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Small heat shock protein 22 kDa can modulate the aggregation and liquid–liquid phase separation behavior of tau
Authors:April L Darling  Jan Dahrendorff  Stefan G Creodore  Chad A Dickey  Laura J Blair  Vladimir N Uversky
Institution:1. Department of Molecular Medicine, College of Medicine, Byrd Alzheimer''s Institute, University of South Florida, Tampa Florida, USA ; 2. Protein Research Group, Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino Russia
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.
Keywords:Alzheimer''s disease  Hsp22  liquid–  liquid phase separation  small heat shock proteins  tau
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