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. 2020 Mar 4;10:4023. doi: 10.1038/s41598-020-60773-1

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Proposed mechanism for HSF1-mediated clearance of Tau. In normal conditions HSF1 is present as an inactive monomer in cytosol. HSF1 in inactive state forms complex with Hsp70. Triggering of Tau-induced stress or treatment of cells with limonoids leads to dissociation of Hsp70 from HSF1. HSF1 monomer is now subjected to phosphorylation and is transported into nucleus. In nucleus, HSF1 trimerizes and interacts with heat shock element (HSE) present in the upstream of Hsp70 promoter. This leads to increase in expression of Hsp70 and thus enhancing the cytosolic levels of Hsp70.