期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 20, 期 20, 页码 -出版社
MDPI
DOI: 10.3390/ijms20204976
关键词
Hsp90; co-chaperones; Alzheimer's disease; Parkinson's disease; Huntington's disease; prionopathy; Hsp90 inhibitors
资金
- European Union [665735]
- Polish Ministry of Science and Higher Education [3548/H2020/COFUND/2016/2]
- NCN [2018/29/B/NZ4/01384, 2016/23/B/NZ6/02536]
- Nencki Institute of Experimental Biology PAS
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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