial for proteins to achieve functional activity in the cell. However, it often occurs that proteins are improperly folded (misfolded) and form aggregates, which are the main hallmark of many diseases including cancers, neurodegenerative diseases and many others. Proteins that assist other proteins in proper folding into three-dimensional structures are chaperones and co-chaperones. The key role of chaperones/co-chaperones is to prevent protein aggregation, especially under stress. An imbalance between chaperone/co-chaperone levels has been documented in neurons, and suggested to contribute to protein misfolding. An essential protein and a major regulator of protein folding in all eukaryotic cells is the heat shock protein 90 (Hsp90). The function of Hsp90 is tightly regulated by many factors, including co-chaperones. In this review we summarize results regarding the role of Hsp90 and its co-chaperones in neurodegenerative disorders such as Alzheimer’s disease (AD), Parkinson’s disease (PD), Huntington’s disease (HD), and prionopathies. View Full-Text
Keywords: Hsp90; co-chaperones; Alzheimer’s disease; Parkinson’s disease; Huntington’s disease; prionopathy; Hsp90 inhibitors Hsp90; co-chaperones; Alzheimer’s disease; Parkinson’s disease; Huntington’s disease; prionopathy; Hsp90 inhibitors
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MDPI and ACS Style

Bohush, A.; Bieganowski, P.; Filipek, A. Hsp90 and Its Co-Chaperones in Neurodegenerative Diseases. Int. J. Mol. Sci. 2019, 20, 4976.

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