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Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1

Phosphorylation of Tyr313 in Hsp90 enhances the binding to its activator Aha1, but the underlying mechanism is unknown. Here, the authors study the structural consequences of Tyr313 phosphorylation, showing that it serves as a conformational switch in Hsp90 that enables Aha1 recruitment.

Wanping Xu
Kristin Beebe
Len Neckers
ResearchOpen Access12 Jun 2019
Nature Communications

Volume: 10, P: 1-14
An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans

The eukaryotic heat shock protein 90 (Hsp90) undergoes an ATP-dependent conformational cycle that is influenced by posttranslational modifications and co-chaperones. Here, the authors show that the yeast co-chaperone Hch1 can be functionally substituted by site-specific phosphorylation in human Hsp90.

Abbey D. Zuehlke
Michael Reidy
Len Neckers
ResearchOpen Access24 May 2017
Nature Communications

Volume: 8, P: 1-10
Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation

The Hsp90 chaperone cycle is influenced by multiple phosphorylation events but their regulatory functions are poorly understood. Here, the authors show that phosphorylation and unfolding of cochaperone Cdc37 tailors the Hsp90 chaperone cycle by recruiting kinases that promote distinct phosphorylation patterns.

Ashleigh B. Bachman
Dimitra Keramisanou
Ioannis Gelis
ResearchOpen Access17 Jan 2018
Nature Communications

Volume: 9, P: 1-14
Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90

The inhibitor PU-H71 preferentially targets tumor-enriched Hsp90 complexes. Affinity purification using PU-H71 reveals cancer-specific protein networks in chronic myeloid leukemia and that the abundance of tumor-specific Hsp90 clients in cells can predict sensitivity to Hsp90 inhibitors.

Kamalika Moulick
James H Ahn
Gabriela Chiosis
Research25 Sept 2011
Nature Chemical Biology

Volume: 7, P: 818-826
Reversible epigenetic alterations regulate class I HLA loss in prostate cancer

Loss of HLA-I gene expression in prostate cancer is associated with repressive chromatin states, which can be reversed by pharmacological DNMT and HDAC inhibition leading to increased activation of co-cultured tumor-specific CD8+ T-cells.

Tamara S. Rodems
Erika Heninger
Joshua M. Lang
ResearchOpen Access01 Sept 2022
Communications Biology

Volume: 5, P: 1-16
HSP90 inhibitors disrupt a transient HSP90-HSF1 interaction and identify a noncanonical model of HSP90-mediated HSF1 regulation

Toshiki Kijima
Thomas L. Prince
Len Neckers
ResearchOpen Access03 May 2018
Scientific Reports

Volume: 8, P: 1-13

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Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1

An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans

Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation

Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90

Reversible epigenetic alterations regulate class I HLA loss in prostate cancer

HSP90 inhibitors disrupt a transient HSP90-HSF1 interaction and identify a noncanonical model of HSP90-mediated HSF1 regulation

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