The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding

Hsp90 is required for the folding, stability and activity of several drivers of oncogenesis. Here the authors show that Folliculin-interacting proteins (FNIP) 1 and 2, whose expression correlates with the cellular response to Hsp90 inhibitors, are co-chaperones of Hsp90 that function by inhibiting i...

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Autores principales:	Mark R. Woodford, Diana M. Dunn, Adam R. Blanden, Dante Capriotti, David Loiselle, Chrisostomos Prodromou, Barry Panaretou, Philip F. Hughes, Aaron Smith, Wendi Ackerman, Timothy A. Haystead, Stewart N. Loh, Dimitra Bourboulia, Laura S. Schmidt, W. Marston Linehan, Gennady Bratslavsky, Mehdi Mollapour
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/51f03ab61e4442f99c334fc8fe1d2ccd
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spelling	oai:doaj.org-article:51f03ab61e4442f99c334fc8fe1d2ccd2021-12-02T15:34:10ZThe FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding10.1038/ncomms120372041-1723https://doaj.org/article/51f03ab61e4442f99c334fc8fe1d2ccd2016-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms12037https://doaj.org/toc/2041-1723Hsp90 is required for the folding, stability and activity of several drivers of oncogenesis. Here the authors show that Folliculin-interacting proteins (FNIP) 1 and 2, whose expression correlates with the cellular response to Hsp90 inhibitors, are co-chaperones of Hsp90 that function by inhibiting its ATPase activity.Mark R. WoodfordDiana M. DunnAdam R. BlandenDante CapriottiDavid LoiselleChrisostomos ProdromouBarry PanaretouPhilip F. HughesAaron SmithWendi AckermanTimothy A. HaysteadStewart N. LohDimitra BourbouliaLaura S. SchmidtW. Marston LinehanGennady BratslavskyMehdi MollapourNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-15 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Mark R. Woodford Diana M. Dunn Adam R. Blanden Dante Capriotti David Loiselle Chrisostomos Prodromou Barry Panaretou Philip F. Hughes Aaron Smith Wendi Ackerman Timothy A. Haystead Stewart N. Loh Dimitra Bourboulia Laura S. Schmidt W. Marston Linehan Gennady Bratslavsky Mehdi Mollapour The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
description	Hsp90 is required for the folding, stability and activity of several drivers of oncogenesis. Here the authors show that Folliculin-interacting proteins (FNIP) 1 and 2, whose expression correlates with the cellular response to Hsp90 inhibitors, are co-chaperones of Hsp90 that function by inhibiting its ATPase activity.
format	article
author	Mark R. Woodford Diana M. Dunn Adam R. Blanden Dante Capriotti David Loiselle Chrisostomos Prodromou Barry Panaretou Philip F. Hughes Aaron Smith Wendi Ackerman Timothy A. Haystead Stewart N. Loh Dimitra Bourboulia Laura S. Schmidt W. Marston Linehan Gennady Bratslavsky Mehdi Mollapour
author_facet	Mark R. Woodford Diana M. Dunn Adam R. Blanden Dante Capriotti David Loiselle Chrisostomos Prodromou Barry Panaretou Philip F. Hughes Aaron Smith Wendi Ackerman Timothy A. Haystead Stewart N. Loh Dimitra Bourboulia Laura S. Schmidt W. Marston Linehan Gennady Bratslavsky Mehdi Mollapour
author_sort	Mark R. Woodford
title	The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
title_short	The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
title_full	The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
title_fullStr	The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
title_full_unstemmed	The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
title_sort	fnip co-chaperones decelerate the hsp90 chaperone cycle and enhance drug binding
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/51f03ab61e4442f99c334fc8fe1d2ccd
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The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding

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