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ProteomicsEffects of a phosphomimetic mutation and nucleotide binding on the interaction of Hsp90a with co-chaperone Aha1 analyzed by chemical cross-linking with mass spectrometry
Complex conformational dynamics are essential for the chaperone function of heat shock protein 90 (Hsp90), including transient, ATP-biased N-domain dimerization establishing ATPase competence. Biochemical data demonstrate that the intrinsic, but weak, ATP hydrolyzing activity of Hsp90 is markedly en...
ORGANISM(S): Homo sapiens (Human) 
2019-06-17 | PXD013476 | Pride
Cross-linking Aha1 Ptm Heat shock Phosphorylation Xl-ms Chaperone Hsp90 
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
ProteomicsProximity Proteomics Revealed Dicer1 and Transporters as Client Proteins of Aha1
Co-chaperone Aha1 activates HSP90 ATPase to promote the folding of client proteins. However, the client proteins of Aha1 are largely unknown. By employing ascorbate peroxidase (APEX) based proximity labeling, we identified 32 proximity proteins of HSP90 that are modulated by genetic depletion of Aha...
ORGANISM(S): Pan troglodytes (Chimpanzee) Homo sapiens (Human) 
2022-11-19 | PXD028980 | Pride
Hsp90 Dicer1 Apex Proximity labeling Aha1 
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 
ProteomicsAcetylome reveals the lysine acetylation modifications on outer membrane protein Aha1 in Aeromonas hydrophila regulate the porin permeability to multidrug antibiotics
Acetylome reveals the lysine acetylation modifications on outer membrane protein Aha1 in Aeromonas hydrophila regulate the porin permeability to multidrug antibiotics
ORGANISM(S): Aeromonas Hydrophila Subsp. Hydrophila Atcc 7966 
PXD028447 |
UnknownAha1 Is an Autonomous Chaperone for SULT1A1.
Not available
S-EPMC9378526 | biostudies-literature
UnknownA chemical compound inhibiting the Aha1-Hsp90 chaperone complex.
Not available
S-EPMC5641884 | biostudies-literature
UnknownDynamic Aha1 co-chaperone binding to human Hsp90.
Not available
S-EPMC6699087 | biostudies-literature
UnknownAha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity.
Not available
S-EPMC8037086 | biostudies-literature
UnknownHSP90 and Aha1 modulate microRNA maturation through promoting the folding of Dicer1.
Not available
S-EPMC9262616 | biostudies-literature
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