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

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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Auteurs principaux: 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
Format: article
Langue:EN
Publié: Nature Portfolio 2016
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Science
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Accès en ligne:https://doaj.org/article/51f03ab61e4442f99c334fc8fe1d2ccd
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Résumé: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.

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