Gene interactions and pathways from curated databases and text-mining

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AHSA1 — ATP5O

Text-mined interactions from Literome

Lotz et al., J Biol Chem 2003 : Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone ... In experiments with purified proteins, Aha1 but not Hch1 stimulated the intrinsic ATPase activity of Hsp90 5-fold
Chadli et al., Mol Cell Biol 2006 : GCUNC-45 binds to the ATP binding domain of hsp90 to prevent the activation of its ATPase activity by the cochaperone Aha1
Holmes et al., Cancer Res 2008 (Neoplasms) : As AHA1 increases the ATPase activity of HSP90, we hypothesized that modulation of AHA1 expression could influence the activity of client proteins and/or the cellular response to 17-AAG
Koulov et al., Mol Biol Cell 2010 (Cystic Fibrosis) : Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis ... To elucidate the structural basis for ATPase stimulation of human Hsp90 by human Aha1 , we have developed novel mass spectrometry approaches that demonstrate that the N- and C-terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90 to modulate the ATP hydrolysis cycle and client activity in vivo
Stark et al., Proteins 2010 : Sequence and structure comparisons with proteins from eukaryotes, prokaryotes, and archaea suggest that YndB is very similar to the eukaryote protein Aha1 , which binds to the middle domain of Hsp90 and induces ATPase activity