The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.
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ABSTRACT:
SUBMITTER: Woodford MR
PROVIDER: S-EPMC4931344 | biostudies-literature | 2016 Jun
REPOSITORIES: biostudies-literature
Publications
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.
Woodford Mark R MR Dunn Diana M DM Blanden Adam R AR Capriotti Dante D Loiselle David D Prodromou Chrisostomos C Panaretou Barry B Hughes Philip F PF Smith Aaron A Ackerman Wendi W Haystead Timothy A TA Loh Stewart N SN Bourboulia Dimitra D Schmidt Laura S LS Marston Linehan W W Bratslavsky Gennady G Mollapour Mehdi M
Nature communications 20160629
Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved in maintaining the stability and activity of numerous signalling proteins, also known as clients. Hsp90 ATPase activity is essential for its chaperone function and it is regulated by co-chaperones. Here we show that the tumour suppressor FLCN is an Hsp90 client protein and its binding partners FNIP1/FNIP2 function as co-chaperones. FNIPs decelerate the chaperone cycle, facilitating FLCN interaction with Hsp9 ...[more]
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