The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model

Variants of the extracellular chaperone Clusterin are associated with Alzheimer’s disease (AD) and Clusterin levels are elevated in AD patient brains. Here, the authors show that Clusterin binds to oligomeric Tau, which enhances the seeding capacity of Tau aggregates upon cellular uptake. They also...

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Autores principales:	Patricia Yuste-Checa, Victoria A. Trinkaus, Irene Riera-Tur, Rahmi Imamoglu, Theresa F. Schaller, Huping Wang, Irina Dudanova, Mark S. Hipp, Andreas Bracher, F. Ulrich Hartl
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6817e37ab6504c1fa561f4ad2a667e95
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spelling	oai:doaj.org-article:6817e37ab6504c1fa561f4ad2a667e952021-12-02T18:50:57ZThe extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model10.1038/s41467-021-25060-12041-1723https://doaj.org/article/6817e37ab6504c1fa561f4ad2a667e952021-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25060-1https://doaj.org/toc/2041-1723Variants of the extracellular chaperone Clusterin are associated with Alzheimer’s disease (AD) and Clusterin levels are elevated in AD patient brains. Here, the authors show that Clusterin binds to oligomeric Tau, which enhances the seeding capacity of Tau aggregates upon cellular uptake. They also demonstrate that Tau/Clusterin complexes enter cells via the endosomal pathway, resulting in damage to endolysosomes and entry into the cytosol, where they induce the aggregation of endogenous, soluble Tau.Patricia Yuste-ChecaVictoria A. TrinkausIrene Riera-TurRahmi ImamogluTheresa F. SchallerHuping WangIrina DudanovaMark S. HippAndreas BracherF. Ulrich HartlNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Patricia Yuste-Checa Victoria A. Trinkaus Irene Riera-Tur Rahmi Imamoglu Theresa F. Schaller Huping Wang Irina Dudanova Mark S. Hipp Andreas Bracher F. Ulrich Hartl The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model
description	Variants of the extracellular chaperone Clusterin are associated with Alzheimer’s disease (AD) and Clusterin levels are elevated in AD patient brains. Here, the authors show that Clusterin binds to oligomeric Tau, which enhances the seeding capacity of Tau aggregates upon cellular uptake. They also demonstrate that Tau/Clusterin complexes enter cells via the endosomal pathway, resulting in damage to endolysosomes and entry into the cytosol, where they induce the aggregation of endogenous, soluble Tau.
format	article
author	Patricia Yuste-Checa Victoria A. Trinkaus Irene Riera-Tur Rahmi Imamoglu Theresa F. Schaller Huping Wang Irina Dudanova Mark S. Hipp Andreas Bracher F. Ulrich Hartl
author_facet	Patricia Yuste-Checa Victoria A. Trinkaus Irene Riera-Tur Rahmi Imamoglu Theresa F. Schaller Huping Wang Irina Dudanova Mark S. Hipp Andreas Bracher F. Ulrich Hartl
author_sort	Patricia Yuste-Checa
title	The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model
title_short	The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model
title_full	The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model
title_fullStr	The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model
title_full_unstemmed	The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model
title_sort	extracellular chaperone clusterin enhances tau aggregate seeding in a cellular model
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/6817e37ab6504c1fa561f4ad2a667e95
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The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model

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