Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

The chaperone Hsp90 plays a key role in maintaining cellular homeostasis. Here the authors provide structural insights into substrate recognition and the pro-folding mechanism of Hsp90/co-chaperone complexes by studying the complex of Hsp90 with its co-chaperone FKBP51 and the substrate Tau bound Hs...

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Main Authors:	Javier Oroz, Bliss J. Chang, Piotr Wysoczanski, Chung-Tien Lee, Ángel Pérez-Lara, Pijush Chakraborty, Romina V. Hofele, Jeremy D. Baker, Laura J. Blair, Jacek Biernat, Henning Urlaub, Eckhard Mandelkow, Chad A. Dickey, Markus Zweckstetter
Format:	Article
Language:	English
Published:	Nature Publishing Group 2018-10-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-018-06880-0

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spelling	doaj-3a370245b8a44bedbc69cc4763edff902021-05-11T09:40:49ZengNature Publishing GroupNature Communications2041-17232018-10-019111310.1038/s41467-018-06880-0Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complexJavier Oroz0Bliss J. Chang1Piotr Wysoczanski2Chung-Tien Lee3Ángel Pérez-Lara4Pijush Chakraborty5Romina V. Hofele6Jeremy D. Baker7Laura J. Blair8Jacek Biernat9Henning Urlaub10Eckhard Mandelkow11Chad A. Dickey12Markus Zweckstetter13German Center for Neurodegenerative Diseases (DZNE)Department for NMR-based Structural Biology, Max Planck Institute for Biophysical ChemistryGerman Center for Neurodegenerative Diseases (DZNE)Bioanalytical Mass Spectrometry, Max Planck Institute for Biophysical ChemistryDepartment of Neurobiology, Max Planck Institute for Biophysical ChemistryGerman Center for Neurodegenerative Diseases (DZNE)Bioanalytical Mass Spectrometry, Max Planck Institute for Biophysical ChemistryDepartment of Molecular Medicine, Morsani College of Medicine, USF Health Byrd Alzheimer’s Institute, University of South FloridaDepartment of Molecular Medicine, Morsani College of Medicine, USF Health Byrd Alzheimer’s Institute, University of South FloridaDZNE, CAESAR Research CenterBioanalytical Mass Spectrometry, Max Planck Institute for Biophysical ChemistryDZNE, CAESAR Research CenterDepartment of Molecular Medicine, Morsani College of Medicine, USF Health Byrd Alzheimer’s Institute, University of South FloridaGerman Center for Neurodegenerative Diseases (DZNE)The chaperone Hsp90 plays a key role in maintaining cellular homeostasis. Here the authors provide structural insights into substrate recognition and the pro-folding mechanism of Hsp90/co-chaperone complexes by studying the complex of Hsp90 with its co-chaperone FKBP51 and the substrate Tau bound Hsp90/FKBP51 ternary complex using a NMR based integrative approach.https://doi.org/10.1038/s41467-018-06880-0
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Javier Oroz Bliss J. Chang Piotr Wysoczanski Chung-Tien Lee Ángel Pérez-Lara Pijush Chakraborty Romina V. Hofele Jeremy D. Baker Laura J. Blair Jacek Biernat Henning Urlaub Eckhard Mandelkow Chad A. Dickey Markus Zweckstetter
spellingShingle	Javier Oroz Bliss J. Chang Piotr Wysoczanski Chung-Tien Lee Ángel Pérez-Lara Pijush Chakraborty Romina V. Hofele Jeremy D. Baker Laura J. Blair Jacek Biernat Henning Urlaub Eckhard Mandelkow Chad A. Dickey Markus Zweckstetter Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex Nature Communications
author_facet	Javier Oroz Bliss J. Chang Piotr Wysoczanski Chung-Tien Lee Ángel Pérez-Lara Pijush Chakraborty Romina V. Hofele Jeremy D. Baker Laura J. Blair Jacek Biernat Henning Urlaub Eckhard Mandelkow Chad A. Dickey Markus Zweckstetter
author_sort	Javier Oroz
title	Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
title_short	Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
title_full	Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
title_fullStr	Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
title_full_unstemmed	Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
title_sort	structure and pro-toxic mechanism of the human hsp90/ppiase/tau complex
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-10-01
description	The chaperone Hsp90 plays a key role in maintaining cellular homeostasis. Here the authors provide structural insights into substrate recognition and the pro-folding mechanism of Hsp90/co-chaperone complexes by studying the complex of Hsp90 with its co-chaperone FKBP51 and the substrate Tau bound Hsp90/FKBP51 ternary complex using a NMR based integrative approach.
url	https://doi.org/10.1038/s41467-018-06880-0
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Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

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