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Small heat shock protein 22 kDa can modulate the aggregation and liquid-liquid phase separation behavior of tau.

ABSTRACT: Alzheimer's disease is a progressive fatal neurodegenerative disease with no cure or effective treatments. The hallmarks of disease include extracellular plaques and intracellular tangles of aggregated protein. The intracellular tangles consist of the microtubule associated protein tau. Preventing the pathological aggregation of tau may be an important therapeutic approach to treat disease. In this study we show that small heat shock protein 22 kDa (Hsp22) can prevent the aggregation of tau in vitro. Additionally, tau can undergo liquid-liquid phase separation (LLPS) in the presence of crowding reagents which causes it to have an increased aggregation rate. We show that Hsp22 can modulate both the aggregation and LLPS behavior of tau in vitro.

SUBMITTER: Darling AL

PROVIDER: S-EPMC8197419 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature

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Small heat shock protein 22 kDa can modulate the aggregation and liquid-liquid phase separation behavior of tau.

Darling April L AL Dahrendorff Jan J Creodore Stefan G SG Dickey Chad A CA Blair Laura J LJ Uversky Vladimir N VN

Protein science : a publication of the Protein Society 20210315 7

Alzheimer's disease is a progressive fatal neurodegenerative disease with no cure or effective treatments. The hallmarks of disease include extracellular plaques and intracellular tangles of aggregated protein. The intracellular tangles consist of the microtubule associated protein tau. Preventing the pathological aggregation of tau may be an important therapeutic approach to treat disease. In this study we show that small heat shock protein 22 kDa (Hsp22) can prevent the aggregation of tau in v ...[more]

PMID: 33686711

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