p(HGNC:AHSA1)
Since Aha1 levels are repressed in aging, but are abnormally preserved in AD, tau aggregation could be accelerated in part by Aha1 in the AD brain. PubMed:29311797
For instance, CyP40, FKBP52, PP5, Hop, p23, and Aha1 are all repressed in the aged brain. PubMed:29311797
Aha1 levels have been shown to increase with AD. PubMed:29311797
Previous studies have also implicated Aha1 for a role in cystic fibrosis. PubMed:29311797
As in the case of Hsp70, cochaperones of Hsp90, such as Aha1, cdc37 and TPR domain-containing proteins, regulate its ATPase activity and control its conformational transitions (reviewed in [84]). PubMed:21882945
In addition, Hsp90’s hydrolysis of ATP, which is stimulated by Aha1, facilitates polypeptide release [82,106] and transfer to CHIP or other E3 ligases [107,108] PubMed:21882945
In addition, Hsp90’s hydrolysis of ATP, which is stimulated by Aha1, facilitates polypeptide release [82,106] and transfer to CHIP or other E3 ligases [107,108] PubMed:21882945
The activator of Hsp90 ATPase homolog 1 (Aha1) works as a co- chaperone to stimulate the ATPase function of Hsp90 to regulate the folding and activation of client proteins. PubMed:29311797
Aha1 levels have been shown to increase with AD. PubMed:29311797
In the same study, we found that high levels of Aha1 in a tau transgenic mouse model increased tau oligomers as well as neuronal loss concomitant with cognitive deficits (Shelton et al., 2017). PubMed:29311797
In the same study, we found that high levels of Aha1 in a tau transgenic mouse model increased tau oligomers as well as neuronal loss concomitant with cognitive deficits (Shelton et al., 2017). PubMed:29311797
Since Aha1 levels are repressed in aging, but are abnormally preserved in AD, tau aggregation could be accelerated in part by Aha1 in the AD brain. PubMed:29311797
Previous studies have also implicated Aha1 for a role in cystic fibrosis. PubMed:29311797
The activator of Hsp90 ATPase (Aha1) binds asymmetrically to the Hsp90 middle domain, stimulating ATP hydrolysis and inducing transition to the closed state (180, 181, 185, 190). PubMed:23746257
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.