ArticleThe Journal of biological chemistry2019
Heat shock protein 104 (HSP104) chaperones soluble Tau via a mechanism distinct from its disaggregase activity.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Chaperone-mediated heterotypic phase separation regulates liquid-to-solid phase transitions of tau into amyloid fibrils.Science advances · 2025Article
- Mapping Hsp104 interactions using cross-linking mass spectrometry.FEBS open bio · 2025Article
- Updates in Alzheimer's disease: from basic research to diagnosis and therapies.Translational neurodegeneration · 2024Review
- Oligomeric State and Holding Activity of Hsp60.International journal of molecular sciences · 2023Article
- Wine Yeast Cells Acquire Resistance to Severe Ethanol Stress and Suppress Insoluble Protein Accumulation during Alcoholic Fermentation.Microbiology spectrum · 2022Article
- From Small Peptides to Large Proteins against Alzheimer'sDisease.Biomolecules · 2022Review
- Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation.The FEBS journal · 2022Article
- Molecular mechanisms of amyloid disaggregation.Journal of advanced research · 2022Review
- Critical Molecular and Cellular Contributors to Tau Pathology.Biomedicines · 2021Review
- The unhappy chaperone.QRB discovery · 2021Article
- Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit.Open biology · 2020Article
- The ABCF gene family facilitates disaggregation during animal development.Molecular biology of the cell · 2020Review
- Structural basis of the interplay between α-synuclein and Tau in regulating pathological amyloid aggregation.The Journal of biological chemistry · 2020Article
- Different Heat Shock Proteins Bind α-Synuclein With Distinct Mechanisms and Synergistically Prevent Its Amyloid Aggregation.Frontiers in neuroscience · 2019Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock protein 104 (HSP104) is a conserved AAA+ protein disaggregase, can disassemble the toxic aggregates formed by different amyloid proteins, and is protective in various animal models associated with amyloid-related diseases. Extensive studies have attempted to elucidate how HSP104 disassembles the aggregated form of clients. Here, we found that HSP104 exhibits a potent holdase activity that does not require energy, prevents the soluble form of amyloid clients from aggregating, and differs from HSP104's disaggregase activity. Using cryo-EM, NMR, and additional biophysical approaches, we found that HSP104 utilizes its small subdomain of nucleotide-binding domain 2 (ssNBD2) to capture the soluble amyloid client (K19 of Tau) independent of its ATP hydrolysis activity. Our results indicate that HSP104 utilizes two fundamental distinct mechanisms to chaperone different forms of amyloid client and highlight the important yet previously unappreciated function of ssNBD2 in chaperoning amyloid client and thereby preventing pathological aggregation.
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