Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation

The Hsp90 chaperone cycle is influenced by multiple phosphorylation events but their regulatory functions are poorly understood. Here, the authors show that phosphorylation and unfolding of cochaperone Cdc37 tailors the Hsp90 chaperone cycle by recruiting kinases that promote distinct phosphorylatio...

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Autores principales:	Ashleigh B. Bachman, Dimitra Keramisanou, Wanping Xu, Kristin Beebe, Michael A. Moses, M. V. Vasantha Kumar, Geoffrey Gray, Radwan Ebna Noor, Arjan van der Vaart, Len Neckers, Ioannis Gelis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1ad30120ac2049d29abb8f3ab36b01ec
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spelling	oai:doaj.org-article:1ad30120ac2049d29abb8f3ab36b01ec2021-12-02T16:49:55ZPhosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation10.1038/s41467-017-02711-w2041-1723https://doaj.org/article/1ad30120ac2049d29abb8f3ab36b01ec2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02711-whttps://doaj.org/toc/2041-1723The Hsp90 chaperone cycle is influenced by multiple phosphorylation events but their regulatory functions are poorly understood. Here, the authors show that phosphorylation and unfolding of cochaperone Cdc37 tailors the Hsp90 chaperone cycle by recruiting kinases that promote distinct phosphorylation patterns.Ashleigh B. BachmanDimitra KeramisanouWanping XuKristin BeebeMichael A. MosesM. V. Vasantha KumarGeoffrey GrayRadwan Ebna NoorArjan van der VaartLen NeckersIoannis GelisNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ashleigh B. Bachman Dimitra Keramisanou Wanping Xu Kristin Beebe Michael A. Moses M. V. Vasantha Kumar Geoffrey Gray Radwan Ebna Noor Arjan van der Vaart Len Neckers Ioannis Gelis Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
description	The Hsp90 chaperone cycle is influenced by multiple phosphorylation events but their regulatory functions are poorly understood. Here, the authors show that phosphorylation and unfolding of cochaperone Cdc37 tailors the Hsp90 chaperone cycle by recruiting kinases that promote distinct phosphorylation patterns.
format	article
author	Ashleigh B. Bachman Dimitra Keramisanou Wanping Xu Kristin Beebe Michael A. Moses M. V. Vasantha Kumar Geoffrey Gray Radwan Ebna Noor Arjan van der Vaart Len Neckers Ioannis Gelis
author_facet	Ashleigh B. Bachman Dimitra Keramisanou Wanping Xu Kristin Beebe Michael A. Moses M. V. Vasantha Kumar Geoffrey Gray Radwan Ebna Noor Arjan van der Vaart Len Neckers Ioannis Gelis
author_sort	Ashleigh B. Bachman
title	Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
title_short	Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
title_full	Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
title_fullStr	Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
title_full_unstemmed	Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
title_sort	phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific hsp90 phosphorylation
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/1ad30120ac2049d29abb8f3ab36b01ec
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Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation

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