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ProteomicsPost-translational Regulation of FNIP1: a Rheostat for the Molecular Chaperone Hsp90
The molecular chaperone Hsp90 stabilizes and activates client proteins. Co-chaperones and post-translational modifications tightly regulate Hsp90 function and consequently lead to activation of clients. However, it is unclear whether this process occurs abruptly or gradually in the cellular context....
ORGANISM(S): Homo sapiens (Human) 
2019-01-31 | PXD012229 | Pride
Heat shock protein-90 (hsp90) Folliculin-interacting protein-1 O-glcnacylation Co-chaperone Fnip1 Pp5 Serine/threonine protein phosphatase-5 
Proteomicsc-Abl Dependent Tyrosine Phosphorylation of theCo-chaperone Aha1 Regulates Interaction with Hsp90
The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity tailoring the chaperone function to specific “client” proteins. The intracellular signaling mechanisms directly regulating Aha1 association wi...
ORGANISM(S): Homo sapiens (Human) 
2015-08-06 | PXD001737 | Pride
Molecular chaperone Q-exactive C-abl 18o labeling Aha1 Co-chaperone Heat shock protein 90 Quantative proteomics 
Proteomicsc-Abl Dependent Tyrosine Phosphorylation of theCo-chaperone Aha1 Regulates Interaction with Hsp90
The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity tailoring the chaperone function to specific “client” proteins. The intracellular signaling mechanisms directly regulating Aha1 association wi...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080713 | MassIVE
ProteomicsDeciphering PTM Crosstalk on Hsp90: Integrating Deep Learning for Drug Sensitivity Prediction
Post-translational modification (PTM) of proteins regulates cellular proteostasis by expanding protein functional diversity. This naturally leads to increased proteome complexity as the result of PTM crosstalk. Here, we used a heavily modified molecular chaperone, Heat shock protein-90 (Hsp90), to i...
ORGANISM(S): Homo sapiens (Human) 
2025-09-08 | PXD061927 | Pride
Hsp90 Ai Ganetespib Deep learning Hdac Acetylation Phosphorylation 
ProteomicsA specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand
Heat shock protein-90 chaperone machinery is involved in the stability and activity of its client proteins. The chaperone function of Hsp90 is regulated by co-chaperones and post-translational modifications. Although structural evidence exists for Hsp90 interaction with clients, our understanding of...
ORGANISM(S): Homo sapiens (Human) 
2023-05-30 | PXD030486 | Pride
Hsp90 Co-chaperone Chaperone Glucocorticoid receptor Tsc1 Fnip1 Fnip2 Steroid hormone receptors 
ProteomicsSUMOylation of Protein Phosphatase 5 Regulates Phosphatase Activity and Substrate Release
The serine/threonine protein phosphatase 5 (PP5) regulates hormone and stress-induced signaling networks. PP5 has been suggested to exist largely in a ‘closed’ and autoinhibitory state whereas the ‘open’ conformation is required for activity. Additionally, PP5 is subject to post-translational modifi...
ORGANISM(S): Homo sapiens (Human) 
2023-09-08 | PXD038701 | Pride
Chaperone Ulk1 Chaperone code Hsp90 Atg1 Autophagy Phosphorylation 
ProteomicsActivation of autophagy depends on Atg1/ULK1 mediated phosphorylation of the chaperone Hsp90
The molecular chaperone Hsp90 is involved in the stability and activity of its client proteins which largely comprise of kinases. Phosphorylation of Hsp90 by these kinase clients provides a reciprocal regulatory mechanism between these proteins, however the mechanism of regulating the cellular pathw...
ORGANISM(S): Homo sapiens (Human) 
2023-09-08 | PXD038924 | Pride
Heat shock protein-90 (hsp90) Co-chaperone Serine/threonine protein phosphatase-5 (pp5) Sumoylation Molecular chaperone Phosphorylation 
ProteomicsMps1 Phosphorylation of the Molecular Chaperone Hsp90 Regulates Mitotic Checkpoint
SUMMARY Mps1 protein kinase is required for accurate chromosome segregation during the mitotic checkpoint. The molecular chaperone Heat Shock Protein 90 (Hsp90) has been linked to Mps1 activity, however the molecular mechanismsunderlying this regulatory process remain elusive. We report that Mps1 d...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-01-27 | PXD001969 | Pride
Mitotic checkpoint Molecular chaperones Heat shock protein 90 Mps1 Phosphatase Kinase Phosphorylation Cdc14 
UnknownSUMOylation of Protein Phosphatase 5 Regulates Phosphatase Activity and Substrate Release
Not available
S-SCDT-10_1038-S44319-024-00250-2 | biostudies-other
TranscriptomicsWee1 Inhibition sensitizes prostate cancer cells to Hsp90 inhibitor to activate the intrinsic apoptotic pathway
Heat shock protein 90 (Hsp90) is an essential evolutionarily conserved molecular chaperone in eukaryotes. Cancer cells rely on Hsp90 to chaperone activated oncoproteins, and its involvement in numerous signaling pathways makes it an attractive target for drug development. Surprisingly, however, the ...
ORGANISM(S): Homo sapiens 
2013-01-10 | E-GEOD-38972 | biostudies-arrayexpress
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