Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1

Phosphorylation of Tyr313 in Hsp90 enhances the binding to its activator Aha1, but the underlying mechanism is unknown. Here, the authors study the structural consequences of Tyr313 phosphorylation, showing that it serves as a conformational switch in Hsp90 that enables Aha1 recruitment.

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Autores principales:	Wanping Xu, Kristin Beebe, Juan D. Chavez, Marta Boysen, YinYing Lu, Abbey D. Zuehlke, Dimitra Keramisanou, Jane B. Trepel, Christosomos Prodromou, Matthias P. Mayer, James E. Bruce, Ioannis Gelis, Len Neckers
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c98ae81e4f7740939a33040bfaf94c2e
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spelling	oai:doaj.org-article:c98ae81e4f7740939a33040bfaf94c2e2021-12-02T15:35:27ZHsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha110.1038/s41467-019-10463-y2041-1723https://doaj.org/article/c98ae81e4f7740939a33040bfaf94c2e2019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10463-yhttps://doaj.org/toc/2041-1723Phosphorylation of Tyr313 in Hsp90 enhances the binding to its activator Aha1, but the underlying mechanism is unknown. Here, the authors study the structural consequences of Tyr313 phosphorylation, showing that it serves as a conformational switch in Hsp90 that enables Aha1 recruitment.Wanping XuKristin BeebeJuan D. ChavezMarta BoysenYinYing LuAbbey D. ZuehlkeDimitra KeramisanouJane B. TrepelChristosomos ProdromouMatthias P. MayerJames E. BruceIoannis GelisLen NeckersNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Wanping Xu Kristin Beebe Juan D. Chavez Marta Boysen YinYing Lu Abbey D. Zuehlke Dimitra Keramisanou Jane B. Trepel Christosomos Prodromou Matthias P. Mayer James E. Bruce Ioannis Gelis Len Neckers Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
description	Phosphorylation of Tyr313 in Hsp90 enhances the binding to its activator Aha1, but the underlying mechanism is unknown. Here, the authors study the structural consequences of Tyr313 phosphorylation, showing that it serves as a conformational switch in Hsp90 that enables Aha1 recruitment.
format	article
author	Wanping Xu Kristin Beebe Juan D. Chavez Marta Boysen YinYing Lu Abbey D. Zuehlke Dimitra Keramisanou Jane B. Trepel Christosomos Prodromou Matthias P. Mayer James E. Bruce Ioannis Gelis Len Neckers
author_facet	Wanping Xu Kristin Beebe Juan D. Chavez Marta Boysen YinYing Lu Abbey D. Zuehlke Dimitra Keramisanou Jane B. Trepel Christosomos Prodromou Matthias P. Mayer James E. Bruce Ioannis Gelis Len Neckers
author_sort	Wanping Xu
title	Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
title_short	Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
title_full	Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
title_fullStr	Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
title_full_unstemmed	Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
title_sort	hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the atpase-stimulating cochaperone aha1
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/c98ae81e4f7740939a33040bfaf94c2e
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Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1

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