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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