HSP-90/kinase complexes are stabilized by the large PPIase FKB-6

Abstract Protein kinases are important regulators in cellular signal transduction. As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation. Depending on client type, Hsp90 interacts with dif...

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Autores principales:	Siyuan Sima, Katalin Barkovits, Katrin Marcus, Lukas Schmauder, Stephan M. Hacker, Nils Hellwig, Nina Morgner, Klaus Richter
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f6aca38767d14b3994c3215e5e2f658e
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id	oai:doaj.org-article:f6aca38767d14b3994c3215e5e2f658e
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spelling	oai:doaj.org-article:f6aca38767d14b3994c3215e5e2f658e2021-12-02T17:47:23ZHSP-90/kinase complexes are stabilized by the large PPIase FKB-610.1038/s41598-021-91667-52045-2322https://doaj.org/article/f6aca38767d14b3994c3215e5e2f658e2021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-91667-5https://doaj.org/toc/2045-2322Abstract Protein kinases are important regulators in cellular signal transduction. As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation. Depending on client type, Hsp90 interacts with different cofactors. Here we report that besides the kinase-specific cofactor Cdc37 large PPIases of the Fkbp-type strongly bind to kinase•Hsp90•Cdc37 complexes. We evaluate the nucleotide regulation of these assemblies and identify prominent interaction sites in this quaternary complex. The synergistic interaction between the participating proteins and the conserved nature of the interaction suggests functions of the large PPIases Fkbp51/Fkbp52 and their nematode homolog FKB-6 as contributing factors to the kinase cycle of the Hsp90 machinery.Siyuan SimaKatalin BarkovitsKatrin MarcusLukas SchmauderStephan M. HackerNils HellwigNina MorgnerKlaus RichterNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Siyuan Sima Katalin Barkovits Katrin Marcus Lukas Schmauder Stephan M. Hacker Nils Hellwig Nina Morgner Klaus Richter HSP-90/kinase complexes are stabilized by the large PPIase FKB-6
description	Abstract Protein kinases are important regulators in cellular signal transduction. As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation. Depending on client type, Hsp90 interacts with different cofactors. Here we report that besides the kinase-specific cofactor Cdc37 large PPIases of the Fkbp-type strongly bind to kinase•Hsp90•Cdc37 complexes. We evaluate the nucleotide regulation of these assemblies and identify prominent interaction sites in this quaternary complex. The synergistic interaction between the participating proteins and the conserved nature of the interaction suggests functions of the large PPIases Fkbp51/Fkbp52 and their nematode homolog FKB-6 as contributing factors to the kinase cycle of the Hsp90 machinery.
format	article
author	Siyuan Sima Katalin Barkovits Katrin Marcus Lukas Schmauder Stephan M. Hacker Nils Hellwig Nina Morgner Klaus Richter
author_facet	Siyuan Sima Katalin Barkovits Katrin Marcus Lukas Schmauder Stephan M. Hacker Nils Hellwig Nina Morgner Klaus Richter
author_sort	Siyuan Sima
title	HSP-90/kinase complexes are stabilized by the large PPIase FKB-6
title_short	HSP-90/kinase complexes are stabilized by the large PPIase FKB-6
title_full	HSP-90/kinase complexes are stabilized by the large PPIase FKB-6
title_fullStr	HSP-90/kinase complexes are stabilized by the large PPIase FKB-6
title_full_unstemmed	HSP-90/kinase complexes are stabilized by the large PPIase FKB-6
title_sort	hsp-90/kinase complexes are stabilized by the large ppiase fkb-6
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f6aca38767d14b3994c3215e5e2f658e
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HSP-90/kinase complexes are stabilized by the large PPIase FKB-6

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