Nature Communications (Jun 2016)
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
- 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
Affiliations
- Mark R. Woodford
- Department of Urology, SUNY Upstate Medical University
- Diana M. Dunn
- Department of Urology, SUNY Upstate Medical University
- Adam R. Blanden
- Cancer Research Institute, SUNY Upstate Medical University
- Dante Capriotti
- Department of Urology, SUNY Upstate Medical University
- David Loiselle
- Department of Pharmacology and Cancer Biology, Duke University Medical Center
- Chrisostomos Prodromou
- Genome Damage and Stability Centre, University of Sussex
- Barry Panaretou
- Institute of Pharmaceutical Science, King’s College London
- Philip F. Hughes
- Department of Pharmacology and Cancer Biology, Duke University Medical Center
- Aaron Smith
- Department of Pharmacology and Cancer Biology, Duke University Medical Center
- Wendi Ackerman
- Health Sciences Library, SUNY Upstate Medical University
- Timothy A. Haystead
- Department of Pharmacology and Cancer Biology, Duke University Medical Center
- Stewart N. Loh
- Cancer Research Institute, SUNY Upstate Medical University
- Dimitra Bourboulia
- Department of Urology, SUNY Upstate Medical University
- Laura S. Schmidt
- Basic Science Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research
- W. Marston Linehan
- Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute
- Gennady Bratslavsky
- Department of Urology, SUNY Upstate Medical University
- Mehdi Mollapour
- Department of Urology, SUNY Upstate Medical University
- DOI
- https://doi.org/10.1038/ncomms12037
- Journal volume & issue
-
Vol. 7,
no. 1
pp. 1 – 15
Abstract
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.
