Oct 12, 2019

Hsp90 and Its Co-Chaperones in Neurodegenerative Diseases

International Journal of Molecular Sciences
Anastasiia BohushAnna Filipek


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.

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Mentioned in this Paper

Nerve Degeneration
Alzheimer's Disease
Protein Aggregation, Pathological
Parkinson Disease
Malignant Neoplasms
Huntington Disease
Protein Folding
Neurodegenerative Disorders

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